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Sosnick, Tobin R.
One or more keywords matched the following items that are connected to Sosnick, Tobin R.
Item TypeName
Concept Ubiquitin
Academic Article Distinguishing between two-state and three-state models for ubiquitin folding.
Academic Article Distinguishing foldable proteins from nonfolders: when and how do they differ?
Academic Article Contribution of hydrogen bonding to protein stability estimated from isotope effects.
Academic Article Discerning the structure and energy of multiple transition states in protein folding using psi-analysis.
Academic Article Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding.
Academic Article Comment on "Force-clamp spectroscopy monitors the folding trajectory of a single protein".
Academic Article PII structure in the model peptides for unfolded proteins: studies on ubiquitin fragments and several alanine-rich peptides containing QQQ, SSS, FFF, and VVV.
Academic Article Intramolecular cross-linking evaluated as a structural probe of the protein folding transition state.
Academic Article Psi-constrained simulations of protein folding transition states: implications for calculating.
Academic Article Characterizing the protein folding transition state using psi analysis.
Academic Article Protein vivisection reveals elusive intermediates in folding.
Academic Article Ubiquitin is a novel substrate for human insulin-degrading enzyme.
Academic Article A "Link-Psi" strategy using crosslinking indicates that the folding transition state of ubiquitin is not very malleable.
Academic Article Probing the folding transition state of ubiquitin mutants by temperature-jump-induced downhill unfolding.
Academic Article Early collapse is not an obligate step in protein folding.
Academic Article Differences in the folding transition state of ubiquitin indicated by phi and psi analyses.
Academic Article Metal binding kinetics of bi-histidine sites used in psi analysis: evidence of high-energy protein folding intermediates.
Academic Article Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculations.
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