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Structural and energetic basis of carbohydrate-aromatic packing interactions in proteins

Academic Article
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Overview

related to degree

  • Chen, Wentao, Ph.D. in Chemistry, Scripps Research 2010 - 2016

authors

  • Chen, Wentao
  • Enck, S.
  • Price, J. L.
  • Powers, D. L.
  • Powers, Evan
  • Wong, Chi-Huey
  • Dyson, Jane
  • Kelly, Jeffery

publication date

  • July 2013

journal

  • Journal of the American Chemical Society  Journal

abstract

  • Carbohydrate-aromatic interactions mediate many biological processes. However, the structure-energy relationships underpinning direct carbohydrate-aromatic packing interactions in aqueous solution have been difficult to assess experimentally and remain elusive. Here, we determine the structures and folding energetics of chemically synthesized glycoproteins to quantify the contributions of the hydrophobic effect and CH-π interactions to carbohydrate-aromatic packing interactions in proteins. We find that the hydrophobic effect contributes significantly to protein-carbohydrate interactions. Interactions between carbohydrates and aromatic amino acid side chains, however, are supplemented by CH-π interactions. The strengths of experimentally determined carbohydrate CH-π interactions do not correlate with the electrostatic properties of the involved aromatic residues, suggesting that the electrostatic component of CH-π interactions in aqueous solution is small. Thus, tight binding of carbohydrates and aromatic residues is driven by the hydrophobic effect and CH-π interactions featuring a dominating dispersive component.

subject areas

  • Carbohydrates
  • Hydrocarbons, Aromatic
  • Models, Molecular
  • Molecular Structure
  • Protein Folding
  • Proteins
  • Thermodynamics
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Identity

PubMed Central ID

  • PMC3715148

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja4040472

PubMed ID

  • 23742246
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Additional Document Info

start page

  • 9877

end page

  • 9884

volume

  • 135

issue

  • 26

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