- Email: [email protected]
Biological membranes: Structure, biogenesis and dynamics
reasonsfor apparent in the information obtaIned by th techniques.~~~~, the reviewof current
~i~~~jc~lmembranes: Structure,
amino acids during membrane insertion, and there is a useful Biogenesis andDynamics reviewof recent progressin understanding how proteins crossa membrane. tifiedbyksA.F.Opckrr By contrast, the authors of many Sp&g#?t2994. f?.M chapters in the book have conceMra&f (x + 356 /sm 3 540 577319 prima&y on presenting, or reviewing, work undertakenin their own &borate. The programme for the NATOAdvanced Someof these chapters even have Study Institute, held in Car&se, France,in sections entitled ‘Materials and Methods’, June 1993on the structure, biogenesisand or ‘Experimental’,and ‘Results’.Readers dynamicsofhio~membranesinciuded will doubtless differ on which approach four major topics: (1) lipid dynamicsand they find more helpful. Personally,in lipid-protein interactions; (2) protein books of this kind f prefer articles cfeaflng translocationand insertion; (3) intracellular with problems, questions and principles, traffic; and (4) protein structure and since details of specific experiments can folding. The Proceedingsof the Institute be obtained from the orlglnal papers. have been assembledby l3r Op den Kamp The book covers a huge range of and published in this volume. membrane topics, which cannot a;Ifbe The book is well produced but, as a considered here. It includeschapters on consequenceof the use of camera-ready membranes in bacteria, yeast, marine copy,the individual chapters differ quite flageffatesand mammalian cells. The markedly in typography and in the ease disciplinescovered are similarly wide with which they can be read. More ranging: from biophysicsto cell biology. significantly,although each contribution For example,on the biophyskal side, beginswith a useful summary and ends noncrystallographic methods to study with a bibliography that lnciudes the membraneprotelns@M-state NMR,magic titles of the papers cited, the chapters angle spinning) are discussed,as are the usesof circular dichroism and NMRto differ markedly in layout, styie and determine the conformational properties apparently also in their aim. Thus, the article on magnetic resonancestudies of of signal sequences,and of fluorescence spectroscopyto analysetheir insertion protein--lipidinteractions in membrane sequencesinto membranes.On the systemsprovides a relatively general reviewof some of the recent advancesin structural side,one chapter describesthe spin-labelelectron spin resonanceand structure and mechanismsof action of solid-statenuclear magn&c resonance porins. Cunent biochemical approaches (NMR).The author covers basic are represented in chapters on principlesof the methods, considerstheir giy~osyiphosphatidyllnosltoi~~ifi~ relative advantagesand discusses phosphoiipase B, and on the
and turnover of
are provided In contributions on the N&Z of p~ph~~~ in (bacterial) cell function. and tht?cdransiational
thechapterondivisiondtheGo@i apparatus during mitosis in animal cells. ~ys~wo~~~~~ biomembranes consider buyfng this book, or recommending it for purchaseby their library? A valuablefeature is that it covers an extremely wide rangeof up&date topicsinasuccinctway.itshouldtherefore be useful to postgraduate students and postdoctoral workers, and also to establishedinvestigators in the field seekinginfoncurren~questlW+, problems and techniques outside their own immediate areasof interest. fn order to avoid repeatedly scanningthrough the list of all 34 chapter titles (which are not !iectionaiizedin the list of contents) to seewhether a specifictopic is covered, it might be useful to design and store keywords for each chapter in your own database of references.However,on a more casualbasis,anyone working on biological membraneswho dips into this book is likely to find severalchapters of interest and value. JACK A. UJCY Oepartmmt of Cellular I%ysiology,Thef3atWim
Institute.Eabmham, Cambridge, UKCE24AT.
-.
Seductionandpfedktbn TheProtein Folding Problem and Tertiary Structure Prediction editedbyK. M.~Jr,S.M.l&md and M. Smtt, 8Mhduser 8oston,1994. E82.uo/$99.u0 (x t 581 pages) lS5Af3 7643 3693 5 The protein folding problem can be stated so seductively:given the ilnear sequence of a protein, predict its &eedimensional structure in its functional envfronment. For more than 30 years, theoretklans have struggfed to unravel the folding code. In the early 1970s.the problem was sometimesacademic-there were several occasionswhen the three&nensional stru&reofaprote&wassofved crystaUographicaflybefore knowledge of
its sequence.But today the genome pro@% are blasting us with sequencesof unknown structure, and a soiutlon has become important to a wide community. The general solution is to identify the conformation of minimum energy.There de at least two major obstacles to overcome. Rrst, an accurate description of the atom interactions is required. Second,there is an enormous search problem to identify the native conformation from the myriad of afternatives. Giventhese hurdles, as protein structures were revealed in the 197Os,many workers decided to ‘cheat’ and developed empirical schemesfor predictfon. Today,these are used widely in both secondary structure prediction and ln obtaining a tertiary model based on the determined coordinates of a homologous molecule. This book reports how the chafiengeof a generalsolution remains, and how
presentday computing power has stimulated the community to employ a variety of new approaches.it is a muftiauthor text covering a broad range of topics. The emphasisis on new solutions to old probim - effective potentials and the search algorithms. The recent applications of stat&-the-art atomic potentials to systemssuch as sidechain conformation and loop selectionare described. fn addition, the topical applications of pseudopotentials derived from statistlcaf analysisof known structures to distinguish between correctly and incorrectly folded structures am!reported. sevea new searcha@rlMnsaredescribed, including simulated allnabn& genetic algorithms, deadend efimination, branch-and-boundminimization and neuraf networks. Proteinfofds with characteristic second-a packingcan be generatedde R900using
