The PHY domain is required for conformational stability and spectral integrity of the bacteriophytochrome from Deinococcus radiodurans

Biochemical and Biophysical Research Communications

Volumn 369, Issue 4, 2008, Pages 1120-1124

  Yoon, Joo Mi ^a   Hahn, Tae Ryong ^a   Cho, Man Ho ^a   Jeon, Jong Seong ^a   Bhoo, Seong Hee ^a   Kwon, Yong Kook ^a  

^a Kyung Hee University   (South Korea)

Author keywords

Dark reversion; DrBphP; Pfr stabilization; Phytochrome; Surface topology

Indexed keywords

APOPROTEIN; BACTERIOPHYTOCHROME; PHYTOCHROME; RECOMBINANT PROTEIN; TRYPSIN; UNCLASSIFIED DRUG;

ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DEINOCOCCUS RADIODURANS; ELECTROPHORESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; DEINOCOCCUS; PHYTOCHROME; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SPECTRUM ANALYSIS; TRYPSIN;

DEINOCOCCUS RADIODURANS;

EID: 41149145039     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.03.001     Document Type: Article

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