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