Protein Structure, Stability, and Folding
Kenneth P. Murphy
Springer Science & Business Media, 2001 - Science - 252 pages
With the huge increase in available data on the DNA sequences of proteins, there is a growing need to understand and characterize how proteins fold into their biologically active native states and the basis for the stability of these states. In Protein Structure, Stability, and Folding, Kenneth P. Murphy and a panel of internationally recognized investigators describe some of the newest experimental and theoretical methods for investigating these critical events and processes. Among the techniques discussed are the many methods for calculating aspects of protein stability and dynamics from knowledge of the structure, for calculating conformational entropy, and for performing molecular dynamics simulations of protein unfolding. New experimental approaches presented include the use of co-solvents, novel applications of hydrogen exchange techniques, temperature-jump methods for looking at folding events, and new strategies for mutagenesis experiments. Unique in its powerful combination of theory and practice, Protein Structure, Stability, and Folding offers protein and biophysical chemists the means to gain a more comprehensive understanding of this complex area by detailing many of the major innovative techniques in use today.
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Acad alanine amide protons amino acids analysis approach atoms barnase binding Biochemistry Biol calculated Chem chymotrypsin chymotrypsin inhibitor conformational entropy conformational stability contributions denatured edited energetics ensemble enthalpy entropy change equilibrium estimate EX1-type exchange experimental experiments Fersht fluorescence folding pathway folding process folding/unfolding formation free energy Freire function g°tr Gibbs energy groups H/D exchange hairpin helices helix Hilser hydrogen bonding hydrogen exchange hydrophobic effect interactions kcal/mol kinetics laser temperature-jump ligand lysozyme measured molecular dynamics molecular dynamics simulations molecules Murphy mutations native protein Natl osmolyte osmolyte solution peptide backbone predicted probe Proc proline protein folding protein stability Protein Structure pulse rate constant region residues sample secondary structure sequence SH3 domain side chains solvation solvent stability constants Struct structure-based studies syringe tein temperature thermodynamic Timasheff tion transfer Gibbs energy transition ture turn two-state urea values