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The path of a protein chain can be approximated by the conformation dictated by interpeptide ionic bridges
Author(s) -
Lim Valery I.,
Venclovas Česlovas,
Kurochkitalya A.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80284-n
Subject(s) - ionic bonding , chemistry , chain (unit) , path (computing) , side chain , peptide , proton , protein structure , crystallography , stereochemistry , ion , biochemistry , physics , computer science , organic chemistry , astronomy , programming language , polymer , quantum mechanics
A stereochemical simulation of the formation of ionic bridges between adjacent peptide groups along the polypeptide chain has been made. Such ionic bridges constrain the amino‐acid residues into eight conformations. It is shown that the path of any protein‐chain fragment 10–15 residues long can be approximated well by these conformations. This suggests that the conformations dictated by the ionic bridges can be used as blocks in the formation of the spatial proton structure.