Kinetic equivalence of the heat and cold structural transitions of lambda6-85

Heat- and cold-denatured proteins are considered separate thermodynamic states because temperature tuning requires the protein to pass through two 'soft' first-order phase transitions. When both pressure and temperature changes are allowed, the heat- and cold-denatured states of proteins c...

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Veröffentlicht in:	Philosophical transactions of the Royal Society of London. Series A: Mathematical, physical, and engineering sciences physical, and engineering sciences, 2005-02, Vol.363 (1827), p.565-573
Hauptverfasser:	Yang, Wei Y, Gruebele, Martin
Format:	Artikel
Sprache:	eng
Schlagworte:	Cold Temperature Computer Simulation DNA-Binding Proteins - analysis DNA-Binding Proteins - chemistry Hot Temperature Kinetics Models, Chemical Models, Molecular Motion Phase Transition Pressure Protein Conformation Protein Denaturation Protein Folding Protein Structure, Tertiary Repressor Proteins - analysis Repressor Proteins - chemistry Viral Proteins Viral Regulatory and Accessory Proteins
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