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General properties of protein folding transitions
Experimental observations of protein unfolding and refolding
A general scheme for protein folding
21 other sections not shown
activity aggregation amide protons amino acid association barnase binding Biochem Biochemistry Biol Biophys BPTI catalysed cell Chem coli complex concentration conformation Creighton cysteine dehydrogenase denatured dimer dissociation disulfide bonds disulfide formation domain enzyme equilibrium Fersht fluorescence folding intermediates folding pathway folding reactions fully folded GdmCl GroEL GSSG helices hydrogen bonds hydrogen exchange hydrophobic inclusion body inhibitor interactions intramolecular involved isomers kinetic phases ligand lysozyme mechanism membrane mitochondrial molecular molecules molten globule monomers mutant native protein native structure native-like Natl non-native observed oxidative folding peptide polypeptide chain proline proline isomerization prolyl isomerase protein disulfide isomerase protein folding pulse rate constant recombinant redox redox buffer residues ribonuclease RNase secondary structure sequence side-chains slow folding slow phase slow refolding solubilization solvent species stability studies substrate subunits synthase temperature tertiary thermodynamic thiol thioredoxin time-scale tion transition translocation trypsin unfolded protein urea vitro vivo