Cold denaturation of a protein dimer monitored at atomic resolution

Nature Chemical Biology

Volumn 9, Issue 4, 2013, Pages 264-270

  Jaremko, Mariusz ^a,b   Jaremko, Łukasz ^a,c   Kim, Hai Young ^a   Cho, Min Kyu ^a   Schwieters, Charles D ^d   Giller, Karin ^a   Becker, Stefan ^a   Zweckstetter, Markus ^a,e  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^b INSTITUTE OF BIOCHEMISTRY AND BIOPHYSICS   (Poland)

^c UNIVERSITY OF WARSAW   (Poland)

^d NATIONAL INSTITUTES OF HEALTH   (United States)

^e GERMAN CENTER FOR NEURODEGENERATIVE DISEASES DZNE   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DIMER; HOMODIMER; MONOMER; PROTEIN CYLR2; REPRESSOR PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; COLD; DISSOCIATION; ENTEROCOCCUS FAECALIS; HYDRODYNAMICS; LOW TEMPERATURE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FUNCTION; PROTEIN STRUCTURE; PROTEIN UNFOLDING; TEMPERATURE;

BACTERIAL PROTEINS; BINDING SITES; COLD TEMPERATURE; CYTOTOXINS; DNA, BACTERIAL; ENTEROCOCCUS FAECALIS; ESCHERICHIA COLI; MODELS, MOLECULAR; MOLECULAR CONFORMATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROMOTER REGIONS, GENETIC; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN UNFOLDING; RECOMBINANT PROTEINS;

EID: 84875442036     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1181     Document Type: Article

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