De novo design of a non-natural fold for an iron-sulfur protein: Alpha-helical coiled-coil with a four-iron four-sulfur cluster binding site in its central core

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1797, Issue 3, 2010, Pages 406-413

  Grzyb, Joanna ^a,d   Xu, Fei ^b   Weiner, Lev ^a   Reijerse, Eduard J ^c   Lubitz, Wolfgang ^c   Nanda, Vikas ^b   Noy, Dror ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^b RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

^c MAX PLANCK INSTITUTE FOR CHEMICAL ENERGY CONVERSION   (Germany)

^d INSTITUTE OF PHYSICS   (Poland)

Author keywords

Coiled coil; EPR spectroscopy; Four helix bundle; Iron sulfur cluster; Protein de novo design; Redox enzyme

Indexed keywords

APOPROTEIN; DITHIONITE; IRON SULFUR PROTEIN; RECOMBINANT PROTEIN;

ACCELERATION; ARTICLE; BINDING SITE; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; ESCHERICHIA COLI; GEL FILTRATION; HYDROPHOBICITY; IN VITRO STUDY; NONHUMAN; OXIDATION REDUCTION POTENTIAL; POWER SPECTRUM; PRIORITY JOURNAL; PROCESS DESIGN; PROCESS OPTIMIZATION; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN PURIFICATION; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE; ULTRACENTRIFUGATION; ULTRAVIOLET RADIATION;

AMINO ACID SEQUENCE; BINDING SITES; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; COMPUTATIONAL BIOLOGY; ELECTRON SPIN RESONANCE SPECTROSCOPY; HUMANS; IRON; IRON-SULFUR PROTEINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PROTEIN FOLDING; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SPECTROPHOTOMETRY, ULTRAVIOLET; SULFUR; ULTRACENTRIFUGATION;

EID: 75649133240     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2009.12.012     Document Type: Article

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