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Theoretical studies on the interaction of proteins with base pairs. I. Ab initio calculation for the effect of H‐bonding interaction of proteins on the stability of adenine–uracil pair
Author(s) -
Sarai Akinori,
Saito Minoru
Publication year - 1984
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.560250308
Subject(s) - uracil , hydrogen bond , ab initio , chemistry , base pair , base (topology) , groove (engineering) , crystallography , computational chemistry , hydrogen , chemical physics , molecule , dna , materials science , organic chemistry , biochemistry , mathematical analysis , mathematics , metallurgy
Abstract The hydrogen‐bonding interaction of protein with the adenine–uracil base pair was investigated by the ab initio MO method ( STO ‐3G level). We found that the stability of the base pair was greatly affected by the hydrogen‐bonding interaction of several residues of protein in different ways, depending on whether the interacting species is charged or neutral, whether the interaction is made from the major groove or minor groove side, and which of the two, adenine or uracil, is hydrogen bonded. These results were interpreted as the cooperative interaction between the base pair hydrogen bonds and external ones. The implications of the present results to biological functions were also discussed.