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Site-specific relaxation of peptide bond planarity induced by electrically attracted proton/deuteron observed by neutron crystallography

Chiba, Kaori*; Matsui, Takuro*; Chatake, Toshiyuki*; Ohara, Takashi   ; Tanaka, Ichiro*; Yutani, Katsuhide*; Niimura, Nobuo*

In structural biology, peptide bonds, fundamental linkages between hundreds of amino acids, of which a protein molecule is composed, have been commonly treated as a plane structure just as Linus Pauling et al. proposed. In this paper, a site-specific peptide bond relaxation mechanism by deuterons whose localization has been suggested by neutron crystallography is proposed. A comprehensive study using X-ray and neutron diffraction and $$^{15}$$N chemical shifts of individual amide nitrogen atoms within the same peptide bond strongly suggests the relaxation of the electronic resonance structure because of site-specific modulation by protons/deuterons localized on the electron orbital of the carbonyl oxygen.

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Category:Biochemistry & Molecular Biology

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