Classification of protein folds.
The diversity and complexity of bioinformatics tools currently available for protein sequence analysis can make it difficult to know where to begin when presented with a new sequence. In this article, we present a protocol outlining one approach to sequence analysis that should give as comprehensive a picture as possible as to the likely structure and function of a protein given the limits of available tools. We also provide worked examples showing how these tools can have an impact on the understanding of protein function prior to experimental studies.
Russell
Robert B
RB
Structural Bioinformatics, EMBL, Meyerhofstrasse 1, Heidelberg, Germany. russell@embl.de
D000262:Adenylyl Cyclases / Q000737:chemistry; D000818:Animals; D005964:Glucosyltransferases / Q000737:chemistry; D006801:Humans; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000145:classification*; D020539:Sequence Analysis, Protein / Q000379:methods*
D011506:Proteins; D005964:Glucosyltransferases; D000262:Adenylyl Cyclases