Dielectric dispersion, relaxation dynamics and thermodynamic studies of Beta-Alanine in aqueous solutions using picoseconds time domain reflectometry

Author’s Accepted Manuscript Dielectric dispersion, relaxation dynamics and thermodynamic studies of Beta-Alanine in aqueous solutions using picoseconds time domain reflectometry K. Vinoth, T. Ganesh, P. Senthilkumar, M. Maria Sylvester, D.J.S. Anand Karunakaran, Praveen Hudge, A.C. Kumbharkhane

PII: DOI: Reference:

www.elsevier.com/locate/physb

S0921-4526(17)30398-8 http://dx.doi.org/10.1016/j.physb.2017.07.009 PHYSB310076

To appear in: Physica B: Physics of Condensed Matter Received date: 1 April 2017 Revised date: 24 June 2017 Accepted date: 6 July 2017 Cite this article as: K. Vinoth, T. Ganesh, P. Senthilkumar, M. Maria Sylvester, D.J.S. Anand Karunakaran, Praveen Hudge and A.C. Kumbharkhane, Dielectric dispersion, relaxation dynamics and thermodynamic studies of Beta-Alanine in aqueous solutions using picoseconds time domain reflectometry, Physica B: Physics of Condensed Matter, http://dx.doi.org/10.1016/j.physb.2017.07.009 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting galley proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

Dielectric dispersion, relaxation dynamics and thermodynamic studies of BetaAlanine in aqueous solutions using picoseconds time domain reflectometry K.Vinotha, T.Ganesha*, P.Senthilkumarb, M.MariaSylvesterc , D.J.S.AnandKarunakaranc Praveen Hudged , A.C.Kumbharkhaned a PG & Research Department of Physics, Rajah Serfoji Government College, Bharathidasan university, Thanjavur-613 005, Tamil Nadu, INDIA b Department of Physics, Saranathan College of Engineering, Tiruchirapalli –620 012, Tamil Nadu, INDIA c PG & Research Department of Physics, Bishop Heber College, Bharathidasan university, Tiruchirapalli – 620 017, Tamil Nadu, INDIA d School of Physical Sciences, Swami Ramanad Teerth Marthwada University, Nanded – 431606, MS, INDIA * Corresponding author: PG & Research Department of Physics, Rajah Serfoji Government College, Bharathidasan university, Thanjavur-613 005, Tamil Nadu, INDIA. Mobile: +91-9003428719. [email protected]

Abstract The aqueous solution of beta-alanine characterised and studied by their dispersive dielectric properties and relaxation process in the frequency domain of 10X106Hz to 30X109Hz with varying concentration in mole fractions and temperatures. The molecular interaction and dielectric parameters are discussed in terms of counter-ion concentration theory. The static permittivity (  0 ), high frequency dielectric permittivity (   ) and excess dielectric parameters are accomplished by frequency depended physical properties and relaxation time (τ). Molecular orientation, ordering and correlation factors are reported as confirmation of intermolecular interactions. Ionic conductivity and thermo dynamical properties are concluded with the behaviour of the mixture constituents. Solute–solvent, solute–solute interaction, structure making and breaking abilities of the solute in aqueous medium are interpreted. Fourier Transform Infrared (FTIR) spectra of beta- alanine single crystal and liquid state have been studied. The 13C

1

Nuclear Magnetic Resonance (NMR) spectral studies give the signature for resonating frequencies and chemical shifts of beta-alanine. Keywords: Beta-alanine; Dielectric Relaxation; Molecular Interaction; Thermodynamic analysis; Spectral characterisation; TDR. 1. Introduction Amino acids as auxiliary segment of proteins play an important role in physiological process of a living cell. The aliphatic amino acid exhibits many of the properties of strong electrolytes when dissolved in solvent of high dielectric constant such as water or polar liquids. The peculiar behavior of amino acids concludes the acidic and basic groups of an amino acid molecule are completely ionized in certain solvents giving rise to a hybrid ion with no resultant charge by Adams et al. [1]. In solution state proteins, amino acids and each of these functional groups experiences very different interactions with other system of components. Even though the ionic charge exists, it cannot contribute to the conductivity of the solution since the hybrid ions are surrounded by a strong electrostatic field, because of the wide separation of its charged groups. Hybrid ions of this type have been represented as zwitterions. The amino acid exists on solution mainly in the zwitterionic form, where the positive and negative charges exist in different parts of the molecule. The structural resemblance to glycine and γ-aminobutylic acid are main inhibitory of neuron transmitting in central nervous system [2-5]. Dielectric properties of biological systems are highly remarkable by Yuri Feldman [6]. The complete understanding about beta-alanine and its geometrical structure is important to biological studies. Tsurko and Kuchtenko [7] have studied the thermodynamics and dissociation process of beta-alanine mixtures from 293.15K to 318.15K and given the extension of Debye model dielectric relaxation phenomena to understand the co-efficient by Ciancio et al. [8]. Mostly amino acid studies carried 2

out in various experimental and theoretical works [9, 10]. The chemical shift and coupling constant gives the identification (or) formation of hydrogen bonding. The NMR, FTIR and dielectric relaxation studies relates the complex formation of binary solution with respect to concentration, frequency and temperature. This work analyse the change in dielectric relaxation of beta-alanine- water binary solution to GHz frequencies. The dielectric parameters, relaxation time and thermodynamic parameters are measured in the frequency range 10MHz to 30GHz from 288k to 303k in steps of 5K. The spectral characterization analysis (FTIR) of beta-alanine mixtures of various concentrations and its crystallisation are analyzed. The carbon NMR chemical shifts are measured and interpreted. 2 Materials and measurements The beta-alanine is the product of sigma-Aldrich 99.8% pure and used ‘as such’ without further purification. Deionized water with conductivity 5.5х10-6 S/m has been utilized to prepare binary mixtures. The samples were set up by a measured amount of solute and allowed to dissolve in deionized water in proportionate ratios to the required concentrations as binary mixtures. 2.1 Dielectric Measurements The complex permittivity spectra were studied using Time Domain Reflectometry (TDR) in the frequency range of 10MHz-30GHz [11-20]. The basic TDR setup comprises broad band sampling oscilloscope, TDR module and coaxial transmission line. The Tektronix DSA8200 sampling oscilloscope with 30GHz bandwidth and TDR module 80E08 with step generator unit is used and this module gives the exact oscilloscope estimation. A 200mV step-pulse of 18ps incident pulse and 20ps reflected pulse time, 200 KHz repetition rate passes through coaxial 50Ω 3

