Peptide chemistry (second edition)

145

(A)

students spend anything from half an hour to two hours working on a given sequence, and write a short report on their results. The c o m m e n t s from the students on the use of this program in teaching have been generally positive. H o w e v e r , a systematic estimation of the effectiveness of this program in teaching is not yet available. S I M S E Q was programmed with Turbo Prolog V 2.0 (Borland International, U S A ) . The program runs in IBM compatible microcomputers, preferably having at least a 286-type of processor. The programs take up 116 kB of disk space and requires 130 kB of free memory. A copy of the program in a compiled form can be obtained from the authors by sending a high density 3.5" diskette to Dr M V u e n t o , Department of Biological and Environmental Science, University of Jyv~iskyl~i, Vapaudenkatu 4, 40100 Jyv~iskyl~, Finland, fax 358-41-602221.

SIMULATION OF PEPTIDE SEQUENCING

F Press Enter or F]O t o accept c h o l c e ~ SELECT pEPTIDE ! SELECT OPERATION I CHECK yOUR RESULTS HELP EXIT PR~RAM

. . .5. . . . . . . . . . . . . .

(B)

--~FN~ ..................

..............

--

Pept ide Peptide peptide Peptide Peptide Peptide Peptide Peptlde Peptide Peptide Peptlde Peptide Peptide Peptide Peptide Peptide Peptide Peptlde Peptide

...................

] 7

SIMULATION OF PEPTIDE SEQUENCING Select a peptide t rum memory I length 7 amino acids I 2 length ? amino acids ~r 3 length I0 amino acids 4 length I0 amino acids 5 length ]0 amino acids 6 length I0 amine acids 7 length 14 amino acids 8 length 14 amino acids 9 length 14 amino acids I 10 length 18 amino ac~dsl Ii length 18 amino acids[ ]2 length 2O amino acids 13 length 20 amino acids 14 length 22 amino acids 15 length 22 amino acids 16 length 22 amino acids [7 lenqt~ 24 amino acids 18 length 26 amino acids g Peptide 19 length 28 amino acids

I

,!~p,,a~io~ in ~rogres~-~

References tBender D A (1986) Biochem Educ 14, 17-22 2Zubay G (1993) Biochemistry, Vol I, Wm C Brown Publishers, Dubuque 3Havlicek P J and Towns A P (1979) Chemistry in Australia 46, 151-153 4Creighton T E (1993) Proteins, Second Edition, W H Freeman and Company, New York

(C) Select operation Trypsin cleavage Chymotrypsin cleavage Thermolysin cleavage Prolyl endopeptidase V8 protease cleavage CNBr cleavage

S-cyanylation Dansyl chloride Amino acid analysis

Carboxypeptidase Automatic

Edman degradation menu

Go back to first

Book Review

(D)

Results After performic acid o×Jdation and acid hydrolysis the amino acid composition was found to be the f o l l o w i n g : Alanine

I

Phenylalanine

i

Clycine I

Lyslne 2

Serine I

Peptide Chemistry (Second Edition)

Tyrosine 1

by M Bodanszky. pp 198. Springer-Verlag, Berlin and N e w York. 1993. D M 48 ISBN 0 - 3 8 7 - 5 6 6 7 5 - 9

---original Peptide # ~ 2

(E)

.......

I~

2 ? :

.................

]F

...................

]

now have the following

amino acids

22 3 amino acids

............... , ( . ;

(F)

N~W

-Re,ulna peptides f r o m # 2 with *** .....................................

,~--------yOU

Peptlde

j~

,cleaved

,cleaved

n]

from # 2 with Trypsin

. . . . . . . . . . . . . . . . . . 11

SIMULATION OF PEPTIDE SEQUENCING GiVe the ID number or the peptide you have sequenced TYPE AMINO AgeD SEQUENCE IN ONE LETTER CODE

2

I Ii

!

Figure I Examples of input and output screens. A, the main menu; B, selecting a peptide from database; C, selecting operation; D, results from an amino acid analysis; E, results from an experiment with trypsin

BIOCHEMICAL

EDUCATION

22(3) 1994

Peptide Chemistry: a Practical Textbook is a revised version of the first edition which was published in 1988. This field is currently greatly expanding and publication of such a book is very necessary. Unfortunately, although the book gives much important information concerning structure determination and peptide synthesis, it is really a textbook on the principles more than a practical one. No experiments are described in such a manner to be immediately useful for a teacher or a student. Moreover, in part two (Peptide Synthesis) the book does not contain much recent information on new applications of peptide synthesis such as multiple antigen peptide (MAP) synthesis, multiple peptide synthesis (tea-bag or pin's method), peptide libraries etc. Furthermore, we may regret that only 3 pages are devoted to enzyme-catalyzed peptide synthesis, with two references from 1969 and 1982, respectively, although about ten reviews have been published in the last twelve years. Nevertheless, due to its low cost, this book will be of interest as an introduction in the field of peptide synthesis.

J Wallach