Apoprotein structure and metal binding characterization of a de Novo designed peptide, α3DIV, that sequesters toxic heavy metals

Biochemistry

Volumn 54, Issue 18, 2015, Pages 2858-2873

  Plegaria, Jefferson S ^a   Dzul, Stephen P ^c   Zuiderweg, Erik R P ^b   Stemmler, Timothy L ^c   Pecoraro, Vincent L ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^c WAYNE STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BOND LENGTH; CADMIUM COMPOUNDS; CONFORMATIONS; DIHEDRAL ANGLE; EXTENDED X RAY ABSORPTION FINE STRUCTURE SPECTROSCOPY; HEAVY METALS; LEAD COMPOUNDS; MERCURY COMPOUNDS; PEPTIDES; SCAFFOLDS (BIOLOGY); X RAY ABSORPTION;

COORDINATION ENVIRONMENT; DE NOVO PROTEIN DESIGN; EXTENDED X-RAY ABSORPTION FINE STRUCTURE ANALYSIS; FUNDAMENTAL CHARACTERISTICS; LOWEST ENERGY STRUCTURE; METALLOREGULATORY PROTEIN; ROOT MEAN SQUARE DEVIATIONS; SOLUTION STRUCTURES;

STRUCTURAL DESIGN;

ALPHA3DIV PEPTIDE; APOPROTEIN; CADMIUM; HEAVY METAL; LEAD; MERCURY; PEPTIDE; UNCLASSIFIED DRUG; CYSTEINE; DIVALENT CATION; METALLOPROTEIN; POLLUTANT; PROTEIN BINDING; SOLUTION AND SOLUBILITY;

ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; METAL BINDING; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; X RAY ABSORPTION SPECTROSCOPY; AMINO ACID SEQUENCE; BINDING SITE; CHEMICAL PHENOMENA; CHEMISTRY; MOLECULAR GENETICS; PH; POLLUTANT; PROTEIN ENGINEERING; PROTEIN SECONDARY STRUCTURE; SOLUTION AND SOLUBILITY;

AMINO ACID SEQUENCE; APOPROTEINS; BINDING SITES; CADMIUM; CATIONS, DIVALENT; CYSTEINE; ENVIRONMENTAL POLLUTANTS; HYDROGEN-ION CONCENTRATION; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; LEAD; MERCURY; METALLOPROTEINS; METALS, HEAVY; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PROTEIN BINDING; PROTEIN ENGINEERING; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS;

EID: 84929303453     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00064     Document Type: Article

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