impedance line. The co-axial semi-rigid copper cable E-286M17 an open end with dimensions of the co-axial cable as the inner diameter of the outer conductor is 2.2mm, outer diameter of the central conductor is 0.51mm and the diameter of the dielectric is 1.6mm. All measurements are carried out in open the load condition. Sampling oscilloscope monitor changes in step-pulse after reflection on sample. Two methods on the specific gravity of liquid were found by hydrometer and by density bottle. A flask was used to hold a known volume of liquid maintained at 303K. The empty bottle was weighed and then it was filled with the liquid whose specific gravity was to be found and weighed again. The difference in weight was divided by the weight of an equal volume of water to give the specific gravity of the liquid. The accuracy of measurement is in the order of 10 -3gm, at 0.1 MPa. 2.2 Data Analysis The time dependent data were processed to obtain complex reflection coefficient ρ*(ω) over a frequency range of 10 MHz to 30 GHz was determined as follows:

ε '' =ε  +

(ε 0 -ε  )ωτ 1+ω2 τ 2 

(1)

Where ρ(ω) and q (ω) are Fourier transform of ρ(t) and q (t) obtained using summation and samulon method [21] respectively, c is the velocity of light, ω is a angular frequency and d is effective pin length (0.09mm). 2.2.1 Debye and Cole-Cole model The complex permittivity spectra of beta-alanine fitted by the non-linear least square fit method of the Debye equation [22-24]

4

ε* = ε  +

ε 0 -ε  1+jωτ

(2)

Where ,ε0 - Static permittivity, ε*(ω)- Complex permittivity at angular frequency, ε∞ Permittivity at high frequency and τ- Relaxation time in ps of the system. Equation (2) expressed as

ε* = ε ' - jε''

(3)

ε'- Dielectric dispersion and ε‫״‬- Dielectric loss

ε ' =ε  +

ε 0 -ε  1+ω2 τ 2 

(4)

ε '' =ε  +

(ε 0 -ε  )ωτ 1+ω2 τ 2 

(5)

The Cole – Cole [25] has suggested an empirical relation to indicating the permittivity in the following form

ε* = ε  +

(ε 0 -ε  ) 1+(jωτ)1-α

(6)

α- indicates the symmetric distribution parameter of the relaxation time. Equation (6) expressed to 1/1-α

1v τ=   ωu 

(7)

Equation (7) is a Cole Cole relaxation time where ω =

1 and fr is the maximum frequency 2πf r

range.

5

2.2.2 Havriliak-Negami model The Havriliak-Negami [22] generalized the expression gives complex permittivity as ε* (ω) = ε  +

(ε 0 -ε  ) 1+(jωτ)1-α 

β

(8)

where α (0 < α  1) is a shape parameter used to express asymmetrical broadness of the relaxation curve and  (0 <   1) is that for symmetrical broadness. The parameters α = 1and  = 1 indicates the Debye -type relaxation and the parameter α = 1 indicates the Cole-Cole-type relaxation with shape parameter . The dielectric strength (Δε) the maximum electric field strength that it can withstand intrinsically without breaking down and is expressed as

Δε = ε 0 - ε 

(9)

2.2.3 Thermodynamic parameters The Energy of activation (ΔF) of complex system have been calculated using this formula [27] ΔF = ε 0 - ε '

(10)

The principle of thermodynamics gives the Gibbs free energy, a thermodynamic potential or free enthalpy is to predict whether a reaction will be spontaneous in the forward or reverse direction (or whether it is at equilibrium) ΔG = ΔH - TΔS

(11)

were H - enthalpy (of a system or process), S- entropy and T-absolute temperature. According to Eyrings rate theory [28-30] the temperature dependence on the relaxation time expressed as. KR =

KT  ΔG  exp h  RT 

(12)

where ΔG- Gibbs energy of activation, KR- Number of times per second, h- Plank’s constant and R- Gas constant 6

The Kirkwood correlation factor g is given by the expression [31, 32] g=

9kTM (εs -ε  )(2εs +ε  ) ε0 μ 2 Nρ εs (ε  +2)2

(13)

μ is dipole moments in gas phase, ρ is a density of the solution, M- Molar weight, k- Boltzmann constant, N- Avogadro’s number and ε0 is the permittivity of free space. Equation (13) has been used to study the orientation of electric dipoles in binary mixture [33, 34]. Such equation used as follows:

g eff =

M  9kT (εs -ε  )(2ε s +ε  )  M A ε0  2 + 2 B  2 N ε s (ε  +2)  μ Aρ A x A μ Bρ B x B 

(14)

The conductivity of the sample is compared using the expressions σ=

CεR1 (t) - R X (t) m mho dR1 (t) - R X (t)

(15)

R1(t) and RX(t) are values of reflected pulse at time t=∞ without and with sample respectively, ε is a permittivity of free space. 2.3 FTIR& NMR Analysis The FTIR spectrum of pure beta-alanine crystal mixed with KBr in the volume ratio of 1:10 and the spectra were recorded in the frequency range 400cm-1 to 4000cm-1 by Perkin-Elmer FTIR spectrophotometer at 303K. The KBr frequency assignments are subtracted from the recorded absorption spectra. ZnSe cuvettes are used for spectral measurement of mixture solutions. The sample solutions were prepared just before conduct of spectral measurements. The precession of the equipment measures approximately ± 1 cm-1. The spin-spin orientation of 13C NMR spectra was recorded using Bruker NMR spectrometer at 500 MHz. Deuterated water (D2O) used as a suitable detonator is mixed with beta-alanine for spectral measurements. The 13C NMR spectra precession of the equipment is ±1ppm. 7

3. Results and Discussions 3.1 Effect of Frequency and Concentration The frequency and concentration dependent complex permittivity spectra of beta-alanine are shown in Fig.1. By using equation (1) the complex reflection coefficient is determined and fitted by non-linear least square fit method using Debye equation (2) and (3).

