메뉴 건너뛰기




Volumn 117, Issue 22, 2013, Pages 6693-6700

2D 1H/1H RFDR and NOESY NMR experiments on a membrane-bound antimicrobial peptide under magic angle spinning

Author keywords

[No Author keywords available]

Indexed keywords

AMIDES; COUPLINGS; ISOTOPES; LIGHT POLARIZATION; MICELLES; MICROORGANISMS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES;

EID: 84879175399     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp4034003     Document Type: Article
Times cited : (44)

References (50)
  • 4
    • 4344648452 scopus 로고    scopus 로고
    • Residual dipolar couplings in structure determination of biomolecules
    • Prestegard, J. H.; Bougault, C. M.; Kishore, A. I. Residual dipolar couplings in structure determination of biomolecules Chem. Rev. 2004, 104, 3519
    • (2004) Chem. Rev. , vol.104 , pp. 3519
    • Prestegard, J.H.1    Bougault, C.M.2    Kishore, A.I.3
  • 5
    • 78049396749 scopus 로고    scopus 로고
    • Supramolecular Interactions Probed by 13C-13C Solid-State NMR Spectroscopy
    • Loquet, A.; Giller, K.; Becker, S.; Lange, A. Supramolecular Interactions Probed by 13C-13C Solid-State NMR Spectroscopy J. Am. Chem. Soc. 2010, 132, 15164
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 15164
    • Loquet, A.1    Giller, K.2    Becker, S.3    Lange, A.4
  • 6
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • Tjandra, N.; Bax, A. Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium Science 1997, 278, 1111
    • (1997) Science , vol.278 , pp. 1111
    • Tjandra, N.1    Bax, A.2
  • 7
    • 84869166856 scopus 로고    scopus 로고
    • The magic of bicelles lights up membrane protein structure
    • Dürr, U. H. N.; Gildenberg, M.; Ramamoorthy, A. The magic of bicelles lights up membrane protein structure Chem. Rev. 2012, 112, 6054-6074
    • (2012) Chem. Rev. , vol.112 , pp. 6054-6074
    • Dürr, U.H.N.1    Gildenberg, M.2    Ramamoorthy, A.3
  • 8
    • 12644267957 scopus 로고
    • Build-up Rates of the Nuclear Overhauser Effects Measured by Two-Dimensional Proton Magnetic Resonance Spectroscopy: Implications for Studies of Protein Conformation
    • Kumar, A.; Wagner, G.; Ernst, R. R.; Wüthrich, K. Build-up Rates of the Nuclear Overhauser Effects Measured by Two-Dimensional Proton Magnetic Resonance Spectroscopy: Implications for Studies of Protein Conformation J. Am. Chem. Soc. 1981, 103, 3654
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 3654
    • Kumar, A.1    Wagner, G.2    Ernst, R.R.3    Wüthrich, K.4
  • 9
    • 0347753822 scopus 로고    scopus 로고
    • NMR spectroscopic determination of the solution structure of a branched nucleic acid from residual dipolar couplings by using isotopically labeled nucleotides
    • van Buuren, B. N.; Schleucher, J.; Wittmann, V.; Griesinger, C.; Schwalbe, H.; Wijmenga, S. S. NMR spectroscopic determination of the solution structure of a branched nucleic acid from residual dipolar couplings by using isotopically labeled nucleotides Angew. Chem., Int. Ed. 2004, 43, 187
    • (2004) Angew. Chem., Int. Ed. , vol.43 , pp. 187
    • Van Buuren, B.N.1    Schleucher, J.2    Wittmann, V.3    Griesinger, C.4    Schwalbe, H.5    Wijmenga, S.S.6
  • 13
    • 78049278005 scopus 로고    scopus 로고
    • Protein-ice interaction of an antifreeze protein observed with solid-state NMR
