Related ArticlesCD and NMR investigations on trifluoroethanol-induced step-wise folding of helical segment from scorpion neurotoxin.
Eur J Biochem. 1999 Sep;264(2):468-78
Authors: Khandelwal P, Seth S, Hosur RV
A 14 amino acid residue peptide from the helical region of Scorpion neurotoxin has been structurally characterized using CD and NMR spectroscopy in different solvent conditions. 2,2,2-Trifluoroethanol (TFE) titration has been carried out in 11 steps from 0 to 90% TFE and the gradual stabilization of the conformation to form predominantly alpha-helix covering all of the 14 residues has been studied by 1H and 13C NMR spectroscopy. Detailed information such as coupling constants, chemical shift indices, NOESY peak intensities and amide proton temperature coefficients at each TFE concentration has been extracted and analysed to derive the step-wise preferential stabilization of the helical segments along the length of the peptide. It was found that there is a finite amount of the helical conformation in the middle residues 5-11 even at low TFE concentrations. It was also observed that > 75% TFE (v/v) is required for the propagation of the helix to the N and C termini and for correct packing of the side chains of all of the residues. These observations are significant to understanding the folding of this segment in the protein and may throw light on the inherent preferences and side chain interactions in the formation of the helix in the peptide.
[NMR900 blog] NMR investigations of metabolomics
NMR investigations of metabolomics
Special issue of Journal of Biomolecular NMR guest edited by Brian D. Sykes, volume 49, numbers 3-4, April 2011.
B.D. Sykes, Journal of Biomolecular NMR 49 (2011) 163-164. (Editorial) http://dx.doi.org/10.1007/s10858-011-9479-3https://blogger.googleusercontent.com/tracker/8663203727601106205-7533376768274982270?l=nmr900.blogspot.com
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07-04-2011 05:47 AM
[NMR paper] NMR structure of the HIV-1 regulatory protein Vpr in H2O/trifluoroethanol. Comparison
NMR structure of the HIV-1 regulatory protein Vpr in H2O/trifluoroethanol. Comparison with the Vpr N-terminal (1-51) and C-terminal (52-96) domains.
Related Articles NMR structure of the HIV-1 regulatory protein Vpr in H2O/trifluoroethanol. Comparison with the Vpr N-terminal (1-51) and C-terminal (52-96) domains.
Eur J Biochem. 2002 Aug;269(15):3779-88
Authors: Wecker K, Morellet N, Bouaziz S, Roques BP
The human immunodeficiency virus type 1, HIV-1, genome encodes a highly conserved regulatory gene product, Vpr (96 amino acids), which is...
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11-24-2010 08:58 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 Reveals Two-Step Association of Congo Red to Amyloid ? in Low-Molecular-Weight Ag
NMR Reveals Two-Step Association of Congo Red to Amyloid ? in Low-Molecular-Weight Aggregates.
Related Articles NMR Reveals Two-Step Association of Congo Red to Amyloid ? in Low-Molecular-Weight Aggregates.
J Phys Chem B. 2010 Nov 15;
Authors: Pedersen MO, Mikkelsen K, Behrens MA, Pedersen JS, Enghild JJ, Skrydstrup T, Malmendal A, Nielsen NC
Aggregation of the Amyloid ? peptide into amyloid fibrils is closely related to development of Alzheimer's disease. Many small aromatic compounds have been found to act as inhibitors of fibril formation, and...
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11-17-2010 05:49 PM
[NMR paper] Helical structure and folding of subunit c of F1F0 ATP synthase: 1H NMR resonance ass
Helical structure and folding of subunit c of F1F0 ATP synthase: 1H NMR resonance assignments and NOE analysis.
Related Articles Helical structure and folding of subunit c of F1F0 ATP synthase: 1H NMR resonance assignments and NOE analysis.
Biochemistry. 1993 Nov 16;32(45):12167-77
Authors: Girvin ME, Fillingame RH
Subunit c of the H(+)-transporting F1F0 ATP synthase (EC 3.6.1.34) is thought to fold across the membrane as a hairpin of two alpha-helices and function as a key component of the H(+)-translocase of F0. We report here the initial...
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08-22-2010 03:01 AM
[NMR paper] Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using
Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide.
Related Articles Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide.
Biochemistry. 1992 Sep 22;31(37):8790-8
Authors: Sönnichsen FD, Van Eyk JE, Hodges RS, Sykes BD
The structure of a synthetic peptide comprising the 28 amino-terminal residues of actin has been examined by 1H-NMR and CD spectroscopy. The peptide is largely unstructured and flexible in solution but becomes...
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08-21-2010 11:45 PM
[Ryan's blog] From FID to Structure in 30 Minutes? Investigating the CASE Limiting Step
Source: Ryan's blog
From FID to Structure in 30 Minutes? Investigating the CASE Limiting Step
In yesterday's post I pointed you to an article that has become the most accessed article of all time in the Journal of Cheminformatics, co-authored by representatives of ACD/Labs. This article is a very comprehensive outline of the different approaches,...
CD and NMR investigations on trifluoroethanol-induced step-wise folding of helical se
Linear Mode
