Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/86336
Title: Rotation of Guanine Amino Groups in G-Quadruplexes: A Probe for Local Structure and Ligand Binding
Authors: Adrian, Michael
Winnerdy, Fernaldo Richtia
Heddi, Brahim
Phan, Anh Tuân
Keywords: DNA
Guanine
Issue Date: 2017
Source: Adrian, M., Winnerdy, F. R., Heddi, B., & Phan, A. T. (2017). Rotation of Guanine Amino Groups in G-Quadruplexes: A Probe for Local Structure and Ligand Binding. Biophysical Journal, 113(4), 775-784.
Series/Report no.: Biophysical Journal
Abstract: Nucleic acids are dynamic molecules whose functions may depend on their conformational fluctuations and local motions. In particular, amino groups are dynamic components of nucleic acids that participate in the formation of various secondary structures such as G-quadruplexes. Here, we present a cost-efficient NMR method to quantify the rotational dynamics of guanine amino groups in G-quadruplex nucleic acids. An isolated spectrum of amino protons from a specific tetrad-bound guanine can be extracted from the nuclear Overhauser effect spectroscopy spectrum based on the close proximity between the intra-residue imino and amino protons. We apply the method in different structural contexts of G-quadruplexes and their complexes. Our results highlight the role of stacking and hydrogen-bond interactions in restraining amino-group rotation. The measurement of the rotation rate of individual amino groups could give insight into the dynamic processes occurring at specific locations within G-quadruplex nucleic acids, providing valuable probes for local structure, dynamics, and ligand binding.
URI: https://hdl.handle.net/10356/86336
http://hdl.handle.net/10220/44018
ISSN: 0006-3495
DOI: http://dx.doi.org/10.1016/j.bpj.2017.05.053
Rights: © 2017 Biophysical Society.
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:SPMS Journal Articles

Google ScholarTM

Check

Altmetric

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.