C. M. Dobson, A. R. Fersht
Cambridge University Press, Aug 8, 1996 - Science - 119 pages
The ability of proteins to fold rapidly and efficiently into intricate and highly specific structures following their synthesis on ribosomes is an essential part of the conversion of genetic information into cellular activity. However, little is understood in detail of how this occurs. The Royal Society meeting on which this volume is based focused on the molecular basis of the folding processes and brought together a wide range of leading experimental and theoretical scientists in this field. This volume offers an authoritative collection of the foundations of current work. The first section discusses the experimental elucidation of the pathways of protein folding. The second section looks at theoretical approaches to folding, and the final group addresses the issue of how proteins fold in vivo. This volume will be of value to all those with an interest in protein folding, especially those in molecular biology, biochemistry and cell biology.
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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