Related ArticlesClosed form of liganded glutamine-binding protein by rotational-echo double-resonance NMR.
Biochemistry. 1997 Aug 5;36(31):9405-8
Authors: Klug CA, Tasaki K, Tjandra N, Ho C, Schaefer J
Rotational-echo double-resonance NMR has been used to determine internuclear distances in the complex of glutamine-binding protein and its ligand, l-glutamine. The distances between the ligand and Tyr185 are consistent with the results of molecular dynamics simulations constrained by three REDOR-determined distances to His156. This model is also consistent with six other REDOR-determined internuclear distances, most of which agree with values from the first report of an X-ray structure of the complex of glutamine-binding protein and l-glutamine.
[NMR paper] Rotational-echo double-resonance NMR-restrained model of the ternary complex of 5-eno
Rotational-echo double-resonance NMR-restrained model of the ternary complex of 5-enolpyruvylshikimate-3-phosphate synthase.
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J Biomol NMR. 2004 Jan;28(1):11-29
Authors: McDowell LM, Poliks B, Studelska DR, O'Connor RD, Beusen DD, Schaefer J
The 46-kD enzyme 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the condensation of shikimate-3-phosphate (S3P) and phosphoenolpyruvate to form EPSP....
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[NMR paper] NMR assignment of the A form of the pheromone-binding protein of Bombyx mori.
NMR assignment of the A form of the pheromone-binding protein of Bombyx mori.
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J Biomol NMR. 2001 Jan;19(1):79-80
Authors: Horst R, Damberger F, Peng G, Nikonova L, Leal WS, Wüthrich K
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[NMR paper] NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein i
NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein involved in bacterial mercuric ion resistance.
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Biochemistry. 1998 Jun 30;37(26):9316-22
Authors: Qian H, Sahlman L, Eriksson PO, Hambraeus C, Edlund U, Sethson I
Mercuric ions are toxic to living organisms because of their strong affinity for cysteine residues in proteins. Some bacteria have developed a resistance...
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[NMR paper] In situ analysis of peptidyl DOPA in mussel byssus using rotational-echo double-reson
In situ analysis of peptidyl DOPA in mussel byssus using rotational-echo double-resonance NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles In situ analysis of peptidyl DOPA in mussel byssus using rotational-echo double-resonance NMR.
Arch Biochem Biophys. 1996 Sep 1;333(1):221-4
Authors: Klug CA, Burzio LA, Waite JH, Schaefer J
Rotational-echo double-resonance (REDOR) 13C NMR spectra with 2H dephasing have been obtained from plaques and threads from the byssus of...
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[NMR paper] An investigation of the ligand-binding site of the glutamine-binding protein of Esche
An investigation of the ligand-binding site of the glutamine-binding protein of Escherichia coli using rotational-echo double-resonance NMR.
Related Articles An investigation of the ligand-binding site of the glutamine-binding protein of Escherichia coli using rotational-echo double-resonance NMR.
Biochemistry. 1994 Jul 26;33(29):8651-61
Authors: Hing AW, Tjandra N, Cottam PF, Schaefer J, Ho C
Glutamine-binding protein (GlnBP) is an essential component of the glutamine transport system in Escherichia coli. Rotational-echo double-resonance...
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[NMR paper] Two-dimensional, rotational-echo double-resonance NMR of cell culture metabolism.
Two-dimensional, rotational-echo double-resonance NMR of cell culture metabolism.
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J Biol Chem. 1993 Oct 5;268(28):20768-71
Authors: McDowell LM, Cohen ER, Schaefer J
Two-dimensional, rotational-echo double-resonance 13C NMR, a new solid-state NMR technique, has been used to show that the relative fluxes of the labeled chemical bond of L-serine along four metabolic pathways (direct purine synthesis, direct glycine incorporation into protein,...
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[NMR paper] Multidimensional 1H and 15N NMR investigation of glutamine-binding protein of Escheri
Multidimensional 1H and 15N NMR investigation of glutamine-binding protein of Escherichia coli.
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J Biomol NMR. 1992 Mar;2(2):149-60
Authors: Tjandra N, Simplaceanu V, Cottam PF, Ho C
Specific and uniform 15N labelings along with site-directed mutagenesis of glutamine-binding protein have been utilized to obtain assignments of the His156, Trp32 and Trp220 residues. These assignments have been made not only to further study the...
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[NMR paper] Determination of membrane protein structure by rotational resonance NMR: bacteriorhod
Determination of membrane protein structure by rotational resonance NMR: bacteriorhodopsin.
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Science. 1991 Feb 15;251(4995):783-6
Authors: Creuzet F, McDermott A, Gebhard R, van der Hoef K, Spijker-Assink MB, Herzfeld J, Lugtenburg J, Levitt MH, Griffin RG
Rotationally resonant magnetization exchange, a new nuclear magnetic resonance (NMR) technique for measuring internuclear distances between like spins in solids, was used to determine...
Closed form of liganded glutamine-binding protein by rotational-echo double-resonance
Linear Mode
