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Biochemistry / Acidophile / Protein folding / Protein domain / Enzyme / Protease / Serpin / Pepsin / Phi value analysis / Biology / Protein structure / Chemistry


J. Mol. Biol[removed], 870–883 doi:[removed]j.jmb[removed]Structural and Mechanistic Exploration of Acid Resistance: Kinetic Stability Facilitates
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Document Date: 2007-06-14 17:09:33


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File Size: 1,47 MB

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City

La Jolla / Nterm / San Francisco / Nterm Ala / Glu Gln / /

Company

Elsevier Ltd. / Millipore / Bioscience Inc. / /

Country

United States / /

Currency

pence / /

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Facility

bridge Glu32 / bridge Asp15B / Howard Hughes Medical Institute / C terminus / N terminus / bridge of NAPase / terminal β-barrels / bridge Salt / University of California / Kyushu Sangyo University / /

IndustryTerm

metal / chemical denaturants / free energy / free energy barrier height / chemical effects / integral site / free energy barrier / metal binding site effects / chemicals / evolutionary tool / energy / /

MusicGroup

Yes / /

Organization

Department of Applied Chemistry and Biochemistry / Department of Biochemistry and Biophysics / University of California / San Francisco / Howard Hughes Medical Institute / Kyushu Sangyo University / Fukuoka / /

Person

Ala / Ser Arg / Kyle P. Eagen / Adam R. Thomason / Shinji Mitsuiki / David A. Agard / Brian A. Kelch / Ser Thr / /

/

Position

Proposed unfolding TS model for pro region dependent proteases / corresponding author / /

Product

NAPase / sodium acetate / potassium acetate / /

ProvinceOrState

Alabama / California / /

Technology

X-ray / Directed Mutagenesis / crystallization / /

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