    • Siemer, A. B.; Huang, K. Y.; McDermott, A. E. Protein-ice interaction of an antifreeze protein observed with solid-state NMR Proc. Natl. Acad. Sci. U.S.A. 2010, 107, 17580
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 17580
    • Siemer, A.B.1    Huang, K.Y.2    McDermott, A.E.3
  • 16
    • 67349241519 scopus 로고    scopus 로고
    • Beyond NMR spectra of antimicrobial peptides: Dynamical images at atomic resolution and functional insights
    • Ramamoorthy, A. Beyond NMR spectra of antimicrobial peptides: Dynamical images at atomic resolution and functional insights Solid State Nucl. Magn. Reson. 2009, 35, 201-207
    • (2009) Solid State Nucl. Magn. Reson. , vol.35 , pp. 201-207
    • Ramamoorthy, A.1
  • 17
    • 84879175106 scopus 로고    scopus 로고
    • Membrane-Disruption and Early Events in the Aggregation of the Diabetes Related Peptide IAPP from a Molecular Perspective
    • Brender, J.; Salamekh, S.; Ramamoorthy, A. Membrane-Disruption and Early Events in the Aggregation of the Diabetes Related Peptide IAPP from a Molecular Perspective Acc. Chem. Res. 2012, 116, 3650-3658
    • (2012) Acc. Chem. Res. , vol.116 , pp. 3650-3658
    • Brender, J.1    Salamekh, S.2    Ramamoorthy, A.3
  • 18
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Braunschweiler, L.; Ernst, R. R. Coherence transfer by isotropic mixing: application to proton correlation spectroscopy J. Magn. Reson. 1983, 53, 521
    • (1983) J. Magn. Reson. , vol.53 , pp. 521
    • Braunschweiler, L.1    Ernst, R.R.2
  • 19
    • 56749150574 scopus 로고    scopus 로고
    • Opical versus systemic antimicrobial therapy for treating mildly infected diabetic foot ulcers: Arandomized, controlled, double-blinded, multicenter trial of pexiganan cream
    • Lipsky, B. A.; Holroyd, K. J.; Zasloff, M. opical versus systemic antimicrobial therapy for treating mildly infected diabetic foot ulcers: arandomized, controlled, double-blinded, multicenter trial of pexiganan cream Clin. Infect. Dis. 2008, 47, 1537-45
    • (2008) Clin. Infect. Dis. , vol.47 , pp. 1537-1545
    • Lipsky, B.A.1    Holroyd, K.J.2    Zasloff, M.3
  • 20
    • 0028920870 scopus 로고
    • Structure-activity studies on magainins and other host defense peptides
    • Maloy, W. L.; Kari, U. P. Structure-activity studies on magainins and other host defense peptides Biopolymers 1995, 37, 105-22
    • (1995) Biopolymers , vol.37 , pp. 105-122
    • Maloy, W.L.1    Kari, U.P.2
  • 21
    • 67649262183 scopus 로고    scopus 로고
    • Membrane Orientation, Mechanism, and Function of Pexiganan - A Highly Potent Antimicrobial Peptide Designed from Magainin
    • Gottler, L. M.; Ramamoorthy, A. Membrane Orientation, Mechanism, and Function of Pexiganan-A Highly Potent Antimicrobial Peptide Designed From Magainin Biochim. Biophys. Acta, Biomembr. 2009, 1788, 1680-6
    • (2009) Biochim. Biophys. Acta, Biomembr. , vol.1788 , pp. 1680-1686
    • Gottler, L.M.1    Ramamoorthy, A.2
  • 22
    • 0000321871 scopus 로고
    • Chemical shift correlation spectroscopy in rotating solids: Radio frequency-driven dipolar recoupling and longitudinal exchange
    • Bennett, A. E.; Griffin, R. G.; Ok, J. H.; Vega, S. Chemical shift correlation spectroscopy in rotating solids: Radio frequency-driven dipolar recoupling and longitudinal exchange J. Chem. Phys. 1992, 96, 8624
    • (1992) J. Chem. Phys. , vol.96 , pp. 8624
