Overview

This volume offers a collection of articles written by speakers at the 68th Annual Symposium of the Biochemical Society held at the University of Leeds in April 2000. The articles present an up-to-date view of protein folding ""in vitro"" and ""in vivo"", the role of chaperones in folding, and the consequences of protein misfolding, for example in amyloid diseases. In addition, simulations of folding mechanisms, protein design principles, and protein engineering to produce novel enzymes are discussed. The chapters highlight successes in these areas, and point the way forward in these disciplines. The articles describe the biology of a yeast prion, using techniques spanning structural biology to yeast genetics to reveal how this protein can cause the inheritance of new traits and explains some of the amazing feats by which protein folding is chaperoned in cells. They also provide guidelines for the assembly of novel coiled-coil structures and highlights how environmental screening has been used to produce new enzymes capable of reducing nitrate esters and theire use in the degradation of explosives. In addition, the approaches of DNA shuffling and phage display and their use in the creation of evolved protease inhibitors and tackles the immensely complex biological and biophysical problem of how a membrane protein folds are examined.

Full Product Details

Author:   A. Berry ,  S. Radford
Publisher:   Portland Press
Imprint:   Portland Press
Volume:   v. 68
Dimensions:   Width: 15.50cm , Height: 1.30cm , Length: 23.00cm
Weight:   0.408kg
ISBN:  

9781855781436

ISBN 10:   1855781433
Pages:   156
Publication Date:   20 January 2001
Audience:   College/higher education ,  Professional and scholarly ,  Undergraduate ,  Postgraduate, Research & Scholarly
Format:   Hardback
Publisher's Status:   Active
Availability:   In Print  
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Table of Contents

The structural basis of protein folding and its links with human with human disease By C.M Dobson * Manipulating the folding of membrane proteins: using the bilayer to our advantage By P.J. Booth, A.R. Curran, R.H. Templer, H. Lu and W. Meijberg * Self-perpetuating changes in Sup35 protein conformation as a mechanism of heredity in yeast By T.R. Serio, A.G. Cashikar, A.S. Kowal, G.J. Sawicki and S.L. Lindquist * Contribution of molecular chaperones to protein folding in the cytoplasm of prokaryotic and eukaryotic cells By D.J. Naylor and F.-Y. Hartl * Defining the structure of the substrate-free state of the DnaK molecular chaperone By J.F. Swain, R. Sivendran and L.M. Gierasch * Validation of protein-unfolding transition states identified in molecular dynamics simulations By Valerie Daggett * Structure, stability and folding of the a -helix By A.J. Doig, C.D. Andrew, D.A.E. Cochran, E. Hughes, S. Penel, J.K. Sun, B.J. Stapley, D.T. Clarke, G.R. Jones * Guidelines for the assembly of novel coiled-coil structures: a-sheets and a -cylinders By J. Walshaw, J.M. Shipway and D.N. Woolfson * Protease inhibitors and directed evolution: enhancing plant resistance to nematodes By M.J. McPherson and D.J. Harrison * Degradation of explosives by nitrate ester reductases By R.E. Williams, D.A. Rathbone, P.C.E. Moody, N.S. Scrutton and N.C. Bruce

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