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Volumn 39, Issue 30, 2000, Pages 8878-8887

The N-terminal fragment of human parathyroid hormone receptor 1 constitutes a hormone binding domain and reveals a distinct disulfide pattern

(9) Grauschopf, U a Lilie, H a Honold, K b Wozny, M b Reusch, D b Esswein, A b Schafer W b Rucknagel K P c Rudolph, R a

a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG (Germany)

b ROCHE DIAGNOSTICS GMBH (Germany)

c MAX PLANCK RESEARCH UNIT FOR ENZYMOLOGY OF PROTEIN FOLDING (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE; PARATHYROID HORMONE RECEPTOR;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CALORIMETRY; CIRCULAR DICHROISM; CYTOSOL; ESCHERICHIA COLI; HORMONE RECEPTOR INTERACTION; HUMAN; LIGAND BINDING; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN FOLDING; RECEPTOR AFFINITY; SURFACE PLASMON RESONANCE;

AMINO ACID SEQUENCE; BINDING SITES; CIRCULAR DICHROISM; DISULFIDES; ESCHERICHIA COLI; HUMANS; KINETICS; LIGANDS; MOLECULAR SEQUENCE DATA; PARATHYROID HORMONE; PEPTIDE FRAGMENTS; PROTEIN FOLDING; PROTEIN RENATURATION; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, PARATHYROID HORMONE; RECOMBINANT PROTEINS;

EID: 0034254482 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi0001426 Document Type: Article

Times cited : (106)

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