Structural propensities in the heme binding region of apocytochrome b5. II. Heme conjugates

Biopolymers - Peptide Science Section

Volumn 90, Issue 4, 2008, Pages 556-566

  Davis Jr , Ronald B ^a,b   Lecomte, Juliette T J ^a,c  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

^b AMERICAN UNIVERSITY   (United States)

^c JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Apoprotein; Coil helix equilibria; Intrinsic disorder; Trifluoroethanol

Indexed keywords

PORPHYRINS;

APO CYTOCHROME; APOPROTEIN; COIL-HELIX EQUILIBRIA; HEME COFACTOR; HEME-BINDING; INTRINSIC DISORDER; MICROSOMAL CYTOCHROME; TRIFLUOROETHANOL;

HEMOGLOBIN;

CYTOCHROME B5; HEME; HISTIDINE 63; HISTIDINE DERIVATIVE; PEPTIDE; PEPTIDE BLP 22; PEPTIDE BLP 22C; PEPTIDE BLP 42; PEPTIDE BLP 8; PEPTIDE H4; PEPTIDE H5; TRIFLUOROETHANOL; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; CHEMICAL BOND; CONJUGATION; HEME BINDING; LIGAND BINDING; PH; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN SYNTHESIS; SEQUENCE ANALYSIS; SPECTROSCOPY; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; CYTOCHROMES B5; HEME; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; RATS; SPECTROPHOTOMETRY, ULTRAVIOLET; TITRIMETRY; TRIFLUOROETHANOL;

RATTUS;

EID: 52949135132     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.20995     Document Type: Article

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