For deriving maximal advantage from information on biomacromolecular flexibility and
rigidity, results from rigidity analyses must be linked to biologically relevant characteristics of …

The effects of amino acid insertions and deletions (InDels) remain a rather under-explored
area of structural biology. These variations oftentimes are the cause of numerous disease …

Predicting how a point mutation alters a protein's stability can guide pharmaceutical drug
design initiatives which aim to counter the effects of serious diseases. Conducting …

Protein rigidity and flexibility can be analyzed accurately and efficiently using the program
floppy inclusion and rigid substructure topography (FIRST). Previous studies using FIRST …

We present a geometry-based, sampling based method to explore conformational pathways
in medium and large proteins which undergo large-scale conformational transitions. In a …

Predicting how a point mutation alters a protein's stability can guide drug design initiatives
which aim to counter the effects of serious diseases. Mutagenesis studies give insights …

We describe an approach (ENT FNC) for performing rigidity analyses of biomacromolecules
on ensembles of network topologies (ENT) generated from a single input structure. The ENT …

Predicting how amino acid substitutions affect the stability of a protein has relevance to drug
design and may help elucidate the mechanisms of disease-causing protein variants …

Accurate prediction of protein stability changes resulting from amino acid substitutions is of
utmost importance in medicine to better understand which mutations are deleterious …

Understanding how an amino acid substitution affects a protein's structure can aid in the
design of pharmaceutical drugs that aim at countering diseases caused by protein mutants …