Polypeptide models of collagen. II. Solution properties of (Pro‐Gly‐Phe)_n Journal Articles

abstract

• AbstractThe 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‐R2‐R3, in collagen.

authors

• Brahmachari, Samir K
• Ananthanarayanan, Vettai
• Rapaka, Rao S
• Bhatnagar, Rajendra S

status

• published 

publication date

• September 1978

has subject area

• Amino Acid Sequence (MeSH)
• Biophysics (Science Metrix)
• Collagen (MeSH)
• Models, Chemical (MeSH)
• Peptides (MeSH)
• Protein Conformation (MeSH)
• Solutions (MeSH)

published in

• Biospectroscopy  Journal

keywords

• Amino Acid Sequence
• Collagen
• Models, Chemical
• Peptides
• Protein Conformation
• Solutions

Digital Object Identifier (DOI)

• 10.1002/bip.1978.360170905

PubMed ID

• 698352

start page

• 2097

end page

• 2105

volume

• 17

issue

• 9