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Single-molecule measurement of conformational dynamics using a genetically encoded fluorescent probe suggests that the selectivity filter region of TRPV1 channels undergoes dynamic motion during agonist activation.

Morphological constraints dictate division mode in the human pathogen Staphylococcus aureus.

A novel high-throughput method for measuring many weak protein-peptide affinities simultaneously reveals how calcineurin, a human phosphatase essential for the immune response, recognizes its peptide substrates.

Bacterial outer membrane proteins are recognized by BamD at specific signals located in multiple β-strands at the C-terminus of these proteins, and this recognition is important for efficient outer membrane protein assembly and maintaining the integrity of outer membrane.

Structural and functional approaches unambiguously revealed physiologically relevant lateral interactions between FtsZ protofilaments.

Engineering transfer RNAs to read codons consisting of four bases requires changes in tRNA that go beyond the anticodon sequence.

X-ray crystallographic studies have completed the first atomic resolution description of the kinetic cycle of a potassium channel's pore domain.

Sequence-variant analogs of mitochondria-targeted tetrapeptides have distinct patterns of membrane-bound conformations, effects on membrane properties, and abilities to protect mitochondria subject to stress, illuminating how side chain variation can be leveraged in the development of more effective therapeutic compounds.

A method was developed for the metabolomic analysis of small numbers of flow cytometrically isolated cells from rare cell populations such as hematopoietic stem cells and circulating cancer cells.