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Polypeptide models of collagen. II. Solution properties of (Pro‐Gly‐Phe) n
Author(s) -
Brahmachari Samir K.,
Ananthanarayanan V. S.,
Rapaka Rao S.,
Bhatnagar Rajendra S.
Publication year - 1978
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1978.360170905
Subject(s) - chemistry , tripeptide , chromophore , residue (chemistry) , stereochemistry , sequence (biology) , phenylalanine , solvent , crystallography , peptide , amino acid , organic chemistry , biochemistry
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.