Computational identification of residues that modulate voltage sensitivity of voltage-gated potassium channels.

ABSTRACT:

Background

Studies of the structure-function relationship in proteins for which no 3D structure is available are often based on inspection of multiple sequence alignments. Many functionally important residues of proteins can be identified because they are conserved during evolution. However, residues that vary can also be critically important if their variation is responsible for diversity of protein function and improved phenotypes. If too few sequences are studied, the support for hypotheses on the role of a given residue will be weak, but analysis of large multiple alignments is too complex for simple inspection. When a large body of sequence and functional data are available for a protein family, mature data mining tools, such as machine learning, can be applied to extract info

SUBMITTER: Li B 

PROVIDER: S-EPMC1208917 | biostudies-literature | 2005 Aug

REPOSITORIES: biostudies-literature