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Results 1 - 10
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303
thermal unfolding of concanavalin
"... differential scanning calorimetric study on the irreversible ..."
Refolding upon force quench and pathways of mechanical and thermal unfolding of ubiquitin. Biophys
- J. 92:547–561
, 2007
"... ABSTRACT The refolding from stretched initial conformations of ubiquitin (PDB ID: 1ubq) under the quenched force is studied using the Ca-Go model and the Langevin dynamics. It is shown that the refolding decouples the collapse and folding kinetics. The force-quench refolding-times scale as tF; exp(f ..."
Abstract
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Cited by 7 (1 self)
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(fqDxF/kBT), where fq is the quench force and DxF 0.96 nm is the location of the average transition state along the reaction coordinate given by the end-to-end distance. This value is close to DxF 0.8 nm obtained from the force-clamp experiments. The mechanical and thermal unfolding pathways are studied
Thermal Unfolding Simulations of Apo-Calmodulin Using Leap-Dynamics
"... ABSTRACT The simulation method leap-dy-namics (LD) has been applied to protein thermal unfolding simulations to investigate domain-spe-cific unfolding behavior. Thermal unfolding simula-tions of the 148-residue protein apo-calmodulinwith implicit solvent were performed at temperatures 290 K, 325 K, ..."
Abstract
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Cited by 1 (0 self)
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ABSTRACT The simulation method leap-dy-namics (LD) has been applied to protein thermal unfolding simulations to investigate domain-spe-cific unfolding behavior. Thermal unfolding simula-tions of the 148-residue protein apo-calmodulinwith implicit solvent were performed at temperatures 290 K, 325 K
Thermal unfolding simulations of bacterial flagellin: insight into its refolding before assembly
- Biophys. J. 2008
"... ABSTRACT Flagellin is the subunit of the bacterial filament, the micrometer-long propeller of a bacterial flagellum. The protein is believed to undergo unfolding for transport through the channel of the filament and to refold in a chamber at the end of the channel before being assembled into the gro ..."
Abstract
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Cited by 3 (0 self)
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into the growing filament. We report a thermal unfolding simulation study of S. typhimurium flagellin in aqueous solution as an attempt to gain atomic-level insight into the refolding process. Each molecule comprises two filament-core domains fD0, D1g and two hypervariable-region domains fD2, D3g. D2 can
Life in the pressure cooker: The thermal unfolding of proteins from hyperthermophiles
"... Abstract Xieported here are the first results of a qcantitative ther-modynamic st-dy involvixg a series of proteins isolated from the anaerobic sulfur-reducixg archaebacterium Pyrococcus furiosus which grows near submrize geotherml vents on the deep ocean floor. The proteins isolated and investigate ..."
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weight (Mw) all three proteins investigated unfold at exactly the same temperature (113OC) The experimentally observed transition temperature Tm coincides with the extrapolated conversion temperature T * (Privalov, Privalov & Gill, Murphy and Gill, lreire and Murphy, 1-4) of 112OC. It is readily
Presence of a slow dimerization equilibrium on the thermal unfolding of the 205–316 thermolysin fragment at neutral pH
- Biochemistry
, 1996
"... ABSTRACT: Differential scanning calorimetry and size-exclusion chromatography have been used to characterize the dimerization and unfolding of the 205-316 C-terminal fragment of thermolysin at pH 7.5. We show that the folded fragment dimerizes at low temperature with a moderate affinity and undergoe ..."
Abstract
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Cited by 3 (1 self)
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and undergoes thermal unfolding according to a N2 a 2N a 2U model. This behavior has already been observed at acid pH, where a similar dissociation equilibrium has been found [Azuaga, A., Conejero-Lara, F., Rivas
Linkage of proton binding to the thermal unfolding of Sso7d from the hyperthermophilic archaebacterium Sulfolobus solfataricus
, 1999
"... In this study the pH dependence of the thermal stability of Sso7d from Sulfolobus solfataricus is analyzed. This small globular protein of 63 residues shows a very marked dependence of thermal stability on pH: the denaturation temperature passes from 65.2°C at pH 2.5 to 97.9°C at pH 4.5. Analysis of ..."
Abstract
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of the data points out that the binding of at least two protons is coupled to the thermal unfolding. By linking the proton binding to the conformational unfolding equilibrium, a thermodynamic model, which is able to describe the dependence upon the solution pH of both the excess heat capacity function
Molecular dynamics simulations to investigate the thermal unfolding behaviors of N-carbamyl-D-amino acid amidohydrolase
"... The thermal unfolding behaviors of N-carbamyl-D-amino acid amidohydrolase (DCase) were investigated by 1 ns molecular dynamics simulations in explicit water with temperature jump technique. Rather than a symmetrical event, the unfolding of the two subunits of the dimeric DCase follows different path ..."
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The thermal unfolding behaviors of N-carbamyl-D-amino acid amidohydrolase (DCase) were investigated by 1 ns molecular dynamics simulations in explicit water with temperature jump technique. Rather than a symmetrical event, the unfolding of the two subunits of the dimeric DCase follows different
Results 1 - 10
of
303
