Related ArticlesNMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein.
Biochemistry. 2004 Nov 30;43(47):14940-7
Authors: Biverstĺhl H, Andersson A, Gräslund A, Mäler L
The structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein (bPrPp) has been investigated by NMR spectroscopy in phospholipid membrane mimetic systems. CD spectroscopy revealed that the peptide adopts a largely alpha-helical structure in zwitterionic bicelles as well as in DHPC micelles but has a less degree of alpha-helix structure in partly charged bicelles. The solution structure of bPrPp was determined in DHPC micelles, and an alpha-helix was found between residues Ser8 and Ile21. The residues within the helical region show slow amide hydrogen exchange. Translational diffusion measurements in zwitterionic q = 0.5 bicelles show that the peptide does not induce aggregation of the bicelles. Increased quadrupolar splittings were observed in the outer part of the (2)H spectrum of DMPC in q = 3.5 bicelles, indicating that the peptide induces a certain degree of order in the bilayer. The amide hydrogen exchange and the (2)H NMR results are consistent with a slight positive hydrophobic mismatch and that bPrPp forms a stable helix that inserts in a transmembrane location in the bilayer. The structure of bPrPp and its position in the membrane may be relevant for the understanding of how the N-terminal (1-30) part of the bovine PrP functions as a cell-penetrating peptide. These findings may lead to a better understanding of how the prion protein accumulates at the membrane surface and also how the conversion into the scrapie form is carried out.
[NMR paper] NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with
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J Biol Chem. 2004 Jul 23;279(30):31455-61
Authors: Okubo S, Hara F, Tsuchida Y, Shimotakahara S, Suzuki S, Hatanaka H, Yokoyama S, Tanaka H, Yasuda H, Shindo H
A member of the PIAS (protein inhibitor of activated STAT) family of proteins, PIAS1, have been reported...
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[NMR paper] Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR stu
Solution structure of the two N-terminal RNA-binding domains of nucleolin and NMR study of the interaction with its RNA target.
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J Mol Biol. 2000 Oct 20;303(2):227-41
Authors: Allain FH, Gilbert DE, Bouvet P, Feigon J
Nucleolin is an abundant 70 kDa nucleolar protein involved in many aspects of ribosomal RNA biogenesis. The central region of nucleolin contains four tandem consensus RNA-binding domains...
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NMR solution structure of the N-terminal domain of hERG and its interaction with the
NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.
NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.
Biochem Biophys Res Commun. 2010 Nov 2;
Authors: Li Q, Gayen S, Chen AS, Huang Q, Raida M, Kang C
The human Ether-ŕ-go-go Related Gene (hERG) potassium channel mediates the rapid delayed rectifier current (IKr) in the cardiac action potential. Mutations in the 135 amino acid residue N-terminal domain (NTD) cause channel dysfunction or...
[NMR paper] Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia col
Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
Biochemistry. 1997 Mar 4;36(9):2517-30
Authors: Garrett DS, Seok YJ, Liao DI, Peterkofsky A, Gronenborn AM, Clore GM
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[NMR paper] Solution structure of the conserved segment of the Myb cognate DNA sequence by 2D NMR
Solution structure of the conserved segment of the Myb cognate DNA sequence by 2D NMR, spectral simulation, restrained energy minimization, and distance geometry calculations.
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Biochemistry. 1995 May 2;34(17):5913-22
Authors: Radha PK, Madan A, Nibedita R, Hosur RV
Solution structure of a self-complementary DNA duplex d-ACCGTTAACGGT containing the TAACGG...
[NMR paper] Sequence-specific 1H NMR assignments and secondary structure in solution of Escherich
Sequence-specific 1H NMR assignments and secondary structure in solution of Escherichia coli trp repressor.
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Biochemistry. 1990 Jul 10;29(27):6332-41
Authors: Arrowsmith CH, Pachter R, Altman RB, Iyer SB, Jardetzky O
Sequence-specific 1H NMR assignments are reported for the active L-tryptophan-bound form of Escherichia coli trp repressor. The repressor is a symmetric dimer of 107 residues per monomer; thus at 25 kDa, this...
NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of
Linear Mode
