Related ArticlesSolution secondary structure of calcium-saturated troponin C monomer determined by multidimensional heteronuclear NMR spectroscopy.
Protein Sci. 1995 Jul;4(7):1279-90
Authors: Slupsky CM, Reinach FC, Smillie LB, Sykes BD
The solution secondary structure of calcium-saturated skeletal troponin C (TnC) in the presence of 15% (v/v) trifluoroethanol (TFE), which has been shown to exist predominantly as a monomer (Slupsky CM, Kay CM, Reinach FC, Smillie LB, Sykes BD, 1995, Biochemistry 34, forthcoming), has been investigated using multidimensional heteronuclear nuclear magnetic resonance spectroscopy. The 1H, 15N, and 13C NMR chemical shift values for TnC in the presence of TFE are very similar to values obtained for calcium-saturated NTnC (residues 1-90 of skeletal TnC), calmodulin, and synthetic peptide homodimers. Moreover, the secondary structure elements of TnC are virtually identical to those obtained for calcium-saturated NTnC, calmodulin, and the synthetic peptide homodimers, suggesting that 15% (v/v) TFE minimally perturbs the secondary and tertiary structure of this stably folded protein. Comparison of the solution structure of calcium-saturated TnC with the X-ray crystal structure of half-saturated TnC reveals differences in the phi/psi angles of residue Glu 41 and in the linker between the two domains. Glu 41 has irregular phi/psi angles in the crystal structure, producing a kink in the B helix, whereas in calcium-saturated TnC, Glu 41 has helical phi/psi angles, resulting in a straight B helix. The linker between the N and C domains of calcium-saturated TnC is flexible in the solution structure.
Solution NMR Studies of A? Monomer Dynamics.
Solution NMR Studies of A? Monomer Dynamics.
Solution NMR Studies of A? Monomer Dynamics.
Protein Pept Lett. 2011 Jan 11;
Authors: Wang C
A? is widely recognized as a key molecule in Alzheimer's disease, causing neurotoxicity through A? aggregates such as A? oligomers and fibrils. A?40 and A?42, composed of 40 and 42 residues, respectively, are the major A? species in human brain. A?42 aggregates much faster than A?40 but the mechanism of such difference in aggregation propensity is poorly understood. Using NMR spin relaxation, we have shown that...
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01-13-2011 12:00 PM
[NMR paper] Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as d
Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as determined by NMR.
Related Articles Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as determined by NMR.
Biochemistry. 2002 Jan 22;41(3):788-96
Authors: Rustandi RR, Baldisseri DM, Inman KG, Nizner P, Hamilton SM, Landar A, Landar A, Zimmer DB, Weber DJ
S100A1, a member of the S100 protein family, is an EF-hand containing Ca(2+)-binding protein (93 residues per subunit) with noncovalent interactions at its dimer interface. Each...
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11-24-2010 08:49 PM
[NMR paper] Secondary structure and calcium-induced folding of the Clostridium thermocellum docke
Secondary structure and calcium-induced folding of the Clostridium thermocellum dockerin domain determined by NMR spectroscopy.
Related Articles Secondary structure and calcium-induced folding of the Clostridium thermocellum dockerin domain determined by NMR spectroscopy.
Arch Biochem Biophys. 2000 Jul 15;379(2):237-44
Authors: Lytle BL, Volkman BF, Westler WM, Wu JH
Assembly of the cellulosome, a large, extracellular cellulase complex, depends upon docking of a myriad of enzymatic subunits to homologous receptors, or cohesin domains, arranged...
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11-19-2010 08:29 PM
[NMR paper] NMR solution structure of a synthetic troponin C heterodimeric domain.
NMR solution structure of a synthetic troponin C heterodimeric domain.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR solution structure of a synthetic troponin C heterodimeric domain.
Biochemistry. 1996 Jun 11;35(23):7429-38
Authors: Shaw GS, Sykes BD
The C-terminal domain from the muscle protein troponin C (TnC) comprises two helix-loop-helix calcium-binding sites (residues 90-162). The assembly of these two sites is governed by calcium binding enabling a synthetic C-terminal...
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08-22-2010 02:27 PM
[NMR paper] NMR solution structure of calcium-saturated skeletal muscle troponin C.
NMR solution structure of calcium-saturated skeletal muscle troponin C.
Related Articles NMR solution structure of calcium-saturated skeletal muscle troponin C.
Biochemistry. 1995 Dec 12;34(49):15953-64
Authors: Slupsky CM, Sykes BD
Troponin C (TnC) is an 18 kDa (162-residue) thin-filament calcium-binding protein responsible for triggering muscle contraction upon the release of calcium from the sarcoplasmic reticulum. The structure of TnC with two calcium ions bound has previously been solved by X-ray methods. Shown here is the solution...
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08-22-2010 03:50 AM
[NMR paper] NMR-derived three-dimensional solution structure of protein S complexed with calcium.
NMR-derived three-dimensional solution structure of protein S complexed with calcium.
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Structure. 1994 Feb 15;2(2):107-22
Authors: Bagby S, Harvey TS, Eagle SG, Inouye S, Ikura M
BACKGROUND: Protein S is a developmentally-regulated Ca(2+)-binding protein of the soil bacterium Myxococcus xanthus. It functions by forming protective, multilayer spore surface assemblies which may additionally act as a cell-cell adhesive. Protein S is...
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[NMR paper] Secondary structure of myristoylated recoverin determined by three-dimensional hetero
Secondary structure of myristoylated recoverin determined by three-dimensional heteronuclear NMR: implications for the calcium-myristoyl switch.
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Biochemistry. 1994 Sep 6;33(35):10743-53
Authors: Ames JB, Tanaka T, Stryer L, Ikura M
Recoverin, a new member of the EF-hand superfamily, serves as a Ca2+ sensor in vision. A myristoyl or related N-acyl group is covalently attached at its...
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[NMR paper] Secondary structure of the homeo domain of yeast alpha 2 repressor determined by NMR
Secondary structure of the homeo domain of yeast alpha 2 repressor determined by NMR spectroscopy.
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Genes Dev. 1991 May;5(5):764-72
Authors: Phillips CL, Vershon AK, Johnson AD, Dahlquist FW
The yeast alpha 2 protein is a regulator of cell type in Saccharomyces cerevisiae. It represses transcription of a set of target genes by binding to an operator located upstream of each of these genes. The alpha 2 protein shares weak sequence...
Solution secondary structure of calcium-saturated troponin C monomer determined by mu
Linear Mode
