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Polypeptide models of collagen. II. Solution properties of (Pro-Gly-Phe)n

✍ Scribed by Samir K. Brahmachari; V. S. Ananthanarayanan; Rao S. Rapaka; Rajendra S. Bhatnagar

Publisher
Wiley (John Wiley & Sons)
Year
1978
Tongue
English
Weight
483 KB
Volume
17
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

The conformation of (Pro‐Gly‐Phe)~n~ in trifluoroethanol was investigated using CD, nmr and ir techniques. After making appropriate correction for the contribution of the phenylalanine chromophore to the observed CD spectra of the polytripeptide at several temperatures, it is found that (Pro‐Gly‐Phe)~n~ can exist in a partially triple‐helical conformation in this solvent a t low temperatures. The nmr and ir data support this conclusion. In conjunction with recent theoretical sutdies, our data offer an explanation for the preferential occurrence of the Phe residue in position 2 of the tripeptide sequence Gly‐R~2~‐R~3~, in collagen.

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