Quantum mechanics/molecular mechanics (QM/MM) methods offer a very appealing option
for the computational study of enzymatic reaction mechanisms, by separating the problem …

Small molecules, such as solvent, substrate, and cofactor molecules, are key players in
enzyme catalysis. Computational methods are powerful tools for exploring the dynamics and …

Site-specific protein labeling is an important technique in protein chemistry and is used for
diverse applications ranging from creating protein conjugates to protein immobilization …

Abstract Metalloproteinase‐1 (MMP‐1) catalyzed collagen degradation is essential for a
wide variety of normal physiological processes, while at the same time contributing to …

We studied the electronic and nuclear dynamics of I-containing organic molecules induced
by intense hard X-ray pulses at the XFEL facility SACLA in Japan. The interaction with the …

The dynamic interactions of enzymes and substrates underpins catalysis, yet few techniques
can interrogate the dynamics of protein-bound ligands. Here we describe the use of field …

Conspectus Metalloproteins are essential to numerous reactions in nature, and constitute
approximately one-third of all known proteins. Molecular dynamics of proteins has been …

A novel cation− π interaction between the bound Cu+ metal ion and Trp44 in the periplasmic
Cu+/Ag+ metallochaperone Escherichia coli CusF protects Cu+ from the oxidative influence …

Two-dimensional electron–electron double resonance (2D-ELDOR) provides extensive
insight into molecular motions. Recent developments permitting experiments at higher …

Farnesyltransferase (FTase) is a heterodimeric enzyme, which catalyzes covalent
attachment of the farnesyl group to target proteins, thus coordinating their trafficking in the …