Studies of the collagen-like peptide (Pro-Pro-Gly)10 confirm that the shape and position of the type I collagen denaturation endotherm is governed by the rate of helix unfolding

Journal of Molecular Biology

Volumn 337, Issue 4, 2004, Pages 917-931

  Miles, Christopher A ^a   Bailey, Allen J ^a  

^a UNIVERSITY OF BRISTOL   (United Kingdom)

Author keywords

(Pro Pro Gly)10; Collagen; Denaturation; Differential equation; DSC, the differential scanning calorimetry; Helix coil transition

Indexed keywords

COLLAGEN; PEPTIDE;

ARTICLE; CONCENTRATION RESPONSE; DIFFERENTIAL SCANNING CALORIMETRY; ENTHALPY; EQUILIBRIUM CONSTANT; KINETICS; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; TEMPERATURE DEPENDENCE;

EID: 1642369882     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.02.012     Document Type: Article

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