The dielectric

permittivity (ε) and loss (ε) values were obtained by equations (4) and (5). The dielectric parameters values of binary solution for varying molar concentration and temperatures from 0.0017 to 0.017 mf and 303K to 283K respectively are listed in table.1. The observation provides the understanding of dielectric parameters as well as relaxation time increases with increase in concentration but decrease with temperature. This conforms the formation of molecular clusters of amino acid in coagulation form. The dipole moment for the amino acid dipolar ion is much greater than the ordinary polar molecules and therefore strong electrostatic interactions takes place between these ions and in addition of solvent more polar molecule are expected. Kirkwood addresses this as a type of amino acid dipolar ion “super polar” molecule surrounded by an intense electrostatic field. According to Debye, amino group has large dipole moment of such bio molecules should provide in large permittivity values. This work confirms that the amino acid permittivity increments in aqueous solutions are appreciable while increasing the concentration and decreasing the temperature are as shown in Fig.2 establishing the decrease in orientational correlation between dipolar moments with increase in temperature. The obtained dielectric parameter values of various concentrations compared with a similar trend of work as increasing values of static permittivity with molar concentration of amino acids reported earlier by chaudhari et al. [35]. The increment in dielectric permittivity is related to the effective dipole moment of the solute due to dipole-dipole alignment or dipolar increment. At lower 8

concentration the amino acid molecule is surrounded by water molecules and therefore the interaction between solute-solute is screened or blocked. Consequently the obtained dielectric constant values at 10MHz closer to water dielectric constant due to solvent strength. This confirms the origination of dipole-dipole correlations between the solute molecules.

3.2 Analysis of Relaxation Process The understanding is that the amino acid-water concentration ranges from a slight tendency towards molecular dipolar alignment of the solute molecules. Dealing with small bio molecules and quite diluted solutions, water predominately screens the solute-solute interactions. In this particular concentration range solute molecule remains mostly in isolated hydrate monomer form even on increasing the solute concentration. Two relaxation peaks are observed from dielectric spectra are properly fitted with Debye and Cole-Cole model as shown in Fig.3. The relaxation time (τ) increases with increase in molar concentration indicating the shifting of the absorption peak fmax to lower frequency is shown in Fig.4. The calculated relaxation time by Debye and Cole-Cole are values shown in table.1 by using equation (6) and (7). The faster one (τ1) is about 30ps at high frequency regime 15GHz to 20GHz is less dependence on solvent concentration. This has to be assigned with the dielectric relaxation of the water molecules and it has been shown by various works [36]. This significantly associated with combined relaxation of bulk frequency range as in the case of pure water. The higher order relaxation time can be considered as clear information about the presence of water associated with the amino acid molecule. The relaxation time of water molecule surrounded on amino acid shows much higher than those of free water molecules. However, the rate of increase in the relaxation time of solute concentration is matched with literature value [37]. The other one slower relaxation (τ2) is about 8-12ps clearly 9

dependent on the solute concentration and thereby mainly assignment due to amino acid relaxation. The higher value of relaxation time for the solutions of greater molar sides reflects the formation of hydrogen bonds between beta-alanine with water. The aqueous solution of alanine forms a cage like structure in the hydration region with enhanced relaxation time for the solute. The higher value of relaxation shows a strong solute-solvent interaction. The behavior of relaxation time reflects the fact that orientational motions of dipolar water molecule is hindered by interactions with neighbours and formation of strong hydrogen bonding. The main contributions of dielectric relaxation of amino acid on water molecules surround around the amino acid cluster are explained by Debye and Cole-Cole model. On increasing the concentration of solvent there is a broadening of peak could appear and this formation can be explained with symmetric Cole - Cole function [38] with equation (8). The relative density (rD) linearly increases in mole fraction as shown in Fig.5. The relaxation depends on density of the medium also increases with increase in concentration but restrain quickly with respect to temperature. The calculated values of density nearly match with the literature values [39]. 3.3 Thermodynamic Parameters and Activation Energy Dielectric strength (Δ, activation energy (ΔF) and thermodynamic parameters like enthalpy (ΔH), entropy (ΔS) and free energy (ΔG) change are calculated from equation (9), (10), (11) and (12) are reported in table.2. The positive values of heat of association i.e. entropy and enthalpy indicate that the association process is endothermic in nature and the reaction consumes more energy. However in some aqueous solutions the association process is releases energy as exothermic in nature. The Gibb’s energy of dissociation shows negative values of all concentrations. The observed value signifies the structure breaking effect on the solvent molecules and with the increase of solvation contribution. Gibb’s energy is connected with 10

solvation of solute ion in solvent and movement of ion and molecules, especially the main contribution of proton ion molecules. The entropy of hydration is related to the structure making and breaking properties of solutes. Marcus [40] identified that the entropy contribution to structured water effects and found that twisted structural entropy contribution is positive about structure breakers and negative for structure makers. The present systems signify the value of ΔF shows no appreciable increase or decrease, but varies slightly with concentration and temperature. This concludes that the molecules show no involvement in hetero association. 3.4 Conductivity and Correlation Factor The ac conductivity of binary solution was calculated by equation (15) and given in table.3. The conductivity increases as temperature increased indicating less solvation or higher mobility of ionic molecules of the solution. The mobility of ions enhanced due to varying degree of solvent ion in solutions and its radii. The breaking of bonds and release of large thermal energy leads to the variation in vibrational, translational and rotational energy of molecules with greater frequency of vibration and hence higher the mobility of ions. The conductivity also depends on ion concentration and rate of ion movement correspond to applied field intensity. The Kirkwood correlation factor (gf) and effective Kirkwood factor (geff) are calculated using equations (13) and (14).The Kirkwood correlation factor (gf) is greater than unity ensuring the existence of H-bonded molecules and multimers as aligned in parallel dipole ordering at lower concentrations. The parallel dipolar alignments in the pure liquid state that for an ideal noninteracting mixture gf must be equal to unity and a slight deviation from unity represents the existence of heterogeneous interaction between the components in the mixture [41]. The value of gf less than unity in higher concentration and temperature indicating the strength of interactions between the multimers are reduced as given in table. 3.

