Zobrazeno 1 - 10
of 18
pro vyhledávání: '"George J. Turner"'
Autor:
Lynell C. Martinez, George J. Turner
Publikováno v:
The Scientific World Journal, Vol 2, Pp 57-58 (2002)
Externí odkaz:
https://doaj.org/article/511f5dd1d12e438698f12925bf0c9f72
Autor:
Kirk G. Hines, Drake C. Mitchell, John J. Correia, George J. Turner, Lauren Pohren, Shirisha Chittiboyina
Publikováno v:
Biochemistry. 48:1112-1122
We examined functional and structural roles for the bacteriorhodopsin (bR) carboxyl-terminus. The extramembranous and intracellular carboxyl-terminus was deleted by insertion of premature translation stop codons. Deletion of the carboxyl-terminus had
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f43b26daca2096599a3a3fc32247813
https://doi.org/10.1021/bi801799j
https://doi.org/10.1021/bi801799j
Autor:
Lynell C. Martinez, George J. Turner
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1564(1):91-98
A high-throughput screening method has been developed which enables functional analysis of bacteriorhodpsin in whole cell pastes. Reflectance spectra, from as little as 5 ml of Halobacterium salinarum cells, show close correspondence to that obtained
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9180de7700468cb77b5289cb0705e7b
Publikováno v:
Proteins: Structure, Function, and Genetics. 48:269-282
We have performed cysteine scanning mutagenesis of the bacteriorhodopsin mutant D85N to explore the role of individual amino acids in the conformational transitions of the reprotonation mechanism. We have used whole-cell reflectance spectroscopy to e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a11d1be3acc44f3b30ecf8f6c943e04f
https://doi.org/10.1002/prot.10158
https://doi.org/10.1002/prot.10158
Autor:
George J. Turner, Thomas K. Harris
Publikováno v:
IUBMB Life (International Union of Biochemistry and Molecular Biology: Life). 53:85-98
In protein and RNA macromolecules, only a limited number of different side-chain chemical groups are available to function as catalysts. The myriad of enzyme-catalyzed reactions results from the ability of most of these groups to function either as n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b150407efbd674403f50092b6fa9fe0d
https://doi.org/10.1080/15216540211468
https://doi.org/10.1080/15216540211468
Autor:
Christopher J. Vineis, Jeremy A. Johnson, Mayank T. Bulsara, Eugene A. Fitzgerald, S. D. Calawa, George J. Turner, Keith A. Nelson, Alexei Maznev, T. C. Harman
The methodology for a heterodyned laser-induced transient thermal grating technique for non-contact, non-destructive measurements of thermal transport in opaque material is presented. Phase-controlled heterodyne detection allows us to isolate pure ph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60e3a6c95dce19a694d6cb8550432a3c
http://arxiv.org/abs/1109.6685
http://arxiv.org/abs/1109.6685
Autor:
Richard F. Shand, Alok K. Mitra, Mary C. Betlach, Robert M. Stroud, George J. Turner, Larry J. W. Miercke
Publikováno v:
Scopus-Elsevier
Highly ordered two-dimensional (2-D) crystals of Escherichia coli-expressed bacteriorhodopsin analog (e-bR) and its D96N variant (e-D96N) reconstituted in Halobacterium halobium lipids have been obtained by starting with the opsin protein purified in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c2091b1d08f690c901c565375dca445
Publikováno v:
Proteins: Structure, Function, and Genetics. 14:351-362
Recent crystallographic studies on the mutant human hemoglobin Ypsilanti (beta 99 Asp-->Tyr) have revealed a previously unknown quaternary structure called "quaternary Y" and suggested that the new structure may represent an important intermediate in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d24faabaf610dd0c3425e599029d23af
https://doi.org/10.1002/prot.340140304
https://doi.org/10.1002/prot.340140304
Autor:
Donald W. Pettigrew, Benjamin W. Turner, Winston F. Moo-Penn, Francine R. Smith, Bo E. Hedlund, Michael L. Doyle, George J. Turner, Gary K. Ackers, Frederic Galacteros, Donald L. Rucknagel
Publikováno v:
Proteins: Structure, Function, and Genetics. 14:333-350
Free energies of oxygen-linked subunit assembly and cooperative interaction have been determined for 34 molecular species of human hemoglobin, which differ by amino acid alterations as a result of mutation or chemical modification at specific sites.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ba74402946ce43d9bda8bf5ead925ab
https://doi.org/10.1002/prot.340140303
https://doi.org/10.1002/prot.340140303
Autor:
George J. Turner
Publisher Summary This chapter demonstrates the role played by mutational studies in determining the functional mechanism of a membrane protein model system, bacteriorhodopsin (bR). The combination of mutagenic and physical analyses can identify the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4db23fc15777303f607c2b01f1fd5943
https://doi.org/10.1016/s0091-679x(07)84016-7
https://doi.org/10.1016/s0091-679x(07)84016-7