Why reversing the sequence of the α domain of human metallothionein-2 does not change its metal-binding and folding characteristics

European Journal of Biochemistry

Volumn 266, Issue 1, 1999, Pages 33-39

  Pan, Peter Kuan Yeu ^a   Zheng, Z F ^a   Lyu, P C ^a   Huang, P C ^a,b,c  

^a NATIONAL TSING HUA UNIVERSITY   (Taiwan)

^b JOHNS HOPKINS UNIVERSITY   (United States)

^c JOHNS HOPKINS BLOOMBERG SCHOOL OF PUBLIC HEALTH   (United States)

Author keywords

Folding nucleus; Metal binding protein; Metallothiohein; Protein design; Retro protein

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); AMINO ACID; CADMIUM; CYSTEINE; METALLOTHIONEIN;

ACIDIFICATION; AMINO ACID SEQUENCE; ARTICLE; CIRCULAR DICHROISM; HUMAN; METAL BINDING; PEPTIDE ANALYSIS; PEPTIDE SYNTHESIS; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; ULTRAVIOLET SPECTROSCOPY;

AMINO ACID SEQUENCE; ANIMALS; CADMIUM; CIRCULAR DICHROISM; CYSTEINE; DINITROBENZENES; HUMANS; METALLOTHIONEIN; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RATS;

EID: 0033571050     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00811.x     Document Type: Article

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