Related ArticlesA proton-NMR study of a site-directed mutation (His388----Glu) in the interdomain region of yeast phosphoglycerate kinase. Implications for domain movement.
Eur J Biochem. 1991 Mar 14;196(2):261-9
Authors: Graham HC, Williams RJ, Littlechild JA, Watson HC
Proton NMR has been used to study a site-directed mutant of yeast phosphoglycerate kinase in which the interdomain residue His388 has been replaced by a glutamine residue. Using 1H-NMR spectroscopy, it was found that 3-phosphoglycerate binding to the mutant protein induces different conformational effects to those observed for the wild-type enzyme. These differences are not only located at the 3-phosphoglycerate binding site but are also seen as long-range effects at the surface of the protein. Measurements of the Kd for 3-phosphoglycerate from the NMR experiments show that the mutant enzyme has a 30-times reduced affinity for this substrate as compared with the wild-type enzyme. These data are consistent with the suggestion that an aromatic residue at position 388 plays an important role in the proposed hinge-bending mechanism.
[NMR paper] Kinetic, Raman, NMR, and site-directed mutagenesis studies of the Pseudomonas sp. str
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Biochemistry. 2002 Sep 17;41(37):11152-60
Authors: Zhuang Z, Song F, Zhang W, Taylor K, Archambault A, Dunaway-Mariano D, Dong J, Carey PR
4-Hydroxybenzoyl-coenzyme A (4-HBA-CoA) thioesterase catalyzes the hydrolysis of 4-HBA-CoA to 4-hydroxybenzoate...
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[NMR paper] Structural consequences of site-directed mutagenesis in flexible protein domains: NMR
Structural consequences of site-directed mutagenesis in flexible protein domains: NMR characterization of the L(55,56)S mutant of RhoGDI.
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Eur J Biochem. 2001 Apr;268(8):2253-60
Authors: Golovanov AP, Hawkins D, Barsukov I, Badii R, Bokoch GM, Lian LY, Roberts GC
The guanine dissociation inhibitor RhoGDI consists of a folded C-terminal domain and a highly flexible N-terminal region, both of...
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[NMR paper] Molecular analysis of sialoside binding to sialoadhesin by NMR and site-directed muta
Molecular analysis of sialoside binding to sialoadhesin by NMR and site-directed mutagenesis.
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Biochem J. 1999 Jul 15;341 ( Pt 2):355-61
Authors: Crocker PR, Vinson M, Kelm S, Drickamer K
The molecular interactions between sialoadhesin and sialylated ligands have been investigated by using proton NMR. Addition of ligands to the 12 kDa N-terminal immunoglobulin-like domain of sialoadhesin result in resonance shifts in the protein...
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[NMR paper] The single mutation Trp35-->Ala in the 35-40 redox site of Chlamydomonas reinhardtii
The single mutation Trp35-->Ala in the 35-40 redox site of Chlamydomonas reinhardtii thioredoxin h affects its biochemical activity and the pH dependence of C36-C39 1H-13C NMR.
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Eur J Biochem. 1998 Jul 1;255(1):185-95
Authors: Krimm I, Lemaire S, Ruelland E, Miginiac-Maslow M, Jaquot JP, Hirasawa M, Knaff DB, Lancelin JM
The role of the invariant Trp...
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[NMR paper] Heparin binding to platelet factor-4. An NMR and site-directed mutagenesis study: arg
Heparin binding to platelet factor-4. An NMR and site-directed mutagenesis study: arginine residues are crucial for binding.
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Biochem J. 1995 Dec 1;312 ( Pt 2):357-65
Authors: Mayo KH, Ilyina E, Roongta V, Dundas M, Joseph J, Lai CK, Maione T, Daly TJ
Native platelet factor-4 (PF4) is an...
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[NMR paper] Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvi
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Biochemistry. 1994 Jan 11;33(1):65-73
Authors: Yamasaki K, Shirouzu M, Muto Y, Fujita-Yoshigaki J, Koide H, Ito Y, Kawai G, Hattori S, Yokoyama S, Nishimura S
The Tyr residues in positions 32 and 40 of human c-Ha-Ras...
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[NMR paper] Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvi
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Biochemistry. 1994 Jan 11;33(1):65-73
Authors: Yamasaki K, Shirouzu M, Muto Y, Fujita-Yoshigaki J, Koide H, Ito Y, Kawai G, Hattori S, Yokoyama S, Nishimura S
The Tyr residues in positions 32 and 40 of human c-Ha-Ras...
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[NMR paper] Structural changes caused by site-directed mutagenesis of tyrosine-98 in Desulfovibri
Structural changes caused by site-directed mutagenesis of tyrosine-98 in Desulfovibrio vulgaris flavodoxin delineated by 1H and 15N NMR spectroscopy: implications for redox potential modulation.
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Biochemistry. 1994 Dec 27;33(51):15298-308
Authors: Stockman BJ, Richardson TE, Swenson RP
Flavodoxins mediate electron transfer at low redox...
A proton-NMR study of a site-directed mutation (His388----Glu) in the interdomain reg
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