Structural characterization of proteins by NMR spectroscopy begins with the process of
sequence specific resonance assignments in which the 1 H, 13 C and 15 N chemical shifts …

Sequence specific resonance assignment constitutes an important step towards high-
resolution structure determination of proteins by NMR and is aided by selective identification …

The detailed characterization of the structure, dynamics and folding process of a protein is
crucial for understanding the biological functions it performs. Modern biophysical and …

Bacteriophages are the most abundant and diverse biological entities on earth.
Bacteriophage endolysins are unique peptidoglycan hydrolases and have huge potential as …

Dimerization of dynein light chain LC8 creates two symmetric grooves at the dimer interface
with diverse binding capabilities. In addition to pH and protein concentration, dimerization is …

A new approach for rapid resonance assignments in proteins based on amino acid selective
unlabeling is presented. The method involves choosing a set of multiple amino acid types for …

Three-dimensional structure determination of proteins by NMR requires the acquisition of
multidimensional spectra followed by assignment of chemical shifts to the respective nuclei …

Proteins are dynamic in nature and exist in a set of equilibrium conformations on various
timescale motions. The flexibility of proteins governs various biological functions, and …

Proteins are one of the most fundamental biomolecules present in living organisms. They
are indispensable to the sustenance of these organisms owing to the multitude of functions …

Understanding protein stability at residue level detail in the native state ensemble of a
protein is crucial to understanding its biological function. At the same time, deriving …