Ananthanarayanan, VS and Brahmachari, Samir K and Pattabiramanc, N (1984) Proline-containing β-turns in peptides and proteins: Analysis of structural data on globular proteins. In: Archives of Biochemistry and Biophysics, 232, I (2). pp. 482-495.
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Tetrapeptide sequences of the type Z-Pro-Y-X were obtained from the crystal structure data on 34 globular proteins, and used in an analysis of the positional preferences of the individual amino acid residues in the Î²-turn conformation. The effect of fixing proline as the second position residue in the tetrapeptide sequence was studied by comparing the data obtained on the positional preferences with the corresponding data obtained by Chou and Fasman using the Z-R-Y-X sequence, where no particular residue was fixed in any of the four positions. While, in general, several amino acid residues having relatively very high or very low preferences for specific positions were found to be common to both the Z-Pro-Y-X and Z-R-Y-X sequences, many significant differences were found between the two sets of data, which are to be attributed to specific interactions arising from the presence of the proline residue.
|Item Type:||Journal Article|
|Additional Information:||Copyright for this article belongs to Elsevier science.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||22 Jan 2010 09:39|
|Last Modified:||19 Sep 2010 05:42|
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