ProCOOP, A Program that Predicts the Cooperatives of Hydrogen Exchange in Proteins
Published: 2013
Author(s) Name: K. Sarvanan |
Author(s) Affiliation: Dean, Faculty of Computer Science, PRIST University, Thanjavur, Tamil Nadu, India
Locked
Subscribed
Available for All
Abstract
Each protein adopts a particular, well-defined, unique
three-dimensional (3D) structure, which is directed
to do certain functions. 3D structures of proteins can
be well-determined at atomic level resolutions using
x-ray crystallography and nuclear magnetic resonance
(NMR) techniques. These high resolution structures of
proteins are essential for understanding their structurefunction
relationships. However, there is a divergent
correlation between these experimental outcomes and
requirements of current research in structural biology.
In this background, ProCOOP algorithm was developed
to predict population of secondary structures in proteins
based on molecular mass of their deuterated-forms. By
taking into consideration of many different structural
and environmental factors, the ProCOOP validates its
outputs and gives suggestion to improve experimental
conditions for better predictions. The applications
of ProCOOP for the data analysis in proteomics and
genomics have also been brought into fore in detail.
Keywords: Proteins, Secondary Structure, Hydrogen Exchange, Rate Constant, Algorithm
View PDF