Výsledky vyhledávání - "Krishnakumar Rajarathnam"

1H NMR evidence that Glu-38 interacts with the N-terminal functional domain in interleukin-8

Autor: Ian Clark-Lewis, Beatrice Dewald, Brian D. Sykes, Krishnakumar Rajarathnam, Marco Baggiolini

Publikováno v: FEBS Letters. 399:43-46

In order to assess the importance of the buried Glu-38 observed in the structure of interleukin-8, an analog in which Glu-38 was replaced with Ala (E38A analog) was investigated by 1H NMR spectroscopy and neutrophil activation. Detailed analysis of t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff788121830b0e6a7da524da3ed0a76f
https://doi.org/10.1016/s0014-5793(96)01277-x

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Structural characterization of a monomeric chemokine: Monocyte chemoattractant protein-3

Autor: Key-Sun Kim, Ian Clark-Lewis, Krishnakumar Rajarathnam, Brian D. Sykes

Publikováno v: FEBS Letters. 395:277-282

1H-NMR spectroscopy and analytical ultracentrifugation studies reveal that monocyte chemoattractant protein-3 (MCP-3) is a monomer. NMR solution structure shows that MCP-3 adopts an alphabeta fold similar to what is observed in structures of other kn

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a98ce93e41d4a6188d8d55968d3edaf
https://doi.org/10.1016/0014-5793(96)01024-1

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1H NMR Solution Structure of an Active Monomeric Interleukin-8

Autor: Brian D. Sykes, Ian Clark-Lewis, Krishnakumar Rajarathnam

Publikováno v: Biochemistry. 34:12983-12990

The solution structure of a monomeric form of interleukin-8 (IL-8) has been solved using 1H NMR spectroscopy. The chemically synthesized nonnatural analog [IL-8 (4-72) L25 NH-->NCH3] has the same activity as that of native IL-8. Thirty structures wer

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82af5798c9175dbef5d927bdd3f8ccb8
https://doi.org/10.1021/bi00040a008

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A Double Mutant of Sperm Whale Myoglobin Mimics the Structure and Function of Elephant Myoglobin

Autor: Xuefeng Zhao, K. Vyas, Bao D. Nguyen, Krishnakumar Rajarathnam, Gerd N. La Mar, Tiansheng Li, George N. Phillips, Raymund F. Eich, John S. Olson, Jinshu Ling, David F. Bocian

Publikováno v: Journal of Biological Chemistry. 270:20763-20774

The functional, spectral, and structural properties of elephant myoglobin and the L29F/H64Q mutant of sperm whale myoglobin have been compared in detail by conventional kinetic techniques, infrared and resonance Raman spectroscopy, 1H NMR, and x-ray

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a70009668244fe92e266b47a46d75450
https://doi.org/10.1074/jbc.270.35.20763

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Correlation between the Steric Bulk of the Distal E7 and E11 Residues and the Tilt of the FeCN Unit in Cyanometmyoglobin As Determined by NMR from the Orientation of the Magnetic Axes in Single and Double Point Mutants

Autor: Krishnakumar Rajarathnam, Gerd N. La Mar, Jun Qin, Mark L. Chiu, Stephen G. Sligar

Publikováno v: Biochemistry. 33:5493-5501

The amino acids in the heme pocket of sperm whale myoglobin single E11 and double E7 and E11 point mutants in the metcyano form have been assigned by NMR methods to assess the role of steric bulk in modulating ligand tilt. The five mutants investigat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b385d0c246c42472852eee6d0e7fd86
https://doi.org/10.1021/bi00184a018

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1H NMR investigation of the heme cavity of elephant (E7 Gln) met-cyano-myoglobin. Evidence for a B-helix phenylalanine interaction with bound ligand

Autor: K. Vyas, G. N. La Mar, Ramaswamy Krishnamoorthi, S.D. Emerson, Liping Yu, H Mizukami, Krishnakumar Rajarathnam

Publikováno v: Journal of Biological Chemistry. 268:14826-14835

A combination of one- and two-dimensional NMR experiments has been used to identify and spatially locate the heme pocket residues in the paramagnetic, low spin, met-cyano complex of elephant myoglobin. In addition to assigning resonances of the conse

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4c81dea7da3c157963028e7e02373bb0
https://doi.org/10.1016/s0021-9258(18)82408-5

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Solution structure determination of the heme cavity in the E7 His .fwdarw. Val cyano-Met myoglobin point mutant based on the proton NMR detected dipolar field of the iron: Evidence for contraction of the heme pocket

Autor: Gerd N. La Mar, Jun Qin, Krishnakumar Rajarathnam, Mark L. Chiu, Stephen G. Sligar

Publikováno v: Biochemistry. 32:5670-5680

The 1H NMR spectrum of the cyanomet complex of the sperm whale His[E7]Val myoglobin (Mb) point mutant has been analyzed by 2D methods to yield the assignments for the active site residues, including the substituted Val E7. The dipolar shifted proxima

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::90bebc9525b3a7507d4321604c4cb2be
https://doi.org/10.1021/bi00072a024

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Determination of the orientation of the magnetic axes of the cyano-MetMb complexes of point mutants of myoglobin by solution 1H NMR: influence of his E7 .fwdarw. Gly and Arg CD3 .fwdarw. Gly substitutions

Autor: Krishnakumar Rajarathnam, Mark L. Chiu, Stephen G. Sligar, Gerd N. La Mar

Publikováno v: Journal of the American Chemical Society. 114:9048-9058

A method is described for obtaining the axes of the diagonal paramagnetic susceptibility tensor for the low-spin cyanide complexes of distal point mutants of ferric sperm whale myoglobin (metMbCN). It relies on using the crystal coordinates of the wi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f3c2e06475ec98c48062b00249ccd7e9
https://doi.org/10.1021/ja00049a042

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