Related ArticlesConformational preferences of synthetic peptides derived from the immunodominant site of the circumsporozoite protein of Plasmodium falciparum by 1H NMR.
Biochemistry. 1990 Aug 28;29(34):7828-37
Authors: Dyson HJ, Satterthwait AC, Lerner RA, Wright PE
Proton nuclear magnetic resonance and ultraviolet circular dichroism spectroscopy have been used to probe the conformational ensemble of the tandemly repeating tetrapeptide unit of the circumsporozoite coat protein of the malaria parasite Plasmodium falciparum. Peptides based on the Asn-Ala-Asn-Pro and Asn-Pro-Asn-Ala cadences and composed of one to three tetrapeptide units were synthesized and examined using one- and two-dimensional NMR spectroscopy. The chemical shift of the amide protons, the temperature dependence of the amide proton chemical shift, and the patterns of NOE connectivities in the various peptides give evidence for the presence of a substantial population of folded conformers in several of the peptides in water solution at pH 5.0. Correlations between the behavior of the tandemly repeated units in different peptides have been used to infer the structure(s) of the folded conformers. The data are consistent with the presence of turnlike structures stabilized by hydrogen bonding of the backbone amide protons of the alanines and the asparagine residues preceding them. Specific differences in the strengths of NOEs between peptides of different lengths indicate that the folded structure is considerably stabilized by the presence of the asparagine residue following the alanine. Differences between peptides with different cadences of the tandemly repeating unit indicate that a repeating structural motif is formed by the Asn-Pro-Asn-Ala-(Asn) cadence.
[NMR paper] Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor prote
Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1.
Related Articles Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1.
Peptides. 2002 Dec;23(12):2127-41
Authors: de Chiara C, Nicastro G, Spisni A, Zanotti F, Cocco T, Papa S
The protein IF(1) is a natural inhibitor of the mitochondrial F(o)F(1)-ATPase. Many investigators have been prompted to identify the shortest segment of IF(1), retaining its native activity, for use in biomedical applications. Here, the...
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[NMR paper] Delineation of conformational preferences in human salivary statherin by 1H, 31P NMR
Delineation of conformational preferences in human salivary statherin by 1H, 31P NMR and CD studies: sequential assignment and structure-function correlations.
Related Articles Delineation of conformational preferences in human salivary statherin by 1H, 31P NMR and CD studies: sequential assignment and structure-function correlations.
J Biomol Struct Dyn. 1998 Aug;16(1):91-107
Authors: Naganagowda GA, Gururaja TL, Levine MJ
Membrane-induced solution structure of human salivary statherin, a 43 amino acid residue acidic phosphoprotein, has been...
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[NMR paper] NMR analysis of main-chain conformational preferences in an unfolded fibronectin-bind
NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein.
J Mol Biol. 1997 Nov 28;274(2):152-9
Authors: Penkett CJ, Redfield C, Dodd I, Hubbard J, McBay DL, Mossakowska DE, Smith RA, Dobson CM, Smith LJ
A 130-residue fragment of the Staphylococcus aureus fibronectin-binding protein has...
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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] Characterization of conformational preferences in a partly folded protein by heteronu
Characterization of conformational preferences in a partly folded protein by heteronuclear NMR spectroscopy: assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol.
Related Articles Characterization of conformational preferences in a partly folded protein by heteronuclear NMR spectroscopy: assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol.
Biochemistry. 1995 Oct 10;34(40):13219-32
Authors: Buck M, Schwalbe H, Dobson CM
2D and 3D heteronuclear NMR methods have been used...
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[NMR paper] NMR and circular dichroism studies of synthetic peptides derived from the third intra
NMR and circular dichroism studies of synthetic peptides derived from the third intracellular loop of the beta-adrenoceptor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR and circular dichroism studies of synthetic peptides derived from the third intracellular loop of the beta-adrenoceptor.
FEBS Lett. 1995 Jan 23;358(2):133-6
Authors: Jung H, Windhaber R, Palm D, Schnackerz KD
The C-terminal part of the third intracellular loop of the beta-adrenoceptor is capable...
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[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...
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[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...
Conformational preferences of synthetic peptides derived from the immunodominant site
Linear Mode