The gf values varies with the 11

concentration and temperature changes. Various authors reported that the value of gf will remain close to unity and there is no interaction between the component molecules [42, 43]. Also the value gf < 1 shows the dipoles of both molecules will be oriented in such a way that it signifies effective dipoles will be then the corresponding average values of the pure liquids.

The

corresponding geff data supplements the same as the effectiveness of correlation. It is considered that the number of aligned dipoles decreases to increasing the amino acid concentration. The long-range interaction between the dipoles in the mixture solution can be identified by this value. If positive, indicates the existence of attractive forces between the dipoles or negative there is a repulsive force between the dipoles. 3.5 FTIR Analysis Fig.6 shows the IR spectral data onto amino acid usually interpreted in terms of vibrations of a structural unit. In these amide bands are the most prominent vibrational bands and are backbone of amino acids [44-45]. The most sensitive spectral region to the amino acid and protein structural component is the amide band (1700-1600cm-1) which is due almost entirely to the C=O stretch vibrations of the amino acid linkages. The frequencies are correlated closely to the secondary structural element of the proteins. The secondary amide band derives mainly from in plane N-H bending and from C-N stretching vibration. The C=O stretching vibration with peptide linkage conforms the molecular geometry and hydrogen bonding pattern. The primary band components are due to mainly to C=O stretching vibration of the amide group coupled with little in plane N-H bending. The obtained (or) extraction frequency of this vibration band depends on the nature of the H-bonding coupled with C=O and NH component. FTIR spectra and the snapshot of beta- alanine single crystal are shown in Fig.7 and fig.8 respectively and corresponding intramolecular vibrations in the IR absorption spectra is given in 12

table.4. The observed IR spectra result is good agreement with various references [46-47]. In the case the symmetric and asymmetric C-H vibrations, the observed frequency value somewhat lowers than the theoretical values. This is probably due to the involvement in CH fundamental forces in Fermi resonance interactions. The frequency assignment to 530-650 cm-1 represents NH3 or NH2 torsional and CO2 rocking, deformation occurs. The symmetric and anti symmetric vibrations of CH2 group deformation, bending, wagging

to occur to the range of in the

vibrational region 900-1500 cm-1 and thus their assignment are fairly uncertain even when distraction from amino acid is involved. The average and week intensity in the 1635 cm -1 occurs to both liquid and solid state IR represents the bending of NH2. The low frequency assignment to this group of bands is connected with low energy vibrations. The table.4 represents the observed various vibrational band assignments are analysed on different well known data on vibrational spectra of organic substances with similar molecules and atomic groups. 3.6 NMR Analysis The 13C NMR spectra of beta-alanine in deuterated water complex have been measured at room temperature using 500MHz high resolution NMR spectrometer. The spectrum consists of single signal in carboxyl region and two lines in the lower field region. This two line represents the α and β methylene group signals on the basis of solution data [48] shown in Fig.9. The chemical shift of carbon atoms are predicted in their respective changes in frequency. The δC=O appears at 177.46ppm and δC2 at 35.64ppm and δC3-NH2 at 32.81ppm represented in table 5. The above mentioned values are taken in deuterated water and we compared with SDBS literature values [49] and it’s significantly matched. The δC=O chemical shift values exhibits formation of hydrogen bond. The negative charge in COO- H+ group is moved from the O=C moiety towards hydroxyl group. The C2 and C3 carbon chemical shifts to give lower region values for the 13

hydrogen bonded conformer. On analyzing the chemical shift values the COOH, CH2 and C-NH2 group shows slight shift approximately 2ppm. Thus the change in carbon chemical shift corresponds to a change in character and formation of hydrogen bond.

4. Conclusion We analyzed the characterization of beta-alanine solution to different concentration, temperature and frequency by Time Domain dielectric spectroscopy method from 10MHz to 30GHz. The dielectric spectra, various dielectric parameters are revealed and it has been found that the complex spectra are well fitted with Debye and Cole-Cole model to obtain dielectric relaxation parameters. This aspect is sensitive to changes in the dynamics in picoseconds range and understanding the molecular interactions of amino acid with water molecules. We have shown that zwitterionic nature of beta-alanine along with presence of strong polar groups of the studied concentration range and the tendency towards dipolar alignment is moderate. From our analysis the rotational relaxation time of beta-alanine with water molecule forms a hydration shell around the side chain of the molecule. The corrective kirkwood factor values found to be greater and less than unity indicates the molecules with parallel and antiparallel dipole moment and it confirms the dipolar orientation as activated one and random oriented. The disorder effect of amino acid on the structure of water in the infinitely dilute aqueous solution is confirmed by their thermodynamic properties. Thus it is clear that the contribution to hydrophilic hydration predominates on increasing the temperature. This expresses the total disorder action of the betaalanine on the structure of the water molecules. Our NMR experimental observation clearly exhibits the existence of hydrogen bonding with two constituents. The formation of complex make a signal shift approximately 2 to 3ppm with respect to pure beta-alanine compared with 14

