Mechanisms of Protein Folding
Roger H. Pain
Oxford University Press, 2000 - Medical - 433 pages
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.
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The nature and significance of protein folding
Strategies for studying protein folding
Energy surfaces for protein folding
27 other sections not shown
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a-lactalbumin acid activity aggregation amide protons amyloid apoMb apomyoglobin assembly barnase binding Biochemistry Biol BPTI burst-phase C-terminal catalysis cell chaperonin characterization Chem circular dichroism coli collagen compact cyclophilin cytochrome cytosol denatured dimeric disulphide bonds DnaK Dobson domain dynamics ensemble enzyme equilibrium Fersht fibrils FKBP fluorescence folding funnel 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 Kuwajima ligand lysozyme mechanism membrane molecular chaperones molecules molten globule mutations native native-like Natl Acad Nature Struct non-native nucleation o-LA observed partially folded peptide bonds polypeptide polypeptide chain Proc proline prolyl isomerase protein folding rate constants refolding residues ribonuclease RNase Schmid secondary structure sequence simulations solvent species stability stopped-flow studies substrate subunits tailspike temperature tertiary tertiary structure thiol trans trigger factor two-state unfolded protein vitro vivo wild-type