Concentration-temperature superposition of helix folding rates in gelatin.
Using optical rotation as the primary technique, we have characterized the kinetics of helix renaturation in water solutions of gelatin. By covering a wide range of solution concentrations we identify a universal exponential dependence of folding rate on concentration and quench temperature. We demonstrate a new concentration-temperature superposition of data at all temperatures and concentrations, and build the corresponding master curve. The normalized rate constant is consistent with helix lengthening. Nucleation of the triple helix occurs rapidly and contributes less to the helical onset than previously thought.
Cavendish Laboratory, University of Cambridge, J J Thomson Avenue, Cambridge CB3 0HE, United Kingdom.
J L
JL
Gornall
E M
EM
Terentjev
D001703:Biophysics / Q000379:methods*; D002152:Calorimetry, Differential Scanning; D004305:Dose-Response Relationship, Drug; D005780:Gelatin / Q000737:chemistry*; D005898:Glass; D007700:Kinetics; D044367:Phase Transition; D011108:Polymers / Q000737:chemistry; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D013696:Temperature; D013816:Thermodynamics; D013997:Time Factors; D014867:Water / Q000737:chemistry
D011108:Polymers; D014867:Water; D005780:Gelatin