Electrophoretic analysis of the unfolding of proteins by urea
- 1 April 1979
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 129 (2), 235-264
- https://doi.org/10.1016/0022-2836(79)90279-1
Abstract
No abstract availableThis publication has 151 references indexed in Scilit:
- Papain denaturation is not a two‐state transitionFEBS Letters, 1978
- Nuclear magnetic resonance evidence for a structural intermediate at an early stage in the refolding of ribonuclease AJournal of Molecular Biology, 1978
- Three-state denaturation of α-lactalbumin by guanidine hydrochlorideJournal of Molecular Biology, 1976
- The nature of the accessible and buried surfaces in proteinsJournal of Molecular Biology, 1976
- The heat-unfolded state of ribonuclease A is an equilibrium mixture of fast and slow refolding speciesJournal of Molecular Biology, 1975
- A comparison of the denatured states of α-lactalbumin and lysozymeJournal of Molecular Biology, 1974
- A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric studyJournal of Molecular Biology, 1974
- Thermal investigations of biopolymer solutions and scanning microcalorimetryFEBS Letters, 1974
- A possible three-dimensional structure of bovine α-lactalbumin based on that of hen's egg-white lysozymeJournal of Molecular Biology, 1969
- The correlation of ribonuclease activity with specific aspects of tertiary structureBiochimica et Biophysica Acta, 1957