Mechanisms of Protein FoldingRoger H. Pain The process by which newly synthesized polypeptide chains become their final 3-dimensional protein forms is clearly explained, providing students and researchers of various backgrounds with both a conceptual and technical understanding of the subject. The new Second Edition incorporates the significant improvements in the field such as advances in interpreting observed kinetic data, the development of technology to observe fast folding reactions, the molten globule state, and the vital role of chaperone proteins in protein folding. The emphasis on experimental approaches has been maintained but this edition does so within the explicit context of simulations and energy surfaces. New discoveries of the central importance of protein folding and unfolding reactions in biology and medicine (including mutation and 'misfolding') are carefully explored. Three case studies elucidate the difficulties of studying protein folding in vivo. |
Contents
The conformational properties of polypeptide chains | 3 |
Results from experimental studies of folding | 10 |
A unified view of protein folding | 18 |
Copyright | |
33 other sections not shown
Other editions - View all
Common terms and phrases
a-lactalbumin aggregation amide protons amino acids amyloid apoMb apomyoglobin assembly barnase binding Biochemistry Biol BPTI C-terminal catalysis cell chaperonin characterization Chem circular dichroism coli collagen compact complex cyclophilin cytochrome denatured dimeric disulphide bonds Dobson domain dynamics ensemble enzyme equilibrium experimental Fersht fibrils FKBP fluorescence folding intermediates folding kinetics folding pathway folding process folding reaction formation free energy function GdmCl GroEL haem helices helix hydrogen exchange hydrophobic inhibitor interactions isomerization ligand lysozyme mechanism membrane molecular chaperones molecules molten globule mutations native native-like Natl Acad Nature Struct non-native nucleation observed partially folded peptide bonds polypeptide polypeptide chain Proc proline prolyl isomerase protein folding rate constants refolding residues ribonuclease RNase Schmid secondary structure sequence side-chains simulations solvent species stability stopped-flow studies substrate subunits tailspike temperature tertiary tertiary structure thiol trans transition trigger factor trimer triple-helix two-state unfolded protein vitro vivo wild-type