Related ArticlesConformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study.
Org Biomol Chem. 2005 Feb 7;3(3):490-7
Authors: Di Natale G, Impellizzeri G, Pappalardo G
Two peptide fragments, corresponding to the amino acid residues 106-126 (PrP[Ac-106-126-NH(2)]) and 106-114 (PrP[Ac-106-114-NH(2)]) of the human prion protein have been synthesised in the acetylated and amide form at their N- and C-termini, respectively. The conformational preferences of PrP[Ac-106-126-NH(2)] and PrP[Ac-106-114-NH(2)] were investigated using CD and NMR spectroscopy. CD results showed that PrP[Ac-106-126-NH(2)] mainly adopts an alpha-helical conformation in TFE-water mixture and in SDS micelles, while a predominantly random structure is observed in aqueous solution. The shorter PrP[Ac-106-114-NH(2)] fragment showed similar propensities when investigated under the same experimental conditions as those employed for PrP[Ac-106-126-NH(2)]. From CD experiments at different SDS concentrations, an alpha-helix/beta-sheet conformational transition was only observed in the blocked PrP[Ac-106-126-NH(2)] sequence. The NMR analysis confirmed the helical nature of PrP[Ac-106-126-NH(2)] in the presence of SDS micelles. The shorter PrP[Ac-106-114-NH(2)] manifested a similar behaviour. The results as a whole suggest that both hydrophobic effects and electrostatic interactions play a significant role in the formation and stabilisation of ordered secondary structures in PrP[Ac-106-126-NH(2)].
[NMR paper] NMR dynamics-derived insights into the binding properties of a peptide interacting wi
NMR dynamics-derived insights into the binding properties of a peptide interacting with an SH2 domain.
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Biochemistry. 2005 Jan 18;44(2):694-703
Authors: Finerty PJ, Mittermaier AK, Muhandiram R, Kay LE, Forman-Kay JD
The signal transduction protein phospholipase C-gamma1 (PLC-gamma1) is activated when its C-terminal SH2 domain (PLCC) binds the phosphorylated Tyr-1021 site (pTyr-1021) in the beta-platelet-derived growth factor...
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[NMR paper] Conformational study of fragments of envelope proteins (gp120: 254-274 and gp41: 519-
Conformational study of fragments of envelope proteins (gp120: 254-274 and gp41: 519-541) of HIV-1 by NMR and MD simulations.
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J Pept Sci. 2004 Jun;10(6):363-80
Authors: Kanyalkar M, Srivastava S, Saran A, Coutinho E
The envelope proteins, gp 120 and gp41 of HIV-1, play a crucial role in receptor (CD4+ lymphocytes) binding and membrane fusion. The fragment 254-274 of gp120 is conserved in all strains of...
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[NMR paper] Reconstitution of a native-like SH2 domain from disordered peptide fragments examined
Reconstitution of a native-like SH2 domain from disordered peptide fragments examined by multidimensional heteronuclear NMR.
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Protein Sci. 2001 Nov;10(11):2162-75
Authors: Ojennus DD, Fleissner MR, Wuttke DS
The N-terminal SH2 domain from the p85alpha subunit of phosphatidylinositol 3' kinase is cleaved specifically into 9- and 5-kD fragments by limited proteolytic digestion with trypsin. The noncovalent...
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[NMR paper] Conformational preferences of a chimeric peptide HIV-1 immunogen from the C4-V3 domai
Conformational preferences of a chimeric peptide HIV-1 immunogen from the C4-V3 domains of gp120 envelope protein of HIV-1 CAN0A based on solution NMR: comparison to a related immunogenic peptide from HIV-1 RF.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Conformational preferences of a chimeric peptide HIV-1 immunogen from the C4-V3 domains of gp120 envelope protein of HIV-1 CAN0A based on solution NMR: comparison to a related immunogenic peptide from HIV-1 RF.
Biochemistry. 1996 Apr 23;35(16):5158-65
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[NMR paper] High helicity of peptide fragments corresponding to beta-strand regions of beta-lacto
High helicity of peptide fragments corresponding to beta-strand regions of beta-lactoglobulin observed by 2D-NMR spectroscopy.
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Fold Des. 1996;1(4):255-63
Authors: Kuroda Y, Hamada D, Tanaka T, Goto Y
BACKGROUND: Whereas protein fragments, when they are structured, adopt conformations similar to that found in the native state, the high helical propensity of beta-lactoglobulin, a predominantly beta-sheet...
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[NMR paper] Orientation of peptide fragments from Sos proteins bound to the N-terminal SH3 domain
Orientation of peptide fragments from Sos proteins bound to the N-terminal SH3 domain of Grb2 determined by NMR spectroscopy.
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Biochemistry. 1994 Nov 22;33(46):13531-9
Authors: Wittekind M, Mapelli C, Farmer BT, Suen KL, Goldfarb V, Tsao J, Lavoie T, Barbacid M, Meyers CA, Mueller L
NMR spectroscopy has been used to characterize the protein-protein interactions between the mouse Grb2 (mGrb2) N-terminal...
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[NMR paper] 1H NMR analysis of fibril-forming peptide fragments of transthyretin.
1H NMR analysis of fibril-forming peptide fragments of transthyretin.
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Int J Pept Protein Res. 1994 Oct;44(4):388-98
Authors: Jarvis JA, Kirkpatrick A, Craik DJ
Peptide fragments of the protein transthyretin, previously shown to form cross beta-sheet amyloid-like fibrils in vitro, were investigated using 1H 1D and 2D NMR techniques. TTR 10-20, TTR 105-115 as well as a substituted analogue, (TTR 105-115Met111) all formed amyloid-like fibrils readily in 20-30%...
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[NMR paper] Conformational studies on a peptide fragment representing the RNA-binding N-terminus
Conformational studies on a peptide fragment representing the RNA-binding N-terminus of a viral coat protein using circular dichroism and NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Conformational studies on a peptide fragment representing the RNA-binding N-terminus of a viral coat protein using circular dichroism and NMR spectroscopy.
Eur J Biochem. 1991 Oct 15;201(2):489-94
Authors: van der Graaf M, Hemminga MA
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Conformational properties of peptide fragments homologous to the 106-114 and 106-126
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