Non-functional conserved residues in globins and their possible role as a folding nucleus 1 1Edited by F. E. Cohen
- 1 August 1999
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 291 (3) , 671-682
- https://doi.org/10.1006/jmbi.1999.2920
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein foldingNature Structural & Molecular Biology, 1998
- Specific Nucleus as the Transition State for Protein Folding: Evidence from the Lattice ModelBiochemistry, 1994
- Pulsed H/D-exchange studies of folding intermediatesCurrent Opinion in Structural Biology, 1993
- Haemoglobin of the Antarctic fish Pagothenia bernacchiiJournal of Molecular Biology, 1992
- Glycera dibranchiata hemoglobinJournal of Molecular Biology, 1989
- Progressive sequence alignment as a prerequisitetto correct phylogenetic treesJournal of Molecular Evolution, 1987
- Determinants of a protein foldJournal of Molecular Biology, 1987
- The crystal structure of human deoxyhaemoglobin at 1.74 Å resolutionJournal of Molecular Biology, 1984
- The cytochrome fold and the evolution of bacterial energy metabolismJournal of Molecular Biology, 1976
- The Structure and History of an Ancient ProteinScientific American, 1972