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Protein–Nucleic acid interactions: Investigations on the peptide backbone interaction with polynucleotides
Author(s) -
Hosur Ramakrishna V.,
Kumar N. Vasanth,
Govil Girjesh
Publication year - 1981
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.560200103
Subject(s) - polynucleotide , nucleic acid , hydrogen bond , chemistry , peptide nucleic acid , peptide , dna , base pair , protein secondary structure , stereochemistry , nuclear magnetic resonance spectroscopy , chemical shift , crystallography , molecule , biochemistry , organic chemistry
Model building, difference spectroscopy, and 1 H and 13 C NMR experiments have been carried out to study the binding of poly( L ‐Ser) with the polyribonucleotides poly( A ) and poly( U ) at p H 7.1. Studies have also been carried out with base paired duplexes poly( A )ṁpoly( U ). Peak doubling of C α and carbonyl resonances in the 13 C NMR spectrum of poly( L ‐Ser) in presence of polyribonucleotides is observed. From the chemical shifts and the linewidth, it is concluded that the interaction occurs through hydrogen bonding between the nucleic acid bases and the peptide backbone. In case of poly( A ) and poly( U ) the hydrogen bonding scheme with peptide backbone is different from that in the base paired poly( A )ṁpoly( U ). The possible binding schemes of double stranded DNA and peptide backbone have been investigated using model building and potential energy calculations. The hydrogen bonding schemes discriminate between various base pairs and their sequence. It is concluded that protein backbone can play an important role in protein–nucleic acid recognition schemes.