Summary
1. The conformational states of glycine residues — R, B, L, P — in the low-energy forms of the tripeptides (I–III) are found with equal frequency.
2. The conformations of the main chain in sections of protein with glycine residues correspond to the preferred forms of the tripeptide fragments (I–III).
3. The close-, medium-, and long-range interactions in proteins do not contradict one another and exist at the favorable forms of the main chain.
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M. M. Shemyakin Institute of Bioorganic Chemistry, Academy of Sciences of the USSR. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 631–637, September–October, 1975.
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Pletnev, V.Z., Kadymova, F.A. & Popov, E.M. Theoretical conformational analysis of tripeptides with a glycine residue. Chem Nat Compd 11, 660–665 (1975). https://doi.org/10.1007/BF00567707
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DOI: https://doi.org/10.1007/BF00567707