Allosteric control in a metalloprotein dramatically alters function

Proceedings of the National Academy of Sciences of the United States of America

Volumn 110, Issue 3, 2013, Pages 948-953

  Baxter, Elizabeth Leigh ^a   Zuris, John A ^a   Wang, Charles ^a   Vo, Phu Luong T ^a   Axelrod, Herbert L ^b   Cohen, Aina E ^b   Paddock, Mark L ^a   Nechushtai, Rachel ^c   Onuchic, Jose N ^a,d   Jennings, Patricia A ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

^c HEBREW UNIVERSITY OF JERUSALEM   (Israel)

^d RICE UNIVERSITY   (United States)

Author keywords

Allostery; CISD1; Energy landscape theory; Iron sulfur cluster; Protein frustration

Indexed keywords

HISTIDINE; METALLOPROTEIN; MITONEET PROTEIN; UNCLASSIFIED DRUG;

ALLOSTERISM; ARTICLE; CONTROLLED STUDY; DIABETES MELLITUS; MUTAGENESIS; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; SIMULATION;

ALLOSTERIC REGULATION; BINDING SITES; BIOPHYSICAL PHENOMENA; CRYSTALLOGRAPHY, X-RAY; HISTIDINE; IRON-SULFUR PROTEINS; METALLOPROTEINS; MITOCHONDRIAL PROTEINS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PROTEIN CONFORMATION; PROTEIN STABILITY;

EID: 84872518004     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1208286110     Document Type: Article

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