Abstract
The disposition of conformationally stanch, helix-prone tetrapeptides and of longer segments containing them in proteins of different structural and functional groups (PDBselect and CATH samples) has been analyzed. Quasirandom Monte Carlo experiments show that the disposition of such segments can be regarded as stochastic. At that, ∼60% of stanch peptides in the protein globules have at least one stanch neighbor within 5 Å.
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Abbreviations
- CSOP:
-
conformationally stanch oligopeptide
- MC:
-
Monte Carlo
- MISD:
-
mean intersegment distance
- NIAD:
-
nearest interatomic distance
- SoN:
-
size of the neighborhood
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Original Russian Text © A.V. Batyanovskii, N.G. Esipova, S.E. Shnoll, 2009, published in Biofizika, 2009, Vol. 54, No. 6, pp. 1137–1143.
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Batyanovskii, A.V., Esipova, N.G. & Shnoll, S.E. Mutual disposition of short conformationally stanch oligopeptides in the 3D structure of globular proteins. BIOPHYSICS 54, 748–752 (2009). https://doi.org/10.1134/S0006350909060153
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DOI: https://doi.org/10.1134/S0006350909060153