Electrostatic aspects of protein-protein interactions

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F B Sheinerman1, R Norel, B Honig

  • 1Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA. fbs5@columbia.edu

Current Opinion in Structural Biology
|April 8, 2000
PubMed

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Protein-protein Interfaces

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Protein-Protein Interfaces02:04

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Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation which is critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.Protein Structure Is Critical to Its Biological FunctionProteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...