Luke M. Rice

TL;DR: The Crystallography & NMR System (CNS) as mentioned in this paper is a software suite for macromolecular structure determination by X-ray crystallography or solution nuclear magnetic resonance (NMR) spectroscopy.

TL;DR: The results show that tubulin isotypes and PTMs can govern motor velocity, processivity and microtubule depolymerization rates, with substantial changes conferred by even single amino acid variation, and that different molecular motors recognize distinctive tubulin ‘signatures’, which supports the tubulin-code hypothesis.

TL;DR: Applications to crystallographic refinement show a significantly increased radius of convergence over conventional techniques, and the sampling strategy presented here combines high temperature torsion angle dynamics with repeated trajectories using different initial velocities.

TL;DR: Evidence is provided that the interplay between biochemistry and mechanics is essential for the cellular functions of microtubules, and that fine-tuning microtubule dynamics is enabled by the allosteric coupling of tubulin subunits, which propagates conformational changes through the lattice.

TL;DR: Molecular dynamics in torsion-angle space was applied to nuclear magnetic resonance structure calculation using nuclear Overhauser effect-derived distances and J-coupling-constant-derived dihedral angle restraints to show increased computational efficiency and success rate for large proteins and a dramatically increased radius of convergence for DNA.