Multiple conformational states in myoglobin revealed by frequency domain fluorometry
Open Access
- 21 February 1989
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 28 (4) , 1508-1512
- https://doi.org/10.1021/bi00430a013
Abstract
Note: In lieu of an abstract, this is the article's first page.Keywords
This publication has 16 references indexed in Scilit:
- Unfolding pathway of myoglobin: Molecular properties of intermediate formsArchives of Biochemistry and Biophysics, 1986
- Protein states and proteinquakes.Proceedings of the National Academy of Sciences, 1985
- Myoglobin structure and regulation of solvent accessibility of heme pocketInternational Journal of Peptide and Protein Research, 1985
- Picosecond fluorescence decay of tryptophans in myoglobin.Proceedings of the National Academy of Sciences, 1984
- Unfolding pathway of myoglobin. Evidence for a multistate processBiochemistry, 1983
- Heme and cysteine microenvironments of tuna apomyoglobin. Evidence of two independent unfolding regionsBiochemistry, 1982
- Location of structural domains in proteinsBiochemistry, 1981
- Tryptophanyl fluorescence heterogeneity of apomyoglobins. Correlation with the presence of two distinct structural domainsBiochemistry, 1981
- Temperature-dependent X-ray diffraction as a probe of protein structural dynamicsNature, 1979
- Amino acid composition and physico-chemical properties of bluefin tuna (Thunnus thynnus) myoglobinComparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1978