title: Forces contributing to the conformational stability of proteins.
abstract: For 35 years, the prevailing view has been that the hydrophobic effect is the dominant force in protein folding. The importance of hydrogen bonding was always clear, but whether it made a net favorable contribution to protein stability was not. Studies of mutant proteins have improved our understanding of the forces stabilizing proteins. They suggest that hydrogen bonding and the hydrophobic effect make large but comparable contributions to the stability of globular proteins.
authors.affiliation: Department of Medical Biochemistry and Genetics, Texas A&M University, College Station 77843-1114, USA.
authors.forename: C N
authors.initials: CN
authors.lastname: Pace
authors.forename: B A
authors.initials: BA
authors.lastname: Shirley
authors.forename: M
authors.initials: M
authors.lastname: McNutt
authors.forename: K
authors.initials: K
authors.lastname: Gajiwala
mesh_terms: D006860:Hydrogen Bonding; D009154:Mutation; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D006163:Ribonuclease T1 / Q000737:chemistry; D013816:Thermodynamics
chemical_list: D006163:Ribonuclease T1