Since its inception nearly a half century ago, CHARMM has been playing a central role in
computational biochemistry and biophysics. Commensurate with the developments in …

Atomistic-level understanding of surface hydration mediating protein–protein interactions
and ligand binding has been a challenge due to the dynamic nature of water molecules near …

Understanding the structural and energetic requirements of non-fibrillar oligomer formation
harbors the potential to decipher an important yet still elusive part of amyloidogenic peptide …

Ordered assembly of collagen molecules on flat substrates has potential for various
applications and serves as a model system for studying the assembly process. While …

Cytosine methylation affects mechanical properties of DNA and potentially alters the
hydration fingerprint for recognition by proteins. The atomistic origin for these effects is not …

The microtubule (MT)-associated motor protein kinesin utilizes its conserved ATPase head
to achieve diverse motility characteristics. Despite considerable knowledge about how its …

Epidemiological studies have shown that the development of Alzheimer's disease (AD) is
associated with type 2 diabetes (T2D), but it still remains unclear how AD and T2D are …

Degradation of fibrillar collagen is critical for tissue maintenance. Yet, understanding
collagen catabolism has been challenging partly due to a lack of atomistic picture for its load …

Self-assembly plays a crucial role in the formation and allosteric processes of many
biomolecules, water molecules can affect these processes. Cytosine (Cyt) has excellent self …

Many proteins and peptides self-associate into highly ordered and structurally similar
amyloid cross-β aggregates. This fibrillation is critically dependent on properties of the …