ITEM METADATA RECORD
Title: Normal mode analysis of trp RNA-binding attenuation protein: structure and collective motions
Authors: Hu, Guang ×
Michielssens, Servaas
Moors, Sam
Ceulemans, Arnout #
Issue Date: Sep-2011
Publisher: American Chemical Society
Series Title: Journal of Chemical Information and Modeling vol:51 issue:9 pages:2361-2371
Abstract: The trp RNA-binding protein (TRAP) has a toroidal topology and a perfect 11-fold symmetry, which make it an excellent candidate for a vibrational study of elastic properties. Normal mode analysis in combination with correlation matrix calculations were used to detect collective low-frequency motions in TRAP. The results reveal the presence of highly-correlated modes at the spectral origin which directly reflect the annular and toroidal topology. Integral correlations over the low-frequency part of the vibrational spectrum further demonstrate the relative rigidity of the 11 monomer building blocks of TRAP. The internal flexibility of each monomer and the effects of tryptophan-binding were also examined. The study clearly shows the determining influence of symmetry and topology on the elastic properties, and also offers a detailed view on the trp affinity of TRAP.
URI: 
ISSN: 1549-9596
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Quantum Chemistry and Physical Chemistry Section
× corresponding author
# (joint) last author

Files in This Item:

There are no files associated with this item.

Request a copy

 




All items in Lirias are protected by copyright, with all rights reserved.

© Web of science