SDBS [49]. Interpretation gives the intermolecular shielding on amino acid in –COOH group. The change in shift on carboxylic group clearly indicates the strength of the hydrogen bonding. The formation of hydrogen bonding significantly indicates in dielectric parameters compliments with FTIR and NMR studies. References [1] EQ. Adams, Relations between the constants of dibasic acids and of amphoteric electorolytes, J. Am. Chem. Soc. 38 (1916) 1503-1510. http://dx.doi.org/10.1021/ja02265a008. [2] L. Bonfanti, P. Peretto, S. De Marchis, A. Fasolo, Carnosine- related dipeptides in the Mammalian brain, Prog. Neurobiol. 59 (1999) 333-353. http://dx.doi.org/10.1016/S03010082(99)00010-6. [3] A.K. Nain, M. Lather, Solute–solute and solute–solvent interactions of L-histidine and Larginine in aqueous-streptomycin sulphate solutions at different temperatures: A physic chemical study, J. Mol. Liq. 211 (2015) 178-186. https://doi.org/10.1016/j.molliq.2015.07.018. [4] A. Bonincontro, C. Cametti , B. Nardiello , S. Marchettib, G. Onori, Dielectric behavior of DNA in water–organic co-solvent mixtures, Biophysical Chemistry. 121 (2006) 7–13. https://doi.org/10.1016/j.bpc.2005.12.002. [5] A.K. Nain, R. Pal, R.K Sharma, Volumetric, ultrasonic, and viscometric behaviour of Lhistidine in aqueous-glucose solutions at different temperatures, J. Chem. Thermodyn. 43 (2011) 603-612. https://doi.org/10.1016/j.jct.2010.11.017. [6] Yu. Feldman, I. Ermolina, Y. Hayashi, Time Domain Dielectric Spectroscopy Study of Biological Systems, IEEE Transactions on Dielectrics and EI. 10 (2003) 728-753. http://dx.doi.org/10.1109/TDEI.2003.1237324. [7] E. N. Tsurko, Yu. S Kuchtenko, Thermodynamics of the dissociation processes of betaalanine in ethanol–water mixtures at temperatures from 293.15 K to 318.15 K, J. Mol. Liq. 189 (2014) 95-99. http://dx.doi.org/10.1016/j.molliq.2013.03.023. [8] V. Ciancio, F.Farsaci, P.Rogolino, On a thermodynamical model for dielectric relaxation phenomena, Physica B. 405(2010) 175-179. https://doi.org/10.1016/j.physb.2009.08.047. [9] A.K. Nain, P. Droliya, J. Yadev, A. Agarwal, Physicochemical study of solute-solute and solute-solvent interactions of l-asparagine and l-glutamine in aqueous-d-mannose solutions at 15

temperatures from 293.15 K to 318.15, J. Chem. Thermodyn. 95 (2016) 202-215. https://doi.org/10.1016/j.jct.2015.11.014. [10] Jan Cz Dobrowolski, E.R Joanna, J. Sadlej, Ab initio simulations of the NMR spectra of βalanine conformers, Computational and Theoretical Chemistry. 964 (2011) 148-154. http://dx.doi.org/10.1016/j.comptc.2010.12.013. [11] T. Ganesh, D. Balamurugan, R. Sabesan, S. Krishnan, Dielectric relaxation studies of alkanols solubilized by sodium dodecyl sulphate aqueous solutions, J. Mol. Liq. 123 (2006) 8085. http://dx.doi.org/10.1016/j.molliq.2005.05.005. [12] T. Ganesh, R. Sabesan, S. Krishnan, Dielectric relaxation spectroscopic studies of ionic surfactants

in

aqueous

solutions,

J.

Mol.

Liq.

128

(2005)

77-80.

http://dx.doi.org/10.1016/j.molliq.2005.11.038. [13] T. Ganesh, R. Sabesan, S. Krishnan, Dielectric relaxation studies of alkanols solubilized by cationic

surfactants

in

aqueous

solutions,

J.

Mol.

Liq.

137

(2008)

31-35.

http://dx.doi.org/10.1016/j.molliq.2007.03.003. [14] R B Talware, P. G. Hudge, Y. S. Joshi, A. C. Kumbharkhane, Dielectric relaxation study of glycine–water mixtures using time domain reflectometry technique, Physics and Chemistry of Liquids. 50 (2012) 102-112. http://dx.doi.org/10.1080/00319104.2010.551345. [15] A.C. Kumbharkhane,

Y.S. Joshi, S.C. Mehrotra, S.Yagihara, Seiichi Sudo, Study of

hydrogen bonding and thermodynamic behavior in water–1,4-dioxane mixture using time domain reflectometry, Physica B. 421(2013)1-7. http://dx.doi.org/10.1016/j.physb.2013.03.040. [16] R. J. Sengwa , R. Chaudhary, S.C. Mehrotra, Dielectric behaviour of propylene glycol-water mixtures studied by time domain reflectometry, Molecular Physics. 99 (2001) 1805-1812. http://dx.doi.org/10.1080/00268970110072782. [17] N. K. Karthick, G. Arivazhagan, A. C. Kumbharkhane, Y.S. Joshi, P.P Kannan, Time Domain Reflectometric and spectroscopic studies on toluene + butyronitrile solution, J. Mol. Stru. 1108 (2015) 203-208. https://doi.org/10.1016/j.molstruc.2015.12.009. [18] K. Dharmalingam, K. Ramachandran , P. Sivagurunathan, B.P. Undre, P.W Khirade, S. C. Mehrotra, Dielectric studies of alkyl acrylates with primary alcohols using time domain reflectometry,

Molecular

Physics.

104

(2006)

2835-2840.

http://dx.doi.org/10.1080/00268970600842737. 16

[19] P. Sivagurunathan, K. Dharmalingam, K. Ramachandran, B.P Undre, P.W. Khirade, S.C. Mehrotra, Dielectric study of butyl methacrylate–alcohol mixtures by time-domain reflectometry, Physica B. 387 (2007) 203-207. http://dx.doi.org/10.1016/j.physb.2006.04.005. [20] S. B. Jones, Dani Or, Modeled effects on permittivity measurements of water content in high

surface

area

porous

media.

Physica

B.

338

(2003)

284-290.

http://dx.doi.org/10.1016/j.physb.2003.08.008. [21]

N. E. Hager III, Broadband time domain reflectometry dielectric spectroscopy using

variabletime

scale

sampling,

Rev.

