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Sequence and Structure Conservation in a Protein Core by Michael A. Rodionov; Tom L. Blundell is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Sequence and Structure Conservation in a Protein Core about?

In order to study structural aspects of sequence conservation in families of homologous proteins, we have analyzed structurally aligned sequences of 585 proteins grouped into 128 homologous families. The conservation of a residue in a family is defined as the average residue similarity in a given position of aligned sequences. The residue similarities were expressed in the form of log-odd substitution tables that take into account the environments of amino acids in three-dimensional structures. The protein core is defined as those residues that have less then 7% solvent accessibility. The density of a protein core is described in terms of atom packing, which is investigated as a criterion for residue substitution and conservation. Although there is no significant correlation between sequence conservation and average atom packing around nonpolar residues such as leucine, valine and isoleucine, a significant correlation is observed for polar residues in the protein core. This may be explained by the hydrogen bonds in which polar residues are involved; the better their protection from water access the more stable should be the structure in that position. Proteins

Who reads Sequence and Structure Conservation in a Protein Core?

Author

Michael A. Rodionov; Tom L. Blundell

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

1998

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)