Calorimetric determination of the energetics of the molten globule intermediate in protein folding: apo-.alpha.-lactalbumin
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00108a010
Reference36 articles.
1. Temperature dependence of the hydrophobic interaction in protein folding.
2. Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig .alpha.-lactalbumin
3. Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations
4. Molten globule intermediates and protein folding
5. α-lactalbumin: compact state with fluctuating tertiary structure?
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