The hydrophobic effect and its role in cold denaturation.
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Assisted protein folding at low temperature: evolutionary adaptation of the Antarctic fish chaperonin CCT and its client proteinsStructural features determining thermal adaptation of esterases.NMR-based structural biology of proteins in supercooled water.Coping with thermal challenges: physiological adaptations to environmental temperatures.NMR chemical shift analysis of the conformational transition between the monomer and tetramer of melittin in an aqueous solution.Function and biotechnology of extremophilic enzymes in low water activity.Evolutionary aspects of enzyme dynamicsSpectroscopic studies of the Salmonella enterica adenosyltransferase enzyme SeCobA: molecular-level insight into the mechanism of substrate Cob(II)alamin activation.Cold adaptation, ca2+ dependency and autolytic stability are related features in a highly active cold-adapted trypsin resistant to autoproteolysis engineered for biotechnological applications.Transcriptomic characterization of cold acclimation in larval zebrafishImmobilization of carboxypeptidase from Sulfolobus solfataricus on magnetic nanoparticles improves enzyme stability and functionality in organic media.Expression and in vitro functional analyses of recombinant Gam1 proteinA thermodynamic framework for understanding temperature sensing by transient receptor potential (TRP) channels.Molecular insights into the reversible formation of tau protein fibrils.Cryopreservation of precision-cut tissue slices.Solvent nanostructure, the solvophobic effect and amphiphile self-assembly in ionic liquids.Non-Arrhenius protein aggregation.Arc is a flexible modular protein capable of reversible self-oligomerization.Essential dynamics of the cold denaturation: pressure and temperature effects in yeast frataxin.Impact of Thermal Stress on Kidney-Specific Gene Expression in Farmed Regional and Imported Rainbow Trout.Effects of salt on the structure, stability, and function of a halophilic dihydrofolate reductase from a hyperhalophilic archaeon, Haloarcula japonica strain TR-1.Magnesium impacts myosin V motor activity by altering key conformational changes in the mechanochemical cycle.Novel immobilization process of a thermophilic catalase: efficient purification by heat treatment and subsequent immobilization at high temperature.The meaning of 'native'.The Role of Solvent-Accessible Leu-208 of Cold-Active Pseudomonas fluorescens Strain AMS8 Lipase in Interfacial Activation, Substrate Accessibility and Low-Molecular Weight Esterification in the Presence of Toluene.Thermodynamic properties of amyloid fibrils in equilibrium.Physical origin of hydrophobicity studied in terms of cold denaturation of proteins: comparison between water and simple fluids.Modeling simple amphiphilic solutes in a Jagla solvent.“Smart” Polymers: Physicochemical Characteristics and Applications in Bio-Separation StrategiesHydrophobic interactions in the formation of secondary structures in small peptidesHydrophobicity within the three-dimensional Mercedes-Benz model: Potential of mean forceEnzyme Catalysis in Psychrophiles
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The hydrophobic effect and its role in cold denaturation.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 17 July 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
The hydrophobic effect and its role in cold denaturation.
@en
The hydrophobic effect and its role in cold denaturation.
@nl
type
label
The hydrophobic effect and its role in cold denaturation.
@en
The hydrophobic effect and its role in cold denaturation.
@nl
prefLabel
The hydrophobic effect and its role in cold denaturation.
@en
The hydrophobic effect and its role in cold denaturation.
@nl
P2093
P50
P1433
P1476
The hydrophobic effect and its role in cold denaturation
@en
P2093
Cristiano L Dias
Ilpo Vattulainen
Martin Grant
P356
10.1016/J.CRYOBIOL.2009.07.005
P577
2009-07-17T00:00:00Z