Plant metallothionein domains: functional insight into physiological metal binding and protein folding

Biochimie

Volumn 88, Issue 6, 2006, Pages 583-593

  Domènech, Jordi ^a   Mir, Gisela ^b   Huguet, Gemma ^b   Capdevila, Mercè ^c   Molinas, Marisa ^b   Atrian, Sílvia ^a  

^a UNIVERSITY OF BARCELONA   (Spain)

^b UNIVERSITY OF GIRONA   (Spain)

^c UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

Author keywords

Cu aggregates; Metallothionein; MT dimers; Quercus suber; Separate Cys rich domains; Spacer region; Yeast complementation; Zn aggregates

Indexed keywords

COPPER; CYSTEINE; GLYCINE; METALLOTHIONEIN; PEPTIDE DERIVATIVE; ZINC;

AMINO TERMINAL SEQUENCE; ARTICLE; ATOMIC EMISSION SPECTROMETRY; CARBOXY TERMINAL SEQUENCE; CELLULAR DISTRIBUTION; CHIMERA; CONTROLLED STUDY; ELECTROSPRAY MASS SPECTROMETRY; METAL BINDING; METAL TOLERANCE; NONHUMAN; PROTEIN DOMAIN; PROTEIN FOLDING; ULTRAVIOLET SPECTROSCOPY; YEAST CELL;

BASE SEQUENCE; BINDING SITES; CHELATING AGENTS; COPPER; METALLOTHIONEIN; METALS; MOLECULAR SEQUENCE DATA; PLANT PROTEINS; PLANTS; PROTEIN BINDING; PROTEIN FOLDING; ZINC;

ANIMALIA;

EID: 33745940302     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2005.11.002     Document Type: Article

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