ArticleBiophysical journal2003
15N-1H Residual dipolar coupling analysis of native and alkaline-K79A Saccharomyces cerevisiae cytochrome c.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 47 citations in OpenAlex.
- Concurrent Identification and Characterization of Protein Structure and Continuous Internal Dynamics with REDCRAFT.Frontiers in molecular biosciences · 2022Article
- REDCRAFT: A computational platform using residual dipolar coupling NMR data for determining structures of perdeuterated proteins in solution.PLoS computational biology · 2021Article
- Distal Unfolding of Ferricytochrome c Induced by the F82K Mutation.International journal of molecular sciences · 2020Article
- Histidine-Lysine Axial Ligand Switching in a Hemoglobin: A Role for Heme Propionates.Biochemistry · 2018Article
- Effect of methionine80 heme coordination on domain swapping of cytochrome c.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Article
- A Compact Structure of Cytochrome c Trapped in a Lysine-Ligated State: Loop Refolding and Functional Implications of a Conformational Switch.Journal of the American Chemical Society · 2015Article
- Improvements to REDCRAFT: a software tool for simultaneous characterization of protein backbone structure and dynamics from residual dipolar couplings.Journal of biomolecular NMR · 2014Article
- Dynafold: a dynamic programming approach to protein backbone structure determination from minimal sets of Residual Dipolar Couplings.Journal of bioinformatics and computational biology · 2014Article
- Advances in the REDCAT software package.BMC bioinformatics · 2013Article
- Protein structure validation and identification from unassigned residual dipolar coupling data using 2D-PDPA.Molecules (Basel, Switzerland) · 2013Article
- Narrowing the conformational space sampled by two-domain proteins with paramagnetic probes in both domains.Journal of biomolecular NMR · 2011Article
- Simultaneous structure and dynamics of a membrane protein using REDCRAFT: membrane-bound form of Pf1 coat protein.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2010Article
- Estimation of relative order tensors, and reconstruction of vectors in space using unassigned RDC data and its application.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2008Article
- REDCRAFT: a tool for simultaneous characterization of protein backbone structure and motion from RDC data.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2008Article
- Conformational stability and dynamics of cytochrome c affect its alkaline isomerization.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2007Article
- Molecular statistics of cytochrome c: structural plasticity and molecular environment.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2007Article
- Determination of protein backbone structures from residual dipolar couplings.Methods in enzymology · 2005Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Residual dipolar couplings (RDCs) and pseudocontact shifts are experimentally accessible properties in nuclear magnetic resonance that are related to structural parameters and to the magnetic susceptibility anisotropy. We have determined RDCs due to field-induced orientation of oxidized-K79A and reduced cytochrome c at pH 7.0 and oxidized-K79A cytochrome c at pH 11.1 through measurements of amide (15)N-(1)H (1)J couplings at 800 and 500 MHz. The pH 7.0 RDCs for Fe(III)- and Fe(II)-cytochrome c together with available nuclear Overhauser effects were used to recalculate solution structures that were consistent with both sets of constraints. Molecular magnetic susceptibility anisotropy values were calculated for both redox states of the protein. By subtracting the residual dipolar couplings (RDCs) of the reduced form from those of the oxidized form measured at the same magnetic field (800 MHz), we found the RDC contribution of the paramagnetic metal ion in the oxidized protein. The magnetic susceptibility anisotropy, which was calculated from the structure, was found to be the same as that of the paramagnetic metal ion obtained independently from pseudocontact shifts, thereby indicating that the elements of secondary structure either are rigid or display the same mobility in both oxidation states. The residual dipolar coupling values of the alkaline-K79A form are small with respect to those of oxidized native cytochrome, whereas the pseudocontact shifts are essentially of the same magnitude, indicating local mobility. Importantly, this is the first time that mobility has been found through comparison of RDCs with pseudocontact shifts.
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