A new alternative method to quantify residual structure in 'unfolded' proteins

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1479, Issue 1-2, 2000, Pages 155-165

  Häckel, Marko ^a   Konno, Takashi ^b   Hinz, Hans Jürgen ^a  

^a UNIVERSITY OF MÜNSTER   (Germany)

^b NATIONAL INSTITUTE FOR PHYSIOLOGICAL SCIENCES   (Japan)

Author keywords

Amino acid; Calorimetry; Heat capacity; Hydration; Model compound; Protein thermodynamics; Unfolded state

Indexed keywords

CALPASTATIN;

CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; HUMAN; HYDRATION; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTEIN VARIANT; REVIEW; SWINE; TECHNIQUE; TEMPERATURE; THERMODYNAMICS;

SUS SCROFA;

EID: 0342264518     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(00)00051-0     Document Type: Article

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