R. William Broadhurst

TL;DR: It is shown that a specific proline (Pro 8*), located at the apex of the loop between the second and third transmembrane helices (M2–M3), can link binding to gating through a cis–trans isomerization of the protein backbone, and suggested that a molecular rearrangement at Pro 8* is the structural mechanism that opens the receptor pore.

TL;DR: Results suggest that chromo domains may function as protein interaction motifs, bringing together different proteins in multi‐protein complexes and locating them in heterochromatin.

TL;DR: DANGLE, a new algorithm that employs Bayesian inference to estimate the likelihood of all possible values of the backbone dihedral angles phi and psi for each residue in a query protein, based on observed chemical shifts and the conformational preferences of each amino acid type, is introduced.

TL;DR: NMR solution structure of a 120 residue polypeptide representing a typical pair of such domains, fused at their respective C and N termini, adopts a stable dimeric structure which reveals the detailed role of these (predominantly helical) domains in docking and dimerization by modular polyketide synthases.

TL;DR: In this paper, a combination of simulation and experiment is used to demonstrate that the sensitivity of a family of 3D/4D NMR experiments used to assign resonances and to obtain structural restraints in proteins is improved by partial random deuteration; the improvement increases as the correlation time of the protein becomes longer.