Sci.

Instrum.

65

(1994)

887-891.

http://dx.doi.org/10.1063/1.1144917. [22] S. Havrilak, S. Negami, A complex plane analysis of or-dispersions in some polymer systems, J. Polym. Sci, Part C. 14 (1996) 99-117. http://dx.doi.org/10.1002/polc.5070140111. [23] K.S. Cole, R.H. Cole, Persion and absorption in dielectrics I. Alternating current characteristics, J. Chem. Phys. 9 (1941) 341-351. http://dx.doi.org/10.1063/1.1750906. [24] D. W. Davidson, R. H. Cole, Dielectric relaxation in glycerol, propylene glycol, and npropanol, J. Chem. Phys. 19 (1951) 1484-1490. http://dx.doi.org/10.1063/1.1748105. [25] N. K. Karthick, G. Arivazhagan, A. C. Kumbharkhane, Y. S. Joshi, P. P Kannan, Time domain reflectometric study on toluene + propionitrile binary mixture, Physics and Chemistry of Liquids. 54(6) (2016) 779-785. http://dx.doi.org/10.1080/00319104.2016.1161042. [26] S.S Shaikh, A. C. Kumbharkhane, Dielectric relaxation studies of aqueous solution of polyethylene glycol 200 (PEG200) using time-domain reflectometry, Physics and Chemistry of Liquids. 53(5) (2015) 1-11. http://dx.doi.org/10.1080/00319104.2015.1018258. [27] M. Jaroszewski, J. J. Pospieszna, Dielectric properties of polypropylene fabrics with carbon plasma coatings for applications in the technique of electromagnetic field shielding, Journal of Non-Crystalline

Solids.

356(11-14)

(2010)

625-628.

http://dx.doi.org/10.1016/j.jnoncrysol.2009.06.049. [28] H. Eyring, S. Glasstone, The theory of rate process, the kinetics of chemical reaction, viscosity, diffusion and electrochemical phenomena, The theory of rate process, M C Graw Hill, NY. (1941) 611p. [29] H. Eyring, Viscosity, plasticity, and diffusion as examples of absolute reaction rates, J. Chem. Phys. 4(1936) 283-291. http://dx.doi.org/10.1063/1.1749836. 17

[30] K. Giese, U. Kaatze, R. Pottel, Permittivity and dielectric and proton magnetic relaxation of aqueous

solutions

of

the alkali

halides,

J.

Phys.

Chem.

74 (1970) 3718-3970.

http://dx.doi.org/10.1021/j100715a005. [31] J.G. Kirkwood, The Dielectric Polarization of Polar Liquids, J. Chem. Phys. 7 (1939) 911920. http://dx.doi.org/10.1063/1.1750343. [32] G. Arivazhagan, T. Thenappan, H-bond interactions of propionic acid with 1,4-dioxane mixture by dielectric studies, UV-Vis and 13C NMR spectral studies, Physics and Chemistry of Liquids. 49(3) (2011) 275-285. http://dx.doi.org/10.1080/00319100903131534. [33] S.M. Puranik, A.C. Kumbhrkhane, S.C. Mehrotra, Dielectric relaxation spectra for N,NDimethylacetamide-water mixures using picosecond time domain reflectometry, J. Mol. Liq. (1991) 143-153. http://dx.doi.org/10.1016/0167-7322(91)80042-3. [34] A.C. Kumbharkhane, S.M. Puranik, S.C. Mehrotra, . Dielectric relaxation studies of aqueous N,N-dimethylformamide using a picosecond time domain technique, J. Sol. Chem. 22(3) (1991) 219-229. http://dx.doi.org/10.1007/BF00649245. [35] H.C. Chaudhari, A. Chaudhair, S.C Mehrotra, Dielectric Study of Aqueous Solutions of Alanine

and

Phenylalanine,

J.

Chinese.

Chem.

Soc.

52

(2005)

5-10.

http://dx.doi.org/10.1002/jccs.200500002. [36] R Buchner, J. Barthel, J. Stauber, The dielectric relaxation of water between 0°C and 35°C, Chem. Phys. Ltt. 306 (1999) 57-63. http://dx.doi.org/10.1016/S0009-2614(99)00455-8. [37] Iñigo Rodriguez-Arteche, Dielectric spectroscopy in the GHz region on fully hydrated zwitterionic

amino

acids,

Phys.

Chem.

Chem.

Phys.

14

(2012)

11352-11362.

http://dx.doi.org/10.1039/c2cp41196a. [38] M. Maria Sylvester, T. Ganesh, D.J.S. AnandKarunakaran, Praveen Hudge, A.C Kumbharkhane, Time domain dielectric relaxation studies of amphiphilics in solution state, J. Mol. Liq. 194 (2014) 57-61. http://dx.doi.org/ 10.1016/j.molliq.2013.12.051. [39] C. M. Romero, J.C.Cadena, Effect of Temperature on the Volumetric Properties of α, ωAmino Acids in Dilute Aqueous Solutions, J. Sol. Chem. 39(2010) 1474-1483. http://dx.doi.org/ 10.1007/s10953-010-9602-1. [40] Y. Marcus, Effect of Ions on the Structure of Water: Structure Making and Breaking, Chem. Revs. 109 (2009) 1346-1370. http://dx.doi.org/10.1021/cr8003828. 18

[41] C. J. F. Bottcher, Theory of electric polarization Vol-I, Elesevier, Amsterdam, (1973). [42] D. Balamurugan, S. Kumar, S. Krishnan, Dielectric relaxation studies of higher order alcohol complexes with amines using time domain reflectometry, J. Mol. Liq. 122 (2005) 11-14. http://dx.doi.org/10.1016/j.molliq.2004.11.004. [43] D.J. S. AnandKarunakaran, T. Ganesh, M. MariaSylvester, Praveen Hudge, A. C. Kumbharkhane, Dielectric properties and analysis of H-bonded interaction study in complex systems of binary and ternary mixtures of polyvinyl alcohol with water and DMSO, Fluid Phase Equilibria. 382 (2014) 300-306. http://dx.doi.org/10.1016/j.fluid.2014.09.018. [44] S. Krimm, J. Bandeker, Vibrational spectroscopy and conformation of peptides, polypeptides

and

proteins,

Adr.