    • Bennett, A.E.1    Griffin, R.G.2    Ok, J.H.3    Vega, S.4
  • 28
    • 0010957050 scopus 로고
    • Reaction Rates by Nuclear Magnetic Resonance
    • McConnell, H. M. Reaction Rates by Nuclear Magnetic Resonance J. Chem. Phys. 1965, 28, 430
    • (1965) J. Chem. Phys. , vol.28 , pp. 430
    • McConnell, H.M.1
  • 33
    • 0037961563 scopus 로고    scopus 로고
    • MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain
    • Hallock, K. J.; Lee, D. K.; Ramamoorthy, A. MSI-78, an analogue of the magainin antimicrobial peptides, disrupts lipid bilayer structure via positive curvature strain Biophys. J. 2003, 84, 3052
    • (2003) Biophys. J. , vol.84 , pp. 3052
    • Hallock, K.J.1    Lee, D.K.2    Ramamoorthy, A.3
  • 34
    • 33646474970 scopus 로고    scopus 로고
    • Structures of the Dimeric and Monomeric Variants of Magainin Antimicrobial Peptides (MSI-78 and MSI-594) in Micelles and Bilayers by NMR Spectroscopy
    • Porcelli, F.; Buck-Koehntop, B. A.; Thennarasu, S.; Ramamoorthy, A.; Veglia, G. Structures of the Dimeric and Monomeric Variants of Magainin Antimicrobial Peptides (MSI-78 and MSI-594) in Micelles and Bilayers by NMR Spectroscopy Biochemistry 2006, 45, 5793
    • (2006) Biochemistry , vol.45 , pp. 5793
    • Porcelli, F.1    Buck-Koehntop, B.A.2    Thennarasu, S.3    Ramamoorthy, A.4    Veglia, G.5
  • 35
    • 84874643050 scopus 로고    scopus 로고
    • When the detergent meets bilayer: Birth and coming of age of lipid bicelles
    • Dürr, U. H. N.; Soong, R.; Ramamoorthy, A. When the detergent meets bilayer: Birth and coming of age of lipid bicelles Prog. NMR Spectrosc. 2013, 69, 1-22
    • (2013) Prog. NMR Spectrosc. , vol.69 , pp. 1-22
    • Dürr, U.H.N.1    Soong, R.2    Ramamoorthy, A.3
  • 36
    • 78049311379 scopus 로고    scopus 로고
    • Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers Determined by Solid-State Nuclear Magnetic Resonance
    • Kijac, A.; Shih, A. Y.; Nieuwkoop, A. J.; Schulten, K.; Sligar, S. G.; Rienstra, C. M. Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers Determined by Solid-State Nuclear Magnetic Resonance Biochemistry 2010, 49, 9190-8
    • (2010) Biochemistry , vol.49 , pp. 9190-9198
    • Kijac, A.1    Shih, A.Y.2    Nieuwkoop, A.J.3    Schulten, K.4    Sligar, S.G.5    Rienstra, C.M.6
  • 37
    • 84873400562 scopus 로고    scopus 로고
    • Optimized Phospholipid Bilayer Nanodiscs Facilitate High-Resolution Structure Determination of Membrane Proteins
    • Hyberts, S. G.; Etzkorn, M.; Raschle, T.; Wagner, G. Optimized Phospholipid Bilayer Nanodiscs Facilitate High-Resolution Structure Determination of Membrane Proteins J. Am. Chem. Soc. 2013, 135, 1919-25
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 1919-1925
    • Hyberts, S.G.1    Etzkorn, M.2    Raschle, T.3    Wagner, G.4
  • 39
    • 36849051197 scopus 로고    scopus 로고
    • The cytochromes P450 and b5 and their reductases - Promising targets for structural studies by advanced solid-state NMR spectroscopy
    • Dürr, U. H. N.; Waskell, L.; Ramamoorthy, A. The cytochromes P450 and b5 and their reductases-Promising targets for structural studies by advanced solid-state NMR spectroscopy Biochim. Biophys. Acta, Biomembr. 2007, 3235-3259
    • (2007) Biochim. Biophys. Acta, Biomembr. , pp. 3235-3259
    • Dürr, U.H.N.1    Waskell, L.2    Ramamoorthy, A.3
  • 40
