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Siemion IZ, Folkers G, Szewczuk Z, et al. Peptides related to the active fragment of "proline rich polypeptide", an immunoregulatory protein of the ovine colostrum. Spectroscopic and computer modeling studies. Int J Pept Protein Res. 1990;36(6):506-14
Siemion, I. Z., Folkers, G., Szewczuk, Z., Jankowski, A., Kubik, A., & Voelter, W. (1990). Peptides related to the active fragment of "proline rich polypeptide", an immunoregulatory protein of the ovine colostrum. Spectroscopic and computer modeling studies. International journal of peptide and protein research, 36(6), 506-14.
Siemion, I Z, et al. "Peptides related to the active fragment of "proline rich polypeptide", an immunoregulatory protein of the ovine colostrum. Spectroscopic and computer modeling studies." International journal of peptide and protein research vol. 36,6 (1990): 506-14.
Siemion IZ, Folkers G, Szewczuk Z, Jankowski A, Kubik A, Voelter W. Peptides related to the active fragment of "proline rich polypeptide", an immunoregulatory protein of the ovine colostrum. Spectroscopic and computer modeling studies. Int J Pept Protein Res. 1990 Dec;36(6):506-14. PMID: 2090642.
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Int J Pept Protein Res. 1990 Dec;36(6):506-14.

Peptides related to the active fragment of "proline rich polypeptide", an immunoregulatory protein of the ovine colostrum. Spectroscopic and computer modeling studies.

International journal of peptide and protein research

I Z Siemion, G Folkers, Z Szewczuk, A Jankowski, A Kubik, W Voelter

Affiliations

  1. Institute of Chemistry, Wroclaw University, Poland.

PMID: 2090642

Abstract

The preferred solution conformation of the PRP-hexapeptide (Tyr-Val-Pro-Leu-Phe-Pro) and of some of its structural analogues was investigated by NMR-spectroscopy, spectrofluorimetry and computer simulation technic. It was found that the preferred conformation is characterized by cis'-conformation of Pro3 and the gamma-turn on the Leu4-residue: for Val2 and Phe5 a beta-structure seems to be privileged. In such a conformation Val2 and Leu4 residues occupy exactly the same positions in space as residues i and i + 3 in an alpha-helix. It suggests that the PRP-hexapeptide can interact with receptor protein inducing or stabilizing its helical conformation by "knobs into holes" packing.

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