Most amino acid substitutions in a protein either lead to partial loss-of-function or are near
neutral. Several studies have shown the existence of second-site mutations that can rescue …

Protein misfolding is involved in a large number of diseases, among which cystic fibrosis.
Complex intra-and inter-domain folding defects associated with mutations in the cystic …

Mutations in protein-coding regions underlie almost all Mendelian disorders, drive
tumorigenesis, and contribute to susceptibility to common diseases. Despite the great …

Although there have been recent transformative advances in the area of protein structure
prediction, prediction of point mutations that improve protein stability remains challenging. It …

The absence of a functional ATP Binding Cassette (ABC) protein called the Cystic Fibrosis
Transmembrane Conductance Regulator (CFTR) from apical membranes of epithelial cells …

Neutral and adaptive mutations are key players in the evolutionary dynamics of proteins at
molecular, cellular and organismal levels. Conversely, largely destabilizing mutations are …

Our general aim is to better understand the biophysical and biochemical principles that
govern nascent or stress-destabilized proteins to unfold and re/fold to their native state or …

Many intrinsically disordered proteins (IDPs) attain a well-defined structure in a coupled
folding and binding reaction with another protein. Such reactions may involve early to late …

Understanding how mutations affect protein activity and organismal fitness is a major
challenge. We used saturation mutagenesis combined with deep sequencing to determine …

Neighbouring domains of multidomain proteins with homologous tandem repeats have
divergent sequences, probably as a result of evolutionary pressure to avoid misfolding and …