title: On the entropy of protein folding.
abstract: The failure to appreciate that the hydration of polar groups is a major contribution to the entropy of protein unfolding has led to considerable underestimates for the loss of configurational freedom when a protein chain folds.
authors.affiliation: Department of Biology and Biocalorimetry Center, Johns Hopkins University, Baltimore, Maryland 21218, USA.
authors.forename: G I
authors.initials: GI
authors.lastname: Makhatadze
authors.forename: P L
authors.initials: PL
authors.lastname: Privalov
mesh_terms: D001426:Bacterial Proteins; D002151:Calorimetry; D008968:Molecular Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry; D012260:Ribonucleases / Q000737:chemistry / Q000378:metabolism; D013696:Temperature; D013816:Thermodynamics; D014452:Ubiquitins / Q000737:chemistry / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D011506:Proteins; D014452:Ubiquitins; D012260:Ribonucleases; C019760:Bacillus amyloliquefaciens ribonuclease