René C. van Schaik

TL;DR: In this paper, a simple, general and numerically stable approach for avoiding the singularities which generally occur when atoms or interaction sites are created or annihilated in free energy calculations based on computer simulations is presented.

TL;DR: It is shown that LAC can be refined without manual interference and using only 5000 steps (10 ps) of 4D-MD, indicating that this method may be a very useful tool when modelling loops in proteins.

TL;DR: The solution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli has been determined by NMR in combination with distance geometry and restrained molecular dynamics, suggesting that the strain may be an artifact of crystallization conditions instead of an essential element in the phosphorylation/dephosphorylation process.

TL;DR: A new method (PEACS) is introduced which has a far better performance than conventional search methods for low-energy conformations and samples a much larger part of the available conformational space than MD does.

TL;DR: The conformation and hydrogen bond pattern of Gln H6 and Glu H6 in antibodies carrying these residues are analyzed and mechanisms by which this residue could contribute to VH domain stability are suggested.