Protein.

Chem.

38

(1986)

181-364.

http://dx.doi.org/10.1016/S0065-3233(08)60528-8. [45] W. K. Surewicz, H.H. Mantsch, New sight into protein secondary structure from resolution enhanced

Infrared

spectra,

Biochim.

Biophys.

Acta.

952

(1988)

115-130.

http://dx.doi.org/10.1016/0167-4838(88)90107-0. [46] J. Kong, Yu. Shaoning, Fourier transform infrared spectroscopic analysis of protein secondary structures, Acta. Biochimica. et Biophysica. Sinica. 39 (2007) 549-559. http://dx.doi.org/10.1111/j.1745-7270.2007.00320.x. [47] L.I. Berezhingky, G.I. Dovbeshko, M. P. Lisitsa, G. S. Litvinor, Vibrational spectra of crystalline β-alanine,

Spectro.

Chimica.

Acta

P-A.

54

(1998)

349-358.

http://dx.doi.org/10.1016/S1386-1425(97)00233-3. [48]

H.

W.

E.

Rattle,

NMR

Spectroscopy,

Annu.

Rep.

11(A)

(1981)

1-64.

http://dx.doi.org/10.1016/S0066-4103(08)60408-1. [49] WWW.SDBS. DB. AIST. GO. JP. (Structural Database for organic systems. Japan).

19

Fig. 1: Complex permittivity spectra for various temperatures of mf 0.0017

Fig. 2: The plot between temperature Vs Ԑ0 for various mole fractions

20

Fig. 3: The Cole-Cole plot for various temperatures of mf 0.0017

Fig. 4: The plot between temperature Vs τps for various molefractions

21

Fig. 5: The plot between mole fractions Vs relative density (rD) at 303K.

Fig. 6: FTIR Spectra of various mole fractions in the range of 400 to 4000 cm-1

22

Fig. 7: FTIR Spectra of beta-alanine single crystal

Fig. 8: The snapshot of beta-alanine Single Crystal

23

Fig. 9: 13C NMR spectrum of beta-alanine in D2O TABLE 1: The dielectric parameters (ε0, ε, ε and ε), relaxation time (τ), distribution parameter(α), dielectric strength (Δε) and dielectric activation(ΔF) for various mole fractions and temperature of beta-alanine at p= 0.1 MPa. ε0 ε‫׳‬ ε" Mole Temp. Debye τps α ε∞= 4.00 fraction K τ1(ps) τ2(ps) Colemf Cole Δε ΔF (kJ/mol) (kJ/mol) 0.0017

0.0035

0.0053

0.0071

283 288 293 298 303 283 288 293 298 303 283 288 293 298 303 283 288 293 298 303

87.06 86.03 84.28 84.17 83.40 87.63 86.05 84.30 84.21 83.45 88.58 86.08 84.75 84.40 83.50 88.80 86.90 85.33 84.55 83.54

45.00 44.90 44.22 44.37 44.07 45.21 44.61 44.30 44.27 44.10 45.66 44.66 44.51 44.46 43.97 45.73 45.22 44.88 44.33 44.00

42.06 41.45 40.05 39.79 39.33 42.41 41.44 39.99 39.93 39.95 42.92 41.41 40.23 39.94 39.53 43.06 41.67 40.44 40.21 39.53

10.78 9.99 9.50 9.32 9.05 10.79 9.82 9.55 9.33 9.06 11.11 10.23 9.66 9.38 9.08 11.21 10.44 9.92 9.41 9.20

18.55 15.43 13.54 12.58 11.64 19.96 16.05 13.98 13.01 12.27 22.49 18.22 16.19 15.13 13.68 24.42 21.49 19.07 16.53 15.45

11.23 10.48 9.91 9.69 9.34 11.26 10.23 9.59 9.39 9.15 11.81 10.86 9.98 9.61 9.30 11.62 10.9 10.6 9.71 9.35

0.15 0.13 0.08 0.06 0.04 0.15 0.13 0.08 0.06 0.04 0.15 0.13 0.08 0.06 0.04 0.15 0.13 0.08 0.06 0.04

85.12 82.26 80.51 79.59 78.67 84.83 81.48 78.90 78.29 77.11 85.84 82.83 80.07 79.18 78.57 86.12 83.35 80.91 79.96 79.06

42.06 41.13 40.05 39.79 39.33 42.41 41.44 39.99 39.93 39.35 45.66 41.41 40.23 39.94 39.28 43.06 41.67 40.44 40.21 39.53

24

0.0089

0.0106

0.0122

0.0142

0.0159

0.0176

283 288 293 298 303 283 288 293 298 303 283 288 293 298 303 283 288 293 298 303 283 288 293 298 303

89.40 87.10 85.35 84.60 84.35 89.55 87.19 85.52 85.12 84.37 89.66 87.23 85.64 85.19 84.54 89.78 87.46 85.87 85.29 84.58 89.81 88.15 86.32 85.56 84.79

46.28 45.28 44.75 44.64 44.59 46.23 45.30 44.81 44.82 44.43 46.06 44.96 44.38 44.41 44.38 46.34 45.10 44.70 44.44 44.16 46.35 45.73 44.97 44.76 44.48

43.12 45.28 44.75 44.64 44.59 43.32 41.88 40.71 40.29 37.41 43.59 42.26 41.26 40.78 40.66 46.34 45.10 44.70 44.44 44.16 43.45 42.42 41.34 40.79 40.31

11.42 10.49 9.94 9.57 9.42 11.48 10.74 10.12 9.84 9.53 11.57 10.79 10.15 9.99 9.68 11.80 10.81 10.22 10.01 9.69 12.04 11.17 10.85 10.14 9.81

