Molecular recognition is central to all biological processes. For the past 50 years,
Koshland's' induced fit'hypothesis has been the textbook explanation for molecular …

Allostery is a fundamental mechanism of cellular homeostasis by intra-protein
communication between distinct functional sites. It is an internal process of proteins to steer …

Protein dynamics are essential for protein function, and yet it has been challenging to
access the underlying atomic motions in solution on nanosecond-to-microsecond time …

The function of bio-macromolecules is determined by both their 3D structure and
conformational dynamics. These molecules are inherently flexible systems displaying a …

Accurate mechanistic description of structural changes in biomolecules is an increasingly
important topic in structural and chemical biology. Markov models have emerged as a …

The development of residual dipolar coupling (RDC) in protein NMR spectroscopy, over a
decade ago, has become a useful and almost routine tool for accurate protein solution …

We present a detailed discussion of the complimentary fields of the application of two-
dimensional infrared (2D-IR) spectroscopy in comparison with two-dimensional nuclear …

We review the role conformational ensembles can play in the analysis of biomolecular
dynamics, molecular recognition, and allostery. We introduce currently available methods for …

A new lanthanide tag was designed for site-specific labeling of proteins with paramagnetic
lanthanide ions. The tag, 4-mercaptomethyl-dipicolinic acid, binds lanthanide ions with …

The majority of protein structures are determined in the crystalline state, yet few methods
exist for the characterization of dynamics for crystalline biomolecules. Solid-state NMR can …