Protein–protein recognition plays an essential role in structure and function. Specific non- covalent interactions stabilize the structure of macromolecular assemblies, exemplified in …
M Nishio, Y Umezawa, J Fantini, MS Weiss… - Physical Chemistry …, 2014 - pubs.rsc.org
This is a sequel to the previous Perspective “The CH–π hydrogen bond in chemistry. Conformation, supramolecules, optical resolution and interactions involving carbohydrates” …
Introduction to Proteins provides a comprehensive and state-of-the-art introduction to the structure, function, and motion of proteins for students, faculty, and researchers at all levels …
Although hydrophobic interaction is the main contributing factor to the stability of the protein fold, the specificity of the folding process depends on many directional interactions. An …
M Guharoy, P Chakrabarti - Bioinformatics, 2007 - academic.oup.com
Motivation: The increasing amount of data on protein–protein interaction needs to be rationalized for deriving guidelines for the alteration or design of an interface between two …
K Hashimoto, H Nishi, S Bryant… - Physical biology, 2011 - iopscience.iop.org
Many soluble and membrane proteins form homooligomeric complexes in a cell which are responsible for the diversity and specificity of many pathways, may mediate and regulate …
Improvements in experimental techniques increasingly provide structural data relating to protein-protein interactions. Classification of structural details of protein-protein interactions …
BE Bowler - Current opinion in structural biology, 2012 - Elsevier
The denatured state ensemble (DSE) of unfolded proteins, once considered to be well- modeled by an energetically featureless random coil, is now well-known to contain flickering …
S Sonavane, P Chakrabarti - PLoS Computational Biology, 2008 - journals.plos.org
A comparative analysis of cavities enclosed in a tertiary structure of proteins and interfaces formed by the interaction of two protein subunits in obligate and non-obligate categories …