Hydrogen bonding stabilizes globular proteins.
It is clear that intramolecular hydrogen bonds are essential to the structure and stability of globular proteins. It is not clear, however, whether they make a net favorable contribution to this stability. Experimental and theoretical studies are at odds over this important question. Measurements of the change in conformational stability, delta (delta G), for the mutation of a hydrogen bonded residue to one incapable of hydrogen bonding suggest a stabilization of 1.0 kcal/mol per hydrogen bond. If the delta (delta G) values are corrected for differences in side-chain hydrophobicity and conformational entropy, then the estimated stabilization becomes 2.2 kcal/mol per hydrogen bond. These and other experimental studies discussed here are consistent and compelling: hydrogen bonding stabilizes globular proteins.
Department of Medical Biochemistry, Texas A & M University, College Station 77843-1114, USA.
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D017122:Bacteriophage T4 / Q000201:enzymology; D002151:Calorimetry; D006860:Hydrogen Bonding; D008836:Micrococcal Nuclease / Q000737:chemistry; D008962:Models, Theoretical; D009113:Muramidase / Q000737:chemistry; D016297:Mutagenesis, Site-Directed; D017354:Point Mutation; D011487:Protein Conformation; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D013816:Thermodynamics
D011506:Proteins; D011994:Recombinant Proteins; D008836:Micrococcal Nuclease; D009113:Muramidase