Do All Backbone Polar Groups in Proteins Form Hydrogen Bonds?

Overview

Journal Protein Sci

Specialty Biochemistry

Date 2005 Jun 7

PMID 15937286

Citations 75

Authors

Patrick J Fleming

George D Rose

Affiliations

Soon will be listed here.

Abstract

Evidence from proteins and peptides supports the conclusion that intrapeptide hydrogen bonds stabilize the folded form of proteins. Paradoxically, evidence from small molecules supports the opposite conclusion, that intrapeptide hydrogen bonds are less favorable than peptide-water hydrogen bonds. A related issue-often lost in this debate about comparing peptide-peptide to peptide- water hydrogen bonds-involves the energetic cost of an unsatisfied hydrogen bond. Here, experiment and theory agree that breaking a hydrogen bond costs between 5 and 6 kcal/mol. Accordingly, the likelihood of finding an unsatisfied hydrogen bond in a protein is insignificant. This realization establishes a powerful rule for evaluating protein conformations.

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