Molecular dynamics (MD) simulations have become increasingly useful in the modern drug
development process. In this review, we give a broad overview of the current application …

RAS proteins are binary switches, cycling between ON and OFF states during signal
transduction. These switches are normally tightly controlled, but in RAS-related diseases …

Proteins participate in various essential processes in vivo via interactions with other
molecules. Identifying the residues participating in these interactions not only provides …

Ras proteins are small GTPases, cycling between inactive GDP-bound and active GTP-
bound states. Through these switches they regulate signaling that controls cell growth and …

Allostery is a universal, biological phenomenon in which orthosteric sites are fine‐tuned by
topologically distal allosteric sites triggered by perturbations, such as ligand binding, residue …

K-Ras is a membrane-associated GTPase that cycles between active and inactive
conformational states to regulate a variety of cell signaling pathways. Somatic mutations in K …

Approximately 15% of all human tumors harbor mutant KRAS, a membrane-associated
small GTPase and notorious oncogene. Mutations that render KRAS constitutively active will …

Recent studies found that membrane-bound K-Ras dimers are important for biological
function. However, the structure and thermodynamic stability of these complexes remained …

Identifying binding hotspots on protein surfaces is of prime interest in structure-based drug
discovery, either to assess the tractability of pursuing a protein target or to drive improved …

Identifying druggable binding sites on proteins is an important and challenging problem,
particularly for cryptic, allosteric binding sites that may not be obvious from X-ray, cryo-EM …