Usha, R and Murthy, MRN (1986) Protein structural homology: A metric approach. In: International Journal of Peptide and Protein Research, 28 (4). pp. 364-369.Full text not available from this repository. (Request a copy)
The flexibility of the polypeptide fold of proteins is essentially due to the rotational freedom about the main chain bonds involving Ca atoms. The polypeptide fold can therefore be represented by virtual bonds joining consecutive Ca atoms. The ordered sequence of virtual torsion and bond angles involving these bonds can be used to specify the fold. Such representations can then be compared to reveal structural similarities using the S. B. Needleman and C. D. Wuensch (1970) algorithm, which has been developed from comparison of amino acid sequences. Such an approach is presented and illustrated with examples. The method is suitable for detecting structural similarities that extend over 7 or more residues.
|Item Type:||Journal Article|
|Additional Information:||Copyright belongs to Munksgaard International Publishers Ltd.|
|Department/Centre:||Division of Chemical Sciences > Organic Chemistry|
|Date Deposited:||17 Apr 2008|
|Last Modified:||27 Aug 2008 13:19|
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