25.65 22.16 18.98 17.64 16.82 27.77 24.27 21.87 20.36 19.06 28.17 24.59 22.25 20.96 19.95 30.77 26.81 24.51 23.08 22.06 32.42 29.10 26.28 24.98 23.80

11.91 10.59 9.99 9.80 9.50 11.80 10.78 10.50 10.10 9.62 11.62 10.84 10.22 10.07 9.73 11.89 10.89 10.37 10.12 9.76 12.15 11.23 10.99 10.47 10.09

0.15 0.13 0.08 0.06 0.04 0.15 0.13 0.08 0.06 0.04 0.15 0.13 0.08 0.06 0.04 0.15 0.13 0.08 0.06 0.04 0.15 0.13 0.08 0.06 0.04

86.24 83.72 81.20 79.93 79.53 86.64 84.22 81.82 80.58 79.88 86.89 84.53 82.52 81.42 80.33 86.88 84.70 82.34 81.70 80.83 87.03 84.84 82.69 81.58 80.63

43.12 41.81 40.60 39.96 39.76 43.31 41.88 40.71 40.29 39.94 43.59 42.26 41.26 40.78 40.16 43.44 42.35 41.17 40.85 40.41 43.45 42.42 41.34 40.79 40.31

283 288 293 298 303

89.83 88.84 87.28 85.70 84.94

46.59 46.21 45.54 44.69 44.69

43.24 42.62 41.73 41.01 40.24

12.09 11.12 10.99 10.12 9.95

34.92 29.70 27.58 26.39 25.41

12.34 11.23 11.10 10.48 10.26

0.15 0.13 0.08 0.06 0.04

86.38 84.24 82.47 81.83 80.49

43.24 42.62 41.73 41.01 40.24

TABLE 2: Thermodynamic parameters (H, S and G) and relative density(rD) for various mole fractions of beta-alanine. Mole Molar enthalpy Molar entropy Gibbs free rD fraction (ΔH) (ΔS) energy (ΔG) (gm/ cm3) mf (kJ/mol) (J/mol K) (kJ/mol)

25

0.0017

3.583

0.877

-262.42

1.0051

0.0035

4.243

1.049

-313.42

1.0059

0.0053

4.567

0.870

-259.81

1.0067

0.0071

4.714

0.625

-184.84

1.0075

0.0089

4.399

1.149

-343.89

1.0082

0.0106

4.375

0.791

-235.47

1.0089

0.0122

3.574

1.161

-347.90

1.0095

0.0142

4.319

1.084

-324.22

1.0134

0.0159

4.800

0.807

-239.99

1.0174

0.0176

5.426

0.213

-139.07

1.0231

TABLE 3: Conductivity(σ), Correlation factor(gf) and effective correlation factor(geff) of beta-alanine on various mole fractions and temperature. Mole Temp σх10-3 gf geff fraction K (m.mho) mf 0.0017

0.0035

0.0053

0.0071

0.0089

283 288 293 298 303 283 288 293 298 303 283 288 293 298 303 283 288 293 298 303 283 288 293 298 303

8.20 10.60 13.10 17.18 28.5 3.91 5.98 7.74 11.7 17.4 2.89 5.46 9.23 13.1 18.6 6.93 9.96 14.2 16.22 19.66 6.51 9.16 10.3 12.4 20.0

1.49 1.53 1.53 1.54 1.55 0.98 1.01 1.01 1.02 1.03 0.74 0.75 0.75 0.76 0.77 0.59 0.60 0.60 0.61 0.62 0.49 0.50 0.50 0.50 0.51

1.00 1.00 1.00 0.99 1.00 0.86 0.85 0.85 0.85 0.86 0.81 0.80 0.80 0.80 0.80 0.78 0.77 0.77 0.77 0.77 0.76 0.76 0.75 0..75 0.76

26

0.0106

0.0122

0.0142

0.0159

0.0176

283 288 293 298 303 283 288 293 298 303 283 288 293 298 303 283 288 293 298 303 283 288 293 298 303

6.85 8.09 10.0 13.6 23.9 6.17 8.52 8.68 11.3 13.9 6.14 8.10 9.98 11.2 14.0 7.83 9.08 11.1 13.6 18.8 16.7 18.1 21.3 23.4 26.9

0.42 0.43 0.43 0.43 0.44 0.36 0.30 0.37 0.38 0.39 0.32 0.33 0.33 0.34 0.35 0.29 0.30 0.30 0.30 0.31 0.26 0.27 0.27 0.27 0.28

0.75 0.74 0.74 0.74 0.75 0.74 0.74 0.74 0.74 0.74 0.74 0.73 0.73 0.73 0.74 0.73 0.73 0.73 0.73 0.73 0.73 0.73 0.72 0.72 0.73

TABLE 4. FTIR Frequency assignments of beta-alanine in solution and crystalline state FTIR Frequency Assignments In solution

Single crystal

Assignments

-

538

NH3+ Torsion & CO2 rocking

670

652

C-O Torsion,CO2- deformation

-

840

C-C strectching

-

990

CH2 deformation rocking

1049

1079

CH2 rocking + NH2 twisting, C-N asymmetric stretching

27

1105

1154, 1187

CN mode, CH2 deformation rocking

-

1293

CH2 bending

1331,1407

1337

Wagging CH2, CH2 deformation wagging

1463

-

Bending CH2

-

1571

CO2- asymmetric stretching

1635

1636

Bending NH2, NH3+ asymmetric deformation

-

2202

Second order bands

-

2821

CH2 stretching

3413

-

Asymmetric stretching NH2

3433

-

Asymmetric OH

3463

-

Secondary amides –free NH transverse mode

TABLE 5: Chemical shif (δ), shif of chemical shift (Δδ) of 13C NMR characteristics for beta-alanine in D2O Carbon in Mixture Pure beta-alanine[63] Δδ δ (ppm)

δ (ppm)

ppm

δC=O

177.46

179.11

1.65

δC2

35.64

37.37

1.73

δC3-NH2

32.81

34.43

1.62

28