[NMR paper] Insight into the modulation of Shaw2 Kv channels by general anesthetics: structural and functional studies of S4-S5 linker and S6 C-terminal peptides in micelles by NMR.
Insight into the modulation of Shaw2 Kv channels by general anesthetics: structural and functional studies of S4-S5 linker and S6 C-terminal peptides in micelles by NMR.
Related ArticlesInsight into the modulation of Shaw2 Kv channels by general anesthetics: structural and functional studies of S4-S5 linker and S6 C-terminal peptides in micelles by NMR.
Biochim Biophys Acta. 2013 Feb;1828(2):595-601
Authors: Zhang J, Qu X, Covarrubias M, Germann MW
Abstract
The modulation of the Drosophila Shaw2 Kv channel by 1-alkanols and inhaled anesthetics is correlated with the involvement of the S4-S5 linker and C-terminus of S6, and consistent with stabilization of the channel's closed state. Structural analysis of peptides from S4-S5 (L45) and S6 (S6c), by nuclear magnetic resonance and circular dichroism spectroscopy supports that an ?-helical conformation was adopted by L45, while S6c was only in an unstable/dynamic partially folded ?-helix in dodecylphosphocholine micelles. Solvent accessibility and paramagnetic probing of L45 revealed that L45 lies parallel to the surface of micelles with charged and polar residues pointing towards the solution while hydrophobic residues are buried inside the micelles. Chemical shift perturbation introduced by 1-butanol on residues Gln320, Thr321, Phe322 and Arg323 of L45, as well as Thr423 and Gln424 of S6c indicates possible anesthetic binding sites on these two important components in the channel activation apparatus. Diffusion measurements confirmed the association of L45, S6c and 1-butanol with micelles which suggests the capability of 1-butanol to influence a possible interaction of L45 and S6c in the micelle environment.
[NMR paper] Structural and Functional Insight into ADF/Cofilin from Trypanosoma brucei.
Structural and Functional Insight into ADF/Cofilin from Trypanosoma brucei.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Structural and Functional Insight into ADF/Cofilin from Trypanosoma brucei.
PLoS One. 2013;8(1):e53639
Authors: Dai K, Liao S, Zhang J, Zhang X, Tu X
Abstract
The ADF/cofilin family has been characterized as a group of actin-binding...
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02-03-2013 10:19 AM
Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II.
Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II.
Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II.
Biophys J. 2011 Sep 7;101(5):1193-201
Authors: Park TJ, Kim JS, Ahn HC, Kim Y
Abstract
Lactophoricin (LPcin-I) is an antimicrobial, amphiphatic, cationic peptide with 23-amino acid residues isolated from bovine milk. Its analogous peptide, LPcin-II, lacks six N-terminal amino acids compared to LPcin-I. Interestingly, LPcin-II does not display any...
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09-06-2011 06:02 PM
Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
Long-Term-Stable Ether-Lipid vs Conventional Ester-Lipid Bicelles in Oriented Solid-State NMR: Altered Structural Information in Studies of Antimicrobial Peptides.
J Phys Chem B. 2011 Feb 10;
Authors: Bertelsen K, Vad B, Nielsen EH, Hansen SK, Skrydstrup T, Otzen DE, Vosegaard T, Nielsen NC
Recently, ether lipids have been introduced as long-term stable alternatives to the more natural,...
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02-12-2011 05:26 PM
Design and NMR Studies of Cyclic Peptides Targeting the N-Terminal Domain of the Protein Tyrosine Phosphatase YopH.
Design and NMR Studies of Cyclic Peptides Targeting the N-Terminal Domain of the Protein Tyrosine Phosphatase YopH.
Design and NMR Studies of Cyclic Peptides Targeting the N-Terminal Domain of the Protein Tyrosine Phosphatase YopH.
Chem Biol Drug Des. 2010 Nov 30;
Authors: Leone M, Barile E, Dahl R, Pellecchia M
We report on the design and evaluation of novel cyclic peptides targeting the N-terminal domain of the protein tyrosine phosphatase YopH from Yersinia. Cyclic peptides have been designed based on a short sequence from the protein SKAP-HOM...
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12-02-2010 02:54 PM
[NMR paper] Structural insight into human Zn(2+)-bound S100A2 from NMR and homology modeling.
Structural insight into human Zn(2+)-bound S100A2 from NMR and homology modeling.
Related Articles Structural insight into human Zn(2+)-bound S100A2 from NMR and homology modeling.
Biochem Biophys Res Commun. 2001 Oct 26;288(2):462-7
Authors: Randazzo A, Acklin C, Schäfer BW, Heizmann CW, Chazin WJ
The S100 subfamily of EF-hand proteins is distinguished by the binding of Zn(2+) in addition to Ca(2+). In an effort to understand the role of Zn(2+) in modulating the activity of S100 proteins, we have carried out heteronuclear NMR studies of...
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11-19-2010 08:44 PM
[NMR paper] NMR studies of the anti-apoptotic protein Bcl-xL in micelles.
NMR studies of the anti-apoptotic protein Bcl-xL in micelles.
Related Articles NMR studies of the anti-apoptotic protein Bcl-xL in micelles.
Biochemistry. 2000 Sep 12;39(36):11024-33
Authors: Losonczi JA, Olejniczak ET, Betz SF, Harlan JE, Mack J, Fesik SW
The Bcl-2 family of proteins play a pivotal role in the regulation of programmed cell death. One of the postulated mechanisms for the function of these proteins involves the formation of ion channels in membranes. As a first step to structurally characterize these proteins in a membrane...
[NMR paper] 1H NMR evidence that Glu-38 interacts with the N-terminal functional domain in interl
1H NMR evidence that Glu-38 interacts with the N-terminal functional domain in interleukin-8.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 1H NMR evidence that Glu-38 interacts with the N-terminal functional domain in interleukin-8.
FEBS Lett. 1996 Dec 9;399(1-2):43-6
Authors: Rajarathnam K, Clark-Lewis I, Dewald B, Baggiolini M, Sykes BD
In order to assess the importance of the buried Glu-38 observed in the structure of interleukin-8, an analog in which Glu-38 was...
Insight into the modulation of Shaw2 Kv channels by general anesthetics: structural and functional studies of S4-S5 linker and S6 C-terminal peptides in micelles by NMR.
Linear Mode
