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Protein–Nucleic acid interactions: Investigations on the peptide backbone interaction with polynucleotides

✍ Scribed by Ramakrishna V. Hosur; N. Vasanth Kumar; Girjesh Govil

Publisher
John Wiley and Sons
Year
1981
Tongue
English
Weight
452 KB
Volume
20
Category
Article
ISSN
0020-7608

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✦ Synopsis

Abstract

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.

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