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Hydrophobic effect / Protein folding / Denaturation / Hydrophobic collapse / Globular protein / Native state / Urea / Guanidine / Random coil / Chemistry / Protein structure / Biology


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Document Date: 2011-07-05 13:24:42

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Country

United Kingdom / Israel / /

Currency

USD / /

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Event

Environmental Issue / /

Facility

Princeton University / Princeton University Library / Weizmann Institute of Science / Lewis-Sigler Institute / /

IndustryTerm

chemical denaturants / chemical reaction essential / transfer free energy / hydrogen-bond network / chemical cosolvents / denaturant solution / low energy / favorable interaction energy / free energy / free energy cost / free energy difference / chemical denaturation / energy change / bond network / urea solution / biological systems / chemical ingredients / energy-entropy trade-off / overall free energy / hydrophobic chain / high-energy / polypeptide chain / denaturant solutions / aqueous solutions / higher-energy conformations / computer technology / interaction energy / protein chain / energy / /

Organization

Chemical Physics Department / Lewis-Sigler Institute for Integrative Genomics / Princeton University / Weizmann Institute of Science / /

Person

Charles Tanford / /

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Position

TRANSFER MODEL / thermodynamic model / great protein chemist / /

ProvinceOrState

New Jersey / /

Technology

Genomics / Thermodynamics / spectroscopy / simulation / computer technology / /

URL

www.annualreviews.org / /

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