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Evaluation of a carbohydrate-pi interaction in a peptide model system

Sarah E Kiehna1, Zachary R Laughrey, Marcey L Waters

  • 1Department of Chemistry, CB 3290, University of North Carolina, Chapel Hill, NC 27599, USA.

Chemical Communications (Cambridge, England)
|October 4, 2007
PubMed

Abstract:

A carbohydrate-pi interaction contributes -0.8 kcal mol(-1) to the stabilization of a beta-hairpin peptide.

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Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
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Peptide Bonds

A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...

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