    • 67349241519 scopus 로고    scopus 로고
    • Beyond NMR spectra of antimicrobial peptides: Dynamical images at atomic resolution and functional insights
    • Ramamoorthy, A. Beyond NMR spectra of antimicrobial peptides: Dynamical images at atomic resolution and functional insights Solid State Nucl. Magn. Reson. 2009, 35, 201-207
    • (2009) Solid State Nucl. Magn. Reson. , vol.35 , pp. 201-207
    • Ramamoorthy, A.1
  • 42
    • 0000941297 scopus 로고
    • Paramagnetic Doping As an Aid in Obtaining High-Resolution Carbon-13 NMR Spectra of Biomolecules in the Solid State
    • Ganapathy, S.; Naito, A.; McDowell, C. A. Paramagnetic Doping As an Aid in Obtaining High-Resolution Carbon-13 NMR Spectra of Biomolecules in the Solid State J. Am. Chem. Soc. 1981, 103, 6011-6015
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 6011-6015
    • Ganapathy, S.1    Naito, A.2    McDowell, C.A.3
  • 43
    • 33846636757 scopus 로고    scopus 로고
    • Sensitivity enhancement in 13C solid-state NMR of protein microcrystals by use of paramagnetic metal ions for optimizing 1H T1 relaxation
    • Wickramasinghe, N. P.; Kotecha, M.; Samoson, A.; Past, J.; Ishii, Y. Sensitivity enhancement in 13C solid-state NMR of protein microcrystals by use of paramagnetic metal ions for optimizing 1H T1 relaxation J. Magn. Reson. 2007, 184, 350-356
    • (2007) J. Magn. Reson. , vol.184 , pp. 350-356
    • Wickramasinghe, N.P.1    Kotecha, M.2    Samoson, A.3    Past, J.4    Ishii, Y.5
  • 44
    • 77952566893 scopus 로고    scopus 로고
    • Use of a Copper-Chelated-Lipid Speeds Up NMR Measurements from Membrane Proteins, A
    • Yamamoto, K.; Xu, J.; Kawulka, K. E.; Vederas, J. C.; Ramamoorthy, A. Use of a Copper-Chelated-Lipid Speeds Up NMR Measurements From Membrane Proteins, A J. Am. Chem. Soc. 2010, 132, 6929-31
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6929-6931
    • Yamamoto, K.1    Xu, J.2    Kawulka, K.E.3    Vederas, J.C.4    Ramamoorthy, A.5
  • 45
    • 80054974914 scopus 로고    scopus 로고
    • Fast NMR Data Acquisition from Bicelles Containing a Membrane-Associated Peptide at Natural-Abundance
    • Yamamoto, K.; Vivekanandan, S.; Ramamoorthy, A. Fast NMR Data Acquisition from Bicelles Containing a Membrane-Associated Peptide at Natural-Abundance J. Phys. Chem. B 2011, 115, 12448-55
    • (2011) J. Phys. Chem. B , vol.115 , pp. 12448-12455
    • Yamamoto, K.1    Vivekanandan, S.2    Ramamoorthy, A.3
  • 46
    • 77954639411 scopus 로고    scopus 로고
    • Rapid Acquisition of Multidimensional Solid-State NMR Spectra of Proteins Facilitated by Covalently Bound Paramagnetic Tags
    • Nadaud, P. S.; Helmus, J. J.; Sengupta, I.; Jaroniec, C. P. Rapid Acquisition of Multidimensional Solid-State NMR Spectra of Proteins Facilitated by Covalently Bound Paramagnetic Tags J. Am. Chem. Soc. 2010, 132, 9561-9563
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 9561-9563
    • Nadaud, P.S.1    Helmus, J.J.2    Sengupta, I.3    Jaroniec, C.P.4
  • 47
    • 79960710930 scopus 로고    scopus 로고
    • Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement
    • Tang, M.; Berthold, D. A.; Rienstra, C. M. Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement J. Phys. Chem. Lett. 2011, 2, 1836-1841
    • (2011) J. Phys. Chem. Lett. , vol.2 , pp. 1836-1841
    • Tang, M.1    Berthold, D.A.2    Rienstra, C.M.