Related ArticlesDetermination of solution conformations of PrP106-126, a neurotoxic fragment of prion protein, by 1H NMR and restrained molecular dynamics.
Eur J Biochem. 1999 Dec;266(3):1192-201
Authors: Ragg E, Tagliavini F, Malesani P, Monticelli L, Bugiani O, Forloni G, Salmona M
Experimental two-dimensional 1H NMR data have been obtained for PrP106-128 under the following solvent conditions: deionized water/2, 2,2-trifluoroethanol 50 : 50 (v/v) and dimethylsulfoxide. These data were analyzed by restrained molecular mechanics calculations to determine how changes in solvation affect the conformation of the peptide. In deionized water at pH 3.5, the peptide adopted a helical conformation in the hydrophobic region spanning residues Met112-Leu125, with the most populated helical region corresponding to the Ala115-Ala119 segment ( approximately 10%). In trifluoroethanol/H2O, the alpha-helix increased in population especially in the Gly119-Val122 tract ( approximately 25%). The conformation of this region was found to be remarkably sensitive to pH, as the Ala120-Gly124 tract shifted to an extended conformation at pH 7. In dimethylsulfoxide, the hydrophobic cluster adopted a prevalently extended conformation. For all tested solvents the region spanning residues Asn108-Met112 was present in a 'turn-like' conformation and included His111, situated just before the starting point of the alpha-helix. Rather than by conformational changes, the effect of His111 is exerted by changes in its hydrophobicity, triggering aggregation. The amphiphilic properties and the pH-dependent ionizable side-chain of His111 may thus be important for the modulation of the conformational mobility and heterogeneity of PrP106-126.
[NMR paper] NMR assignment of the Xenopus laevis prion protein fragment xlPrP (98-226).
NMR assignment of the Xenopus laevis prion protein fragment xlPrP (98-226).
Related Articles NMR assignment of the Xenopus laevis prion protein fragment xlPrP (98-226).
J Biomol NMR. 2005 Mar;31(3):260
Authors: Pérez DR, Wüthrich K
nmrlearner
Journal club
0
11-24-2010 11:14 PM
[NMR paper] NMR assignment of the turtle prion protein fragment tPrP(121-225).
NMR assignment of the turtle prion protein fragment tPrP(121-225).
Related Articles NMR assignment of the turtle prion protein fragment tPrP(121-225).
J Biomol NMR. 2004 Sep;30(1):97
Authors: Calzolai L, Lysek DA, Wüthrich K
nmrlearner
Journal club
0
11-24-2010 10:01 PM
[NMR paper] Active conformations of glycosaminoglycans. NMR determination of the conformation of
Active conformations of glycosaminoglycans. NMR determination of the conformation of heparin sequences complexed with antithrombin and fibroblast growth factors in solution.
Related Articles Active conformations of glycosaminoglycans. NMR determination of the conformation of heparin sequences complexed with antithrombin and fibroblast growth factors in solution.
Semin Thromb Hemost. 2002 Aug;28(4):325-34
Authors: Hricovíni M, Guerrini M, Bisio A, Torri G, Naggi A, Casu B
Binding to proteins usually induces perturbation of nuclear magnetic...
nmrlearner
Journal club
0
11-24-2010 08:58 PM
[NMR paper] Solid-state NMR studies of the secondary structure of a mutant prion protein fragment
Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.
Related Articles Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.
Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11686-90
Authors: Laws DD, Bitter HM, Liu K, Ball HL, Kaneko K, Wille H, Cohen FE, Prusiner SB, Pines A, Wemmer DE
The secondary structure of a 55-residue fragment of the mouse prion protein, MoPrP(89-143), was studied in...
nmrlearner
Journal club
0
11-19-2010 08:44 PM
[NMR paper] Toward direct determination of conformations of protein building units from multidime
Toward direct determination of conformations of protein building units from multidimensional NMR experiments part II: a theoretical case study of formyl-L-valine amide.
Related Articles Toward direct determination of conformations of protein building units from multidimensional NMR experiments part II: a theoretical case study of formyl-L-valine amide.
Chemistry. 2001 Mar 2;7(5):1069-83
Authors: Perczel A, Császár AG
Chemical shielding anisotropy tensors have been determined for all twenty-seven characteristic conformers of For-L-Val-NH2 using...
nmrlearner
Journal club
0
11-19-2010 08:32 PM
[NMR paper] Solid-state NMR studies of the prion protein H1 fragment.
Solid-state NMR studies of the prion protein H1 fragment.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solid-state NMR studies of the prion protein H1 fragment.
Protein Sci. 1996 Aug;5(8):1655-61
Authors: Heller J, Kolbert AC, Larsen R, Ernst M, Bekker T, Baldwin M, Prusiner SB, Pines A, Wemmer DE
Conformational...
nmrlearner
Journal club
0
08-22-2010 02:20 PM
[NMR paper] Solution conformations of proline rings in proteins studied by NMR spectroscopy.
Solution conformations of proline rings in proteins studied by NMR spectroscopy.
Related Articles Solution conformations of proline rings in proteins studied by NMR spectroscopy.
J Biomol NMR. 1995 Sep;6(2):123-8
Authors: Cai M, Huang Y, Liu J, Krishnamoorthi R
Three different conformations of proline rings in a protein in solution, Up, Down and Twist, have been distinguished, and stereospecific assignments of the pyrrolidine beta-, gamma- and delta-hydrogens have been made on the basis of 1H-1H vicinal coupling constant patterns and...
nmrlearner
Journal club
0
08-22-2010 03:50 AM
[NMR paper] NMR-derived solution conformations of a hybrid synthetic peptide containing multiple
NMR-derived solution conformations of a hybrid synthetic peptide containing multiple epitopes of envelope protein gp120 from the RF strain of human immunodeficiency virus.
Related Articles NMR-derived solution conformations of a hybrid synthetic peptide containing multiple epitopes of envelope protein gp120 from the RF strain of human immunodeficiency virus.
Biochemistry. 1994 Mar 1;33(8):2055-62
Authors: de Lorimier R, Moody MA, Haynes BF, Spicer LD
Solution conformations of a 40-residue hybrid peptide containing T-helper epitopes and B-cell...
Determination of solution conformations of PrP106-126, a neurotoxic fragment of prion
Linear Mode
