Conformational entropy from mobile bond vectors in proteins: A viewpoint that unifies NMR relaxation theory and molecular dynamics simulation approaches
A new method for determining conformational entropy in proteins is reported. Proteins
prevail as conformational ensembles, p∝ exp (− u). By selecting a bond vector (eg, N–H) as …
prevail as conformational ensembles, p∝ exp (− u). By selecting a bond vector (eg, N–H) as …
Local Ordering at Mobile Sites in Proteins: Combining Perspectives from NMR Relaxation and Molecular Dynamics
O Tchaicheeyan, N Mendelman… - The Journal of …, 2019 - ACS Publications
We report on progress toward improving NMR relaxation analysis in proteins in terms of the
slowly relaxing local structure (SRLS) approach by developing a method that combines …
slowly relaxing local structure (SRLS) approach by developing a method that combines …
SRLS Analysis of 15N–1H NMR Relaxation from the Protein S100A1: Dynamic Structure, Calcium Binding, and Related Changes in Conformational Entropy
N Mendelman, E Meirovitch - The Journal of Physical Chemistry B, 2021 - ACS Publications
We report on amide (N–H) NMR relaxation from the protein S100A1 analyzed with the
slowly relaxing local structure (SRLS) approach. S100A1 comprises two calcium-binding …
slowly relaxing local structure (SRLS) approach. S100A1 comprises two calcium-binding …
15N–H-Related Conformational Entropy Changes Entailed By Plexin-B1 RBD Dimerization: Combined Molecular Dynamics/NMR Relaxation Approach
M Zerbetto, E Meirovitch - The Journal of Physical Chemistry B, 2017 - ACS Publications
We report on a new method for determining function-related conformational entropy
changes in proteins. Plexin-B1 RBD dimerization serves as example, and internally mobile …
changes in proteins. Plexin-B1 RBD dimerization serves as example, and internally mobile …
Conformational Entropy from Slowly Relaxing Local Structure Analysis of 15N–H Relaxation in Proteins: Application to Pheromone Binding to MUP-I in the 283–308 …
L Žídek, E Meirovitch - The Journal of Physical Chemistry B, 2017 - ACS Publications
The slowly relaxing local structure (SRLS) approach is applied to 15N–H relaxation from the
major urinary protein I (MUP-I), and its complex with pheromone 2-sec-butyl-4, 5 …
major urinary protein I (MUP-I), and its complex with pheromone 2-sec-butyl-4, 5 …
Conformational Entropy from Restricted Bond-Vector Motion in Proteins: The Symmetry of the Local Restrictions and Relation to NMR Relaxation
N Mendelman, E Meirovitch - The Journal of Physical Chemistry B, 2020 - ACS Publications
Locally mobile bond-vectors contribute to the conformational entropy of the protein, given by
Sk≡ S/k=−∫(P eq ln P eq) dΩ–ln∫ dΩ. The quantity P eq= exp (− u)/Z is the orientational …
Sk≡ S/k=−∫(P eq ln P eq) dΩ–ln∫ dΩ. The quantity P eq= exp (− u)/Z is the orientational …