Zobrazeno 1 - 10
of 39
pro vyhledávání: '"Christopher J. Falzone"'
Autor:
Ananya Majumdar, David A. Vuletich, Juliette T. J. Lecomte, Christopher J. Falzone, Matthew P. Pond
Publikováno v:
Biomolecular NMR Assignments. 3:211-214
The hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 is a monomeric 123-residue Group I 2/2 hemoglobin. Here, we report (1)H, (15)N, and (13)C assignments for the ferric (low-spin, S = (1/2)) protein with a b heme cofactor and after post
Autor:
John H. Golbeck, Eckhard Bill, Carolyn E. Lubner, Estelle M. Maes, Mikhail L. Antonkine, Ramakrishnan Balasubramanian, Christopher J. Falzone, Christoph Breitenstein, Donald A. Bryant, Roman S. Czernuszewicz
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1767:712-724
Chemical rescue of site-modified amino acids using externally supplied organic molecules represents a powerful method to investigate structure-function relationships in proteins. Here we provide definitive evidence that aryl and alkyl thiolates, reag
Publikováno v:
Biochemistry. 45:14075-14084
The recombinant two-on-two hemoglobin from the cyanobacterium Synechoccocus sp. PCC 7002 (S7002 rHb) is a bishistidine hexacoordinate globin capable of forming a covalent cross-link between a heme vinyl and a histidine in the C-terminal helix (H heli
Autor:
Henry J. Nothnagel, Juliette T. J. Lecomte, David A. Vuletich, B. Christie Vu, Christopher J. Falzone
Publikováno v:
Biochemistry. 43:12622-12633
The truncated hemoglobin (Hb) from the cyanobacterium Synechocystis sp. PCC 6803 is a bis-histidyl hexacoordinate complex in the absence of exogenous ligands. This protein can form a covalent cross-link between His117 in the H-helix and the heme 2-vi
Autor:
Juliette T. J. Lecomte, David A. Vuletich, Christopher J. Falzone, Syna A. Kuriakose, B. Christie Vu
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 9:183-194
The recombinant product of the hemoglobin gene of the cyanobacterium Synechocystis sp. PCC 6803 forms spontaneously a covalent bond linking one of the heme vinyl groups to a histidine located in the C-terminal helix (His117, or H16). The present repo
Publikováno v:
Protein Science. 12:185-191
The alpha subunit of tryptophan synthase (alphaTS) from S. typhimurium belongs to the triosephosphate isomerase (TIM) or the (beta/alpha)(8) barrel fold, one of the most common structures in biology. To test the conservation of the global fold in the
Publikováno v:
Biochemistry. 40:6541-6552
The product of the cyanobacterium Synechocystis sp. PCC 6803 gene slr2097 is a 123 amino acid polypeptide chain belonging to the truncated hemoglobin family. Recombinant, ferric heme-reconstituted Synechocystis sp. PCC 6803 hemoglobin is a low-spin c
Autor:
Juliette T. J. Lecomte, Christopher J. Falzone, Shibani Bhattacharya, Nancy L. Scott, B.C. Vu, Y. Wang
Publikováno v:
Biochemistry. 40:4879-4891
The water-soluble domain of rat hepatic cytochrome b(5) undergoes marked structural changes upon heme removal. The solution structure of apocytochrome b(5) shows that the protein is partially folded in the absence of the heme group, exhibiting a stab
Publikováno v:
Protein Science. 8:1484-1491
Apomyoglobin from sperm whale is often used for studies of ligand binding, protein folding, and protein stability. In an effort to describe its conformational properties in solution, homonuclear and heteronuclear (13C and 15N) NMR methods were applie
Publikováno v:
eLS
Proteins are linear polypeptides made out of a small set of amino acids. The chemical diversity of the building blocks is limited, but a protein's covalent structure can be amended in vivo so that unusual linkages are introduced and new functionaliti