Protein dynamics by NMR has been reviewed extensively in recent years [1–10]. These
surveys show decisively that information on structure should be complemented by …

The ever‐increasing cellular roles ascribed to RNA raise fundamental questions regarding
how a biopolymer composed of only four chemically similar building‐block nucleotides …

NMR relaxation experiments have provided a wealth of information about molecular motions
in macromolecules and ordered fluids. Even though a rigorous theory of spin relaxation is …

We propose a fractional Brownian dynamics model for time correlation functions
characterizing the internal dynamics of proteins probed by NMR relaxation spectroscopy …

Abstract Domain dynamics in biomacromolecules is currently an area of intense research
because of its importance for understanding the huge quantity of available data relating the …

The orientational relaxation dynamics of semiflexible dendrimers are theoretically calculated
within the framework of optimized Rouse–Zimm formalism. Semiflexibility is modeled …

A simple general expression for the NMR cross-correlated relaxation rate under anisotropic
molecular tumbling is presented for globular proteins. The derivation includes effects of fast …

Internal motions in proteins, such as oscillations of internuclear vectors u (N i H i N) of amide
bonds about their equilibrium position, can be characterized by a local order parameter. This …

Among the numerous contributions of Geoffrey Bodenhausen to NMR spectroscopy, his
developments in the field of spin-relaxation methodology and theory will definitely have a …

Nuclear magnetic resonance (NMR) has proven to be the most valuable tool for
investigating internal dynamics of proteins. In this perspective, the interpretation of NMR …