Context-dependent secondary structure formation of a designed protein sequence

Article Abstract:

Non-local interactions influence the alpha-helix and the beta-sheet secondary structures of peptide sequences. Protein folding that helps tertiary interactions also affect the structure. Eleven amino-acid sequences, termed the chameleon sequence, were designed and examined for the formation of a secondary structure. Biophysical analysis reveals that chameleon-alpha and chameleon-beta have structures similar to that of the native immunoglobulin G-binding domain of protein G.

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Jury returns on structure prediction

Article Abstract:

Comparison of the structure of Src-homology 3 (SH3) domain derived theoretically by S.A. Benner and his colleagues with the structure found by crystallography shows that the ETH structure prediction method used was accurate in predicting secondary structure, and wrong about tertiary structure. An electronic mail address is given for researchers who wish to submit sequences. Blind predictions of secondary structure will be returned.

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Globin fold in a bacterial toxin

Article Abstract:

Colicin A, a bacterial toxin, contains a membrane-insertion domain whose six alpha-helices and one turn of 3-10-helix are nearly identical to the globin fold's structure. This similarity was determined by using an algorithm to compare over 150 protein tertiary structures. Colicin A's resemblance to globin fold proves that three-on-three helical layering is a basic structural pattern of proteins.

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