My 65 years in protein chemistry.

摘要: This is a tour of physical chemist through 65 years protein chemistry from the time when emphasis was placed on determination size and shape molecule as colloidal particle, with an early breakthrough by James Sumner, followed Linus Pauling Fred Sanger, that real molecule, albeit macromolecule. It deals recognition nature importance hydrogen bonds hydrophobic interactions in determining structure, properties, biological function proteins until present acquisition understanding thermodynamics, folding pathways linear array amino acids to entity. Along way, combination experiment theoretical interpretation, mechanism elucidated for thrombin-induced conversion fibrinogen fibrin blood clot oxidative-folding ribonuclease A. Before atomic structure determined x-ray diffraction or nuclear magnetic resonance spectroscopy, experimental studies fundamental underlying led several distance constraints which motivated approach determine culminated Empirical Conformational Energy Program Peptides (ECEPP), all-atom force field, structures fibrous collagen-like 46-residue globular staphylococcal A were determined. To undertake study larger proteins, physics-based coarse-grained UNited-RESidue (UNRES) field developed, applied protein-folding problem terms dynamics, pathways. Initially, single-chain and, ultimately, multiple-chain examined, methodology extended protein–protein nucleic protein–nucleic acid interactions. The ultimate results variety processes natural disease phenomena.