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Physics / Protein structure / Coiled coil / Chemical bonding / Protein folding / Thermodynamic equilibrium / Spin–lattice relaxation / Peptide bond / Equilibrium constant / Chemistry / Equilibrium chemistry / Nuclear magnetic resonance


D. Andre´ d’Avignon1 G. Larry Bretthorst1 Marilyn Emerson Holtzer1 Kathleen A. Schwarz1 Ruth Hogue Angeletti2 Lisa Mints2
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Document Date: 2011-04-28 11:57:20

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City

St. Louis / /

Company

Wiley InterScience / Wiley Periodicals Inc. / /

Currency

SIT / /

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Facility

Washington University / University Mass Spectrometry Resource / Albert Einstein College of Medicine / Campus Box / /

IndustryTerm

unfavorable energy / chemical exchange / entropic search / last such site / benign media / monomer chains / chemical rate constants / energy level diagrams / energy difference / energy / /

Organization

Laboratory for Macromolecular Analysis & Proteomics / transition state ensemble / Albert Einstein College of Medicine / Washington University / Department of Chemistry / /

Person

Jun Coiled Coils / Marilyn Emerson / Ruth Hogue / Az / Alfred Holtzer / /

Position

model for the equilibrium conformational population / G1 ðTÞ=RT / Hiz ðT0 Þ=RT / General / ðT0 Þ=RT / NMR General / /

ProgrammingLanguage

DC / K / /

ProvinceOrState

Missouri / New York / /

Technology

Proteomics / simulation / adopted protocol / /

URL

www.interscience.wiley.com / /

SocialTag