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Published online before print June 3, 2005, 10.1110/ps.051454805
Protein Science (2005), 14:1911-1917. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society
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FOR THE RECORD

Do all backbone polar groups in proteins form hydrogen bonds?

Patrick J. Fleming and George D. Rose

T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218, USA

(RECEIVED March 10, 2005; FINAL REVISION April 5, 2005; ACCEPTED April 5, 2005)

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.

Keywords: protein hydrogen bonds; protein stability; hydrogen bond satisfaction; protein folding

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051454805.

Reprint requests to: George D. Rose, Jenkins Department of Biophysics, Johns Hopkins University, 3400 N. Charles Street, Baltimore, MD 21218, USA; e-mail: grose{at}jhu.edu; fax: (410) 516-4118.


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