Structural stability and folding pathways of proteins under native conditions as monitored by hydrogen/deuterium (H/D) exchange methods

Abstract

The conformational stability and dynamics of proteins are indispensable to address the structure function relationships of proteins and also to design novel proteins for therapeutic purposes. At molecular level, conformational stability of a protein can be monitored in presence of external denaturing agents by using traditional biophysical techniques, whereas at residue level, conformational stability of a protein can be measured by hydrogen/deuterium (H/D) exchange methods in conjunction with nuclear magnetic resonance (NMR) techniques. In this review, stability and folding of proteins probed at residue level resolutions by using H/D exchange methods to date have been exclusively covered, systematically classified and discussed in detail. Moreover the merits and limitations of the exquisite methods and computational alternatives to the proteins H/D exchanges have also been discoursed.