329
~i~~~jc~lmembranes: Structure,
amino acids during membrane insertion, and there is a useful Biogenesis andDynamics reviewof recent progressin understanding how proteins crossa membrane. tifiedbyksA.F.Opckrr By contrast, the authors of many Sp&g#?t2994. f?.M chapters in the book have conceMra&f (x + 356 /sm 3 540 577319 prima&y on presenting, or reviewing, work undertakenin their own &borate. The programme for the NATOAdvanced Someof these chapters even have Study Institute, held in Car&se, France,in sections entitled ‘Materials and Methods’, June 1993on the structure, biogenesisand or ‘Experimental’,and ‘Results’.Readers dynamicsofhio~membranesinciuded will doubtless differ on which approach four major topics: (1) lipid dynamicsand they find more helpful. Personally,in lipid-protein interactions; (2) protein books of this kind f prefer articles cfeaflng translocationand insertion; (3) intracellular with problems, questions and principles, traffic; and (4) protein structure and since details of specific experiments can folding. The Proceedingsof the Institute be obtained from the orlglnal papers. have been assembledby l3r Op den Kamp The book covers a huge range of and published in this volume. membrane topics, which cannot a;Ifbe The book is well produced but, as a considered here. It includeschapters on consequenceof the use of camera-ready membranes in bacteria, yeast, marine copy,the individual chapters differ quite flageffatesand mammalian cells. The markedly in typography and in the ease disciplinescovered are similarly wide with which they can be read. More ranging: from biophysicsto cell biology. significantly,although each contribution For example,on the biophyskal side, beginswith a useful summary and ends noncrystallographic methods to study with a bibliography that lnciudes the membraneprotelns@M-state NMR,magic titles of the papers cited, the chapters angle spinning) are discussed,as are the usesof circular dichroism and NMRto differ markedly in layout, styie and determine the conformational properties apparently also in their aim. Thus, the article on magnetic resonancestudies of of signal sequences,and of fluorescence spectroscopyto analysetheir insertion protein--lipidinteractions in membrane sequencesinto membranes.On the systemsprovides a relatively general reviewof some of the recent advancesin structural side,one chapter describesthe spin-labelelectron spin resonanceand structure and mechanismsof action of solid-statenuclear magn&c resonance porins. Cunent biochemical approaches (NMR).The author covers basic are represented in chapters on principlesof the methods, considerstheir giy~osyiphosphatidyllnosltoi~~ifi~ relative advantagesand discusses phosphoiipase B, and on the
and turnover of
are provided In contributions on the N&Z of p~ph~~~ in (bacterial) cell function. and tht?cdransiational
thechapterondivisiondtheGo@i apparatus during mitosis in animal cells. ~ys~wo~~~~~ biomembranes consider buyfng this book, or recommending it for purchaseby their library? A valuablefeature is that it covers an extremely wide rangeof up&date topicsinasuccinctway.itshouldtherefore be useful to postgraduate students and postdoctoral workers, and also to establishedinvestigators in the field seekinginfoncurren~questlW+, problems and techniques outside their own immediate areasof interest. fn order to avoid repeatedly scanningthrough the list of all 34 chapter titles (which are not !iectionaiizedin the list of contents) to seewhether a specifictopic is covered, it might be useful to design and store keywords for each chapter in your own database of references.However,on a more casualbasis,anyone working on biological membraneswho dips into this book is likely to find severalchapters of interest and value. JACK A. UJCY Oepartmmt of Cellular I%ysiology,Thef3atWim
Institute.Eabmham, Cambridge, UKCE24AT.
-.
Seductionandpfedktbn TheProtein Folding Problem and Tertiary Structure Prediction editedbyK. M.~Jr,S.M.l&md and M. Smtt, 8Mhduser 8oston,1994. E82.uo/$99.u0 (x t 581 pages) lS5Af3 7643 3693 5 The protein folding problem can be stated so seductively:given the ilnear sequence of a protein, predict its &eedimensional structure in its functional envfronment. For more than 30 years, theoretklans have struggfed to unravel the folding code. In the early 1970s.the problem was sometimesacademic-there were several occasionswhen the three&nensional stru&reofaprote&wassofved crystaUographicaflybefore knowledge of
its sequence.But today the genome pro@% are blasting us with sequencesof unknown structure, and a soiutlon has become important to a wide community. The general solution is to identify the conformation of minimum energy.There de at least two major obstacles to overcome. Rrst, an accurate description of the atom interactions is required. Second,there is an enormous search problem to identify the native conformation from the myriad of afternatives. Giventhese hurdles, as protein structures were revealed in the 197Os,many workers decided to ‘cheat’ and developed empirical schemesfor predictfon. Today,these are used widely in both secondary structure prediction and ln obtaining a tertiary model based on the determined coordinates of a homologous molecule. This book reports how the chafiengeof a generalsolution remains, and how
presentday computing power has stimulated the community to employ a variety of new approaches.it is a muftiauthor text covering a broad range of topics. The emphasisis on new solutions to old probim - effective potentials and the search algorithms. The recent applications of stat&-the-art atomic potentials to systemssuch as sidechain conformation and loop selectionare described. fn addition, the topical applications of pseudopotentials derived from statistlcaf analysisof known structures to distinguish between correctly and incorrectly folded structures am!reported. sevea new searcha@rlMnsaredescribed, including simulated allnabn& genetic algorithms, deadend efimination, branch-and-boundminimization and neuraf networks. Proteinfofds with characteristic second-a packingcan be generatedde R900using
329