Osmolytes induce structure in an early intermediate on the folding pathway of barstar.

Osmolytes induce structure in an early intermediate on the folding pathway of barstar.

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http://www.wikidata.org/entity/Q44982138
The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state.Role of protein stabilizers on the conformation of the unfolded state of cytochrome c and its early folding kinetics: investigation at single molecular resolution.Chemical chaperone rescue of mutant human cystathionine beta-synthaseThermodynamic dissection of the intrinsically disordered N-terminal domain of human glucocorticoid receptor.Molecular mechanism for the preferential exclusion of TMAO from protein surfaces.Native and nonnative conformational preferences in the urea-unfolded state of barstar.Barrierless evolution of structure during the submillisecond refolding reaction of a small protein.Single-Molecule Chemo-Mechanical Spectroscopy Provides Structural Identity of Folding Intermediates.Effects of denaturants and osmolytes on proteins are accurately predicted by the molecular transfer modelTMAO-Protein Preferential Interaction Profile Determines TMAO's Conditional In Vivo Compatibility.Trimethylamine N-oxide abolishes the chaperone activity of α-casein: an intrinsically disordered protein.Hydrogen bonding progressively strengthens upon transfer of the protein urea-denatured state to water and protecting osmolytes.Exploring the cooperativity of the fast folding reaction of a small protein using pulsed thiol labeling and mass spectrometry.Observing the osmophobic effect in action at the single molecule level
P2860

Osmolytes induce structure in an early intermediate on the folding pathway of barstar.

Item
http://www.wikidata.org/entity/Q44982138
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Osmolytes induce structure in an early intermediate on the folding pathway of barstar.
@en
Osmolytes induce structure in an early intermediate on the folding pathway of barstar.
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type
label
Osmolytes induce structure in an early intermediate on the folding pathway of barstar.
@en
Osmolytes induce structure in an early intermediate on the folding pathway of barstar.
@nl
prefLabel
Osmolytes induce structure in an early intermediate on the folding pathway of barstar.
@en
Osmolytes induce structure in an early intermediate on the folding pathway of barstar.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P356
P1433
P1476
Osmolytes induce structure in an early intermediate on the folding pathway of barstar.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698