Conservative mutations within a secondary active transport protein influenced the conformational equilibrium probed using NMR spectroscopy which correlated to the functional output in vivo.
Lindsay D Clark, Igor Dikiy ... Daniel M Rosenbaum
Generation of a highly deuterated 13C-methyl labeled wild-type GPCR sample is used to facilitate characterization of the molecular environments and fast ps-ns dynamics of sidechains when the receptor is bound to ligands of different efficacy.
Yiyi Chen, Laimdota Zizmare ... Christoph Trautwein
Targeted manipulations on organotypic cultures show that the retina switches between at least four different metabolic pathways, each with different yields and kinetics, to dynamically adapt to momentaneous energy needs.
Ca2+-free synaptotagmin-1 binds to neuronal SNARE complexes anchored on nanodiscs, and Ca2+ releases this interaction to induce tight, specific binding to PIP2-containing membranes.
Solution NMR spectroscopy reveals the energy landscape of immature Cu, Zn-superoxide dismutase and leads to atomic resolution structural models of transiently populated non-native oligomers.
Eugene Serebryany, Sourav Chowdhury ... Eugene I Shakhnovich
The human eye lens imports and concentrates within itself a naturally abundant small molecule that inhibits cataract-associated aggregation of an eye lens protein before the aggregates get large enough to scatter light.
Robust NMR approach allowed simultaneous detection of substrate cleavage site and real-time kinetics of hydrolysis for Staphylococcus aureus peptidoglycan hydrolases lysostaphin and LytM, and revealed D-alanyl-glycine activity for LytM.
Nicolai Tidemand Johansen, Marta Bonaccorsi ... Lise Arleth
The Mg2+-channel CorA explores a wide conformational landscape of non-conducting states irrespective of bound Mg2+, but only in abscence of Mg2+, conducting states become accessible due to increased backbone dynamics.
Tomohide Saio, Soichiro Kawagoe ... Charalampos G Kalodimos
A combined NMR and kinetic study demonstrates how the dynamic transition of a molecular chaperone between different oligomerization states can modulate its activity by altering the binding kinetics and energetics of non-native proteins.
NMR-based flux measurements show that both bacterial and human Hsp70 chaperones interact with helical, as well as sheet substrates predominantly through a conformational selection mechanism.