Kolaskar, AS and Ramabrahmam, V and Soman, KV (1980) Reversals of polypeptide chain in globular proteins. In: International Journal of Peptide and Protein Research, 16 (1). pp. 1-11.Full text not available from this repository.
A simple algorithm has been developed to detect β-bends and 'loops'-chain reversals containing five amino acid residues, using only coordinates of Cα-atoms from crystal structure data of globular proteins using the above algorithm. Analysis of bends have showed that the total number of bends in each protein (TB) is linearly related to total number of non-hydrophobic residues in that protein which in turn is related linearly to total number of amino acid residues. Secondly, we found that a large number of consecutive bends occur in each protein which give rise to on an average only three independent residues per turn. Positional preference of amino acid residues in chain reversals is stressed. Consideration of pairs of amino acid residues in positions (i + 1) and (i + 2) of bends seems to provide a more reliable basis for predicting chain reversals in proteins.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to John Wiley & Sons, Inc.|
|Keywords:||β-bends and "loops" • polypeptide chain reversals • protein data analysis|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||04 Feb 2010 11:30|
|Last Modified:||04 Feb 2010 11:30|
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