Conserved thermodynamic contributions of backbone hydrogen bonds in a protein fold
Conserved thermodynamic contributions of backbone hydrogen bonds in a protein fold
Engineering Village 2
? 2006 Elsevier Inc
Accession number: 8922021
Title: Conserved thermodynamic contributions of backbone hydrogen bonds in a protein fold
Authors: Wang, M.1 ; Wales, T.E.1 ; Fitzgerald, M.C.1
Author affiliation: 1 Dept. of Chem., Duke Univ., Durham, NC, USA
Serial title: Proceedings of the National Academy of Sciences of the United States of America
Abbreviated serial title: Proc. Natl. Acad. Sci. USA (USA)
Volume: 103
Issue: 8
Publication date: 21 Feb. 2006
Pages: 2600-4
Language: English
ISSN: 0027-8424
CODEN: PNASA6
Document type: Journal article (JA)
Publisher: National Academy of Sciences of the United States of America
Country of publication: USA
Material Identity Number: P030-2006-013
Abstract: Backbone-backbone hydrogen-bonding interactions are a ubiquitous and highly conserved structural feature of proteins that adopt the same fold (i.e., have the same overall backbone topology). This work addresses the question of whether or not this structural conservation is also reflected as a thermodynamic conservation. Reported here is a comparative thermodynamic analysis of backbone hydrogen bonds in two proteins that adopt the same fold but are unrelated at the primary amino acid sequence level. With amide-to-ester bond mutations introduced by total chemical synthesis methods, the thermodynamic consequences of backbone-backbone hydrogen-bond deletions at five different structurally equivalent positions throughout the ?-a-a fold of Arc represser and CopG were assessed. The ester bond-containing analogues all folded into native-like three-dimensional structures that were destabilized from 2.5 to 6.0 kcal/(mol dimer) compared with wild-type controls. Remarkably, the five paired analogues with amide-to-ester bond mutations at structurally equivalent positions were destabilized to exactly the same degree, regardless of the degree to which the mutation site was buried in the structure. The results are interpreted as evidence that the thermodynamics of backbone-backbone hydrogen-bonding interactions in a protein fold are conserved
Number of references: 30
Inspec controlled terms: biochemistry - cellular biophysics - hydrogen bonds - macromolecules - molecular biophysics - proteins - thermodynamic properties
Uncontrolled terms: thermodynamic conservation - protein fold - backbone-backbone hydrogen-bonding interactions - primary amino acid sequence level - amide-to-ester bond mutations - chemical synthesis methods - Arc represser - CopG system
Inspec classification codes: A8715B Biomolecular structure, configuration, conformation, and active sites - A8715K Biomolecular interactions, charge transfer complexes - A8725 Cellular biophysics - A8715D Physical chemistry of biomolecular solutions; condensed states - A3620H Macromolecular configuration (bonds, dimensions)
Treatment: Experimental (EXP)
Discipline: Physics (A)
DOI: 10.1073/pnas.0508121103
Database: Inspec
Copyright 2006, The Institution of Engineering and Technology
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