The "two-state folder" MerP forms partially unfolded structures that show temperature dependent hydrogen exchange

Journal of Molecular Biology

Volumn 340, Issue 2, 2004, Pages 333-344

  Brorsson, Ann Christin ^a   Kjellson, Annika ^a   Aronsson, Göran ^b   Sethson, Ingmar ^a   Hambraeus, Charlotta ^c   Jonsson, Bengt Harald ^d  

^a UMEÅ UNIVERSITY   (Sweden)

^b Biopool AB   (Sweden)

^c SÖDERTÖRN UNIVERSITY   (Sweden)

^d LINKÖPING UNIVERSITY   (Sweden)

Author keywords

GuHCl, guanidine hydrochloride; HSQC, heteronuclear single quantum spectroscopy; hydrogen exchange; intermediate; partially unfolded; protein folding; protein stability

Indexed keywords

HYDROGEN; PROTEIN; PROTEIN MERP; UNCLASSIFIED DRUG;

AMINO ACID TRANSPORT; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; FLUORESCENCE ANALYSIS; ION EXCHANGE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON TRANSPORT; TEMPERATURE DEPENDENCE;

EID: 2942511345     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.05.003     Document Type: Article

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