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The Use of Proton Chemical Shifts to Define the Solution Structure of a Dimeric Peptide
Author(s) -
Busetta Bernard,
Picard Philippe
Publication year - 1996
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.67
Subject(s) - chemical shift , dimer , proton , molecule , nuclear overhauser effect , chemistry , process (computing) , peptide , chemical physics , biological system , computer science , computational chemistry , combinatorial chemistry , physics , organic chemistry , nuclear physics , biochemistry , biology , operating system
Abstract For flexible peptides, nuclear Overhauser Effects (NOE) experiments do not provide enough information to ensure a correct definition of their solution structure. The use of distance constraints, derived from the knowledge of proton chemical shifts, is developed to restrict the number of possible conformations. In the case of flexible molecules, randomization appears as an important factor of the correct estimation of the chemical shifts from the 3D structure. The refinement of the solution structure of the highly flexible AVP‐like parallel dimer is described to illustrate this process.