1H and 15N resonance assignments and secondary structure of the carbon monoxide complex of sperm whale myoglobin |
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| Authors: | Yves Thériault Thomas C. Pochapsky Claudio Dalvit Mark L. Chiu Stephen G. Sligar Peter E. Wright |
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| Affiliation: | (1) Department of Molecular Biology, The Scripps Research Institute, 92037 La Jolla, CA, U.S.A.;(2) Department of Biochemistry and Chemistry, University of Illinois, 61801 Urbana, IL, U.S.A.;(3) Present address: Ontogen Corporation, 92009 Carlsbad, CA, U.S.A.;(4) Present address: Department of Chemistry, Brandeis University, 02254 Waltham, MA, U.S.A.;(5) Present address: Sandoz Pharma, CH-4002 Basel, Switzerland |
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| Abstract: | Summary Sequence-specific backbone 1H and 15N resonance assignments have been made for 95% of the amino acids in sperm whale myoglobin, complexed with carbon monoxide (MbCO). Many assignments for side-chain resonances have also been obtained. Assignments were made by analysis of an extensive series of homonuclear 2D spectra, measured with unlabeled protein, and both 2D and 3D 1H-15N-correlated spectra obtained from uniformly 15N-labeled myoglobin. Patterns of medium-range NOE connectivities indicate the presence of eight helices in positions that are very similar to those found in the crystal structures of sperm whale myoglobin. The resonance assignments of MbCO form the basis for determination of the solution structure and for hydrogen-exchange measurements to probe the stability and folding pathways of myoglobin. They will also form a basis for assignment of the spectra of single-site mutants with altered ligand-binding properties. |
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| Keywords: | Heme protein Multidimensional NMR Sequential assignment |
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