C. M. Dobson, A. R. Fersht
Cambridge University Press, Aug 8, 1996 - Science - 119 pages
A discussion organized and edited by C. M. Bobson and A. R. Fersht. Disulphide-coupled protein folding pathways. (T. Creighton). Mapping the structures of transition states and intermediates in folding: delineation of pathways at high resolution. (A. R. Fersht). Insights into protein folding using physical techniques: studies of lysozyme and a-lactalbumin. (Sheena E. Radford and Christopher M. Dobson). Initial studies of the equilibrium folding pathway of staphysilococcal nuclease. (Yi Wang, Andrei T. Alexandrescu and David Shortle). Kinetic and equilibrium folding intermediates. (O. B. Ptitsyn, V. E. Bychkova and V, N, Uversky). Does the molten globule have a native-like tertiary fold? (Zheng-Yu Peng, Lawren C. Wu, Brenda A. Schulman and Peter S. Kim). Investigation of protein unfolding and stability by computer simulation. (W. F. van Gunsteren, P. H. Hunenberber, H. Kovacs, A. E. Mark and C. A. Schiffer). Models of cooperativity in protein folding. (Hue Sun Chan, Sarina Bromberg and Ken A. Dill). Protein folds: towards understanding folding from inspection of native structures. (Janet M. Thornton, david T. Jones, Malcolm W. MacArthur, Christine M. Orengo and Mark B. Swindells). Design of two-stranded and three-stranded coiled-coil peptides. (Stephen Betz, Robert Fairman, Karyn O'Neil, james Lear and Willian DeGrado). Nascent chains: folding and chaperone interaction during elongation on ribosomes. (Kostas Tokatlidis, Bertrand Friguet, Dominique Deville-Bonne, François Baleux, Alexey N. Fedorov, Amiel Navon, Lisa Djavadi-Ohaniance and Michel E. Goldberg). Folding and association versus misfolding and aggregation of proteins. (Rainer Jaenicke). Principles of chaperone-mediated protein folding. (F. Ulrich Hartl). Unliganded GroEL at 2.8 A: structure and functional implications. (Paul B. Sigler and Arthur L. Horwich).
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Disulphidecoupled protein folding pathways
delineation of pathways at high resolution
studies of lysozyme and 𝛼lactalbumin
Initial studies of the equilibrium folding pathway of staphylococal nuclease
Kinetic and equilibrium folding intermediates
Does the molten globule have a nativelike tertiary fold?
Investigation of protein unfolding and stability by computer simulation
Models of cooperativity in protein folding
towards understanding folding from inspection of native structures
Design of twostranded and threestranded coiledcoil peptides
folding and chaperone interaction during elongation on ribosomes
Folding and association versus misfolding and aggregation of proteins
Principles of chaperonemediated protein folding
structure and functional implications
a-domain a-LA a-lactalbumin a/coil aggregation Alexandrescu alpha helix amino acid antibody apical domain barnase binding Biochemistry Biochemistry 32 Biol bovine pancreatic trypsin BPTI chaperonin Chem coiled coils coiled-coil collapse concentration conformation cooperativity Creighton denatured Dill dimer disulphide bonds DnaK Dobson equilibrium experimental FEBS Lett Fersht figure folding intermediates folding pathway folding process formation free energy function GdmCl globular proteins glycerol GroEL GroES Gunsteren Hartl helical helix hen lysozyme hydrogen exchange hydrophobic core interactions Jaenicke kinetic Kuwajima lysozyme molec molecular chaperones molten globule monomer mutations nascent chains native disulphide native protein native-like natn nuclease one-state packing pancreatic trypsin inhibitor peptide polypeptide chain propensities protein folding protein structure Ptitsyn Radford refolding residues ribosome-bound ribosomes secondary structure sequence Shortle sidechain simulation solution solvent SP-C specific stability struct studies subunits tailspike temperature tertiary tertiary structure transition trimer two-state unfolded urea Uversky vitro vivo