Hot spots—A review of the protein–protein interface determinant amino‐acid residues
Proteins tendency to bind to one another in a highly specific manner forming stable
complexes is fundamental to all biological processes. A better understanding of complex …
complexes is fundamental to all biological processes. A better understanding of complex …
[HTML][HTML] Electrostatic aspects of protein–protein interactions
Structural and mutational analyses reveal a central role for electrostatic interactions in
protein–protein association. Experiment and theory both demonstrate that clusters of …
protein–protein association. Experiment and theory both demonstrate that clusters of …
Principles of protein− protein interactions: what are the preferred ways for proteins to interact?
Proteins are the working horse of the cellular machinery. They are responsible for diverse
functions ranging from molecular motors to signaling. They catalyze reactions, transport …
functions ranging from molecular motors to signaling. They catalyze reactions, transport …
The Poisson–Boltzmann equation for biomolecular electrostatics: a tool for structural biology
Electrostatics plays a fundamental role in virtually all processes involving biomolecules in
solution. The Poisson–Boltzmann equation constitutes one of the most fundamental …
solution. The Poisson–Boltzmann equation constitutes one of the most fundamental …
Folding funnels, binding funnels, and protein function
Folding funnels have been the focus of considerable attention during the last few years.
These have mostly been discussed in the general context of the theory of protein folding …
These have mostly been discussed in the general context of the theory of protein folding …
The power of two: protein dimerization in biology
The self-association of proteins to form dimers and higher-order oligomers is a very common
phenomenon. Recent structural and biophysical studies show that protein dimerization or …
phenomenon. Recent structural and biophysical studies show that protein dimerization or …
Close‐range electrostatic interactions in proteins
Two types of noncovalent bonding interactions are present in protein structures, specific and
nonspecific. Nonspecific interactions are mostly hydrophobic and van der Waals. Specific …
nonspecific. Nonspecific interactions are mostly hydrophobic and van der Waals. Specific …
Protein–protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfaces
Polar residue hot spots have been observed at protein–protein binding sites. Here we show
that hot spots occur predominantly at the interfaces of macromolecular complexes …
that hot spots occur predominantly at the interfaces of macromolecular complexes …
Withanone from Withania somnifera Attenuates SARS-CoV-2 RBD and Host ACE2 Interactions to Rescue Spike Protein Induced Pathologies in Humanized Zebrafish …
Purpose SARS-CoV-2 engages human ACE2 through its spike (S) protein receptor binding
domain (RBD) to enter the host cell. Recent computational studies have reported that …
domain (RBD) to enter the host cell. Recent computational studies have reported that …
How do thermophilic proteins deal with heat?
Recent years have witnessed an explosion of sequence and structural information for
proteins from hyperthermophilic and thermophilic organisms. Complete genome sequences …
proteins from hyperthermophilic and thermophilic organisms. Complete genome sequences …