Nuclear magnetic resonance (NMR) is widely used across many fields of science because
of the rich data it produces, and some of the most valuable data come from studies of …

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 …

Conformational sampling for a set of 10 α-or β-(1→ 6)-linked oligosaccharides has been
studied using explicit solvent Hamiltonian replica exchange (HREX) simulations and NMR …

The intrinsic flexibility of glycans complicates the study of their structures and dynamics,
which are often important for their biological function. NMR has provided insights into the …

The conformation of saccharides in solution is challenging to characterize in the context of a
single well-defined three-dimensional structure. Instead, they are better represented by an …

Carbohydrates, also known as glycans in biological systems, are omnipresent in nature
where they as glycoconjugates occur as oligo‐and polysaccharides linked to lipids and …

The conformational dynamics of the human milk oligosaccharide lacto-N-fucopentaose (LNF-
1), α-l-Fuc p-(1→ 2)-β-d-Gal p-(1→ 3)-β-d-Glc p NAc-(1→ 3)-β-d-Gal p-(1→ 4)-d-Glc p, has …

An integrated computational methodology for interpreting NMR spin relaxation in proteins
has been developed. It combines a two-body coupled-rotator stochastic model with a …

The intrinsic flexibility of carbohydrates facilitates different 3D structures in response to
altered environments. At glycosidic (1→ 6)-linkages, three torsion angles are variable, and …

A computational stochastic approach is applied to the description of flexible molecules. By
combining (i) molecular dynamics simulations,(ii) hydrodynamics approaches, and (iii) a …