Observed octameric assembly of a Plasmodium yoelii peroxiredoxin can be explained by the replacement of native "ball-and-socket" interacting residues by an affinity tag

Protein Science

Volumn 22, Issue 10, 2013, Pages 1445-1452

  Gretes, Michael C ^a,b   Karplus, P Andrew ^a,b  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^b OREGON STATE UNIVERSITY   (United States)

Author keywords

Artifact; Dimer interface; Hyperoxidation; Malaria; Peroxidase; Protein structure; Radiation damage; Structural genomics

Indexed keywords

PEROXIREDOXIN; PEROXIREDOXIN 1; PEROXIREDOXIN 1A; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; DISULFIDE BOND; NONHUMAN; PLASMODIUM YOELII; PRIORITY JOURNAL;

ARTIFACT; DIMER INTERFACE; HYPEROXIDATION; MALARIA; PEROXIDASE; PROTEIN STRUCTURE; RADIATION DAMAGE; STRUCTURAL GENOMICS;

AMINO ACID SEQUENCE; AMINO ACIDS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; GENETIC VARIATION; HUMANS; MALARIA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEROXIREDOXINS; PLASMODIUM YOELII; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTOZOAN PROTEINS;

EID: 84892926595     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2328     Document Type: Article

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