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On the importance of amino acid sequence and spatial proximity of interacting residues for protein folding

Simon Mitternacht1, Igor N Berezovsky

  • 1Department of Informatics, University of Bergen, Bergan, Norway. Igor.Berezovsky@uni.no

Journal of Biomolecular Structure & Dynamics
|December 15, 2010
PubMed
Abstract

No abstract available in PubMed .

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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, 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.
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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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