Effect of Self-Association on the Structural Organization of Partially Folded Proteins: Inactivated Actin
Open Access
- 30 November 1999
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 77 (5) , 2788-2800
- https://doi.org/10.1016/s0006-3495(99)77111-0
Abstract
No abstract availableKeywords
This publication has 74 references indexed in Scilit:
- Anion-induced folding of Staphylococcal nuclease: characterization of multiple equilibrium partially folded intermediatesJournal of Molecular Biology, 1998
- Protein Globularization During Folding. A Study by Synchrotron Small-angle X-ray ScatteringJournal of Molecular Biology, 1996
- Purification and characterization of the proteinase ECP 32 from Escherichia coli A2 strainBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1996
- Reversible Association of the Equilibrium Unfolding Intermediate of λ Cro RepressorJournal of Molecular Biology, 1996
- Two‐stage thermal unfolding of [Cys55]‐substituted Cro repressor of bacteriophage λFEBS Letters, 1991
- Physico‐chemical properties of actin cleaved with bacterial protease from E. coli A2 strainFEBS Letters, 1991
- α‐lactalbumin: compact state with fluctuating tertiary structure?FEBS Letters, 1981
- Ultra‐violet fluorescence of actin. Determination of native actin content in actin preparationsFEBS Letters, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- The interaction of a naphthalene dye with apomyoglobin and apohemoglobinJournal of Molecular Biology, 1965