Knowledge of protein structure is paramount to the understanding of biological function,
develo** new therapeutics, and making detailed mechanistic hypotheses. Therefore …

Prediction of protein tertiary structures from amino acid sequence and understanding the
mechanisms of how proteins fold, collectively known as “the protein folding problem,” has …

Recently, mass spectrometry (MS) has become a viable method for elucidation of protein
structure. Surface-induced dissociation (SID), colliding multiply charged protein complexes …

Structures of biomolecular systems are increasingly computed by integrative modeling. In
this approach, a structural model is constructed by combining information from multiple …

The small multidrug transporter from Escherichia coli, EmrE, couples the energetically uphill
extrusion of hydrophobic cations out of the cell to the transport of two protons down their …

In recent years mass spectrometry-based covalent labeling techniques such as hydroxyl
radical footprinting (HRF) have emerged as valuable structural biology techniques, yielding …

The bifunctional spin label double-histidine copper-(II) capped with nitrilotriacetate [dHis-Cu
(II)-NTA], used in conjunction with electron paramagnetic resonance (EPR) methods can …

Despite advances in sampling and scoring strategies, Monte Carlo modeling methods still
struggle to accurately predict de novo the structures of large proteins, membrane proteins, or …

Recent development of high-resolution mass spectrometry (MS) instruments enables
chemical crosslinking (XL) to become a high-throughput method for obtaining structural …

Knowing atomistic details of proteins is essential not only for the understanding of protein
function but also for the development of drugs. Experimental methods such as X-ray …