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Conserved thermodynamic contributions of backbone hydrogen bonds in a protein fold.

Publication ,  Journal Article
Wang, M; Wales, TE; Fitzgerald, MC
Published in: Proceedings of the National Academy of Sciences of the United States of America
February 2006

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 beta-alpha-alpha fold of Arc repressor 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.

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Published In

Proceedings of the National Academy of Sciences of the United States of America

DOI

EISSN

1091-6490

ISSN

0027-8424

Publication Date

February 2006

Volume

103

Issue

8

Start / End Page

2600 / 2604

Related Subject Headings

  • Thermodynamics
  • Repressor Proteins
  • Proteins
  • Protein Folding
  • Protein Conformation
  • Molecular Sequence Data
  • Models, Molecular
  • Hydrogen Bonding
  • Amino Acid Sequence
 

Citation

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Wang, M., Wales, T. E., & Fitzgerald, M. C. (2006). Conserved thermodynamic contributions of backbone hydrogen bonds in a protein fold. Proceedings of the National Academy of Sciences of the United States of America, 103(8), 2600–2604. https://doi.org/10.1073/pnas.0508121103
Wang, Min, Thomas E. Wales, and Michael C. Fitzgerald. “Conserved thermodynamic contributions of backbone hydrogen bonds in a protein fold.Proceedings of the National Academy of Sciences of the United States of America 103, no. 8 (February 2006): 2600–2604. https://doi.org/10.1073/pnas.0508121103.
Wang M, Wales TE, Fitzgerald MC. Conserved thermodynamic contributions of backbone hydrogen bonds in a protein fold. Proceedings of the National Academy of Sciences of the United States of America. 2006 Feb;103(8):2600–4.
Wang, Min, et al. “Conserved thermodynamic contributions of backbone hydrogen bonds in a protein fold.Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 8, Feb. 2006, pp. 2600–04. Epmc, doi:10.1073/pnas.0508121103.
Wang M, Wales TE, Fitzgerald MC. Conserved thermodynamic contributions of backbone hydrogen bonds in a protein fold. Proceedings of the National Academy of Sciences of the United States of America. 2006 Feb;103(8):2600–2604.
Journal cover image

Published In

Proceedings of the National Academy of Sciences of the United States of America

DOI

EISSN

1091-6490

ISSN

0027-8424

Publication Date

February 2006

Volume

103

Issue

8

Start / End Page

2600 / 2604

Related Subject Headings

  • Thermodynamics
  • Repressor Proteins
  • Proteins
  • Protein Folding
  • Protein Conformation
  • Molecular Sequence Data
  • Models, Molecular
  • Hydrogen Bonding
  • Amino Acid Sequence