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Journal of Biomolecular NMR|July 29, 1998
Detailed NMR analysis of the heme-protein interactions in component IV Glycera dibranchiata monomeric hemoglobin-COS L Alam, B F Volkman, J L Markley, et al.Biochemistry|January 28, 1992
Solution studies of staphylococcal nuclease H124L. 1. Backbone 1H and 15N resonances and secondary structure of the unligated enzyme as identified by three-dimensional NMR spectroscopyJ F Wang, E S Mooberry, W F Walkenhorst, et al.Virology|October 30, 1983
Carbon-13 and proton nuclear magnetic resonance spectroscopy of plant viruses: evidence for protein-nucleic acid interactions in belladonna mottle virus and detection of polyamines in turnip yellow mosaic virusR Virudachalam, K Sitaramant, K L Heusst, et al.Biochemistry|March 26, 1996
High-pressure denaturation of staphylococcal nuclease proline-to-glycine substitution mutantsG J Vidugiris, D M Truckses, J L Markley, et al.Biochemistry|January 12, 1988
Flavodoxin from Anabaena 7120: uniform nitrogen-15 enrichment and hydrogen-1, nitrogen-15, and phosphorus-31 NMR investigations of the flavin mononucleotide binding site in the reduced and oxidized statesB J Stockman, W M Westler, E S Mooberry, et al.Biochemistry|August 7, 1998
Solution structure and backbone dynamics of component IV Glycera dibranchiata monomeric hemoglobin-COB F Volkman, S L Alam, J D Satterlee, et al.Archives of Biochemistry and Biophysics|January 6, 2000
Electron-nuclear interactions in two prototypical [2Fe-2S] proteins: selective (chiral) deuteration and analysis of (1)H and (2)H NMR signals from the alpha and beta hydrogens of cysteinyl residues that ligate the iron in the active sites of human ferredoxin and Anabaena 7120 vegetative ferredoxinB Xia, D Jenk, D M LeMaster, et al.The Journal of Biological Chemistry|March 25, 1982
Changes in the natural abundance 13C NMR spectra of intact frog muscle upon storage and caffeine contractureM Bárány, D D Doyle, G Graff, et al.Magnetic Resonance in Medicine|March 1, 1984
Natural abundance 13C NMR spectra of human muscle, normal and diseasedM Bárány, D D Doyle, G Graff, et al.Biochemistry|April 23, 1991
Refinement of the NMR solution structure of a protein to remove distortions arising from neglect of internal motionJ Fejzo, A M Krezel, W M Westler, et al.Pageof 16