Members of the fatty acid binding protein (FABP) family function as intracellular transporters
of long-chain fatty acids and other hydrophobic molecules to different cellular compartments …

Structural dynamics of fatty acid binding proteins (FABPs), which accommodate poorly
soluble ligands in the internalized binding cavities, are intimately related to their function …

Many proteins fold in apparent two-state behavior, as partially folded intermediates only
transiently accumulate and easily escape detection. Besides a native form and a mainly …

The mechanism of urea's action in protein denaturation remains largely unknown. To
provide an experimental basis for molecular dynamics (MD) simulations on urea-protein …

The viral protease domain (NS3pro) of dengue virus is essential for virus replication, and its
cofactor NS2B is indispensable for the proteolytic function. Although several NS3pro-NS2B …

Solid-state nuclear magnetic resonance (SSNMR) is an excellent tool for determining the
molecular motions within a dynamic system. SSNMR relaxation measurements can access a …

The thioredoxin (Trx)-coupled arsenate reductase (ArsC) is a family of enzymes that
catalyzes the reduction of arsenate to arsenite in the arsenic detoxification pathway. The …

Proteins are intrinsically dynamic molecules and undergo exchanges among multiple
conformations to perform biological functions. The CPMG relaxation dispersion and CEST …

Members of the fatty acid binding protein (FABP) family function as intracellular transporters
of hydrophobic molecules, facilitating both fatty acid and lipid metabolism. FABPs share a …

Prevalence of one or more partially folded intermediates during protein unfolding with
different secondary and ternary conformations has been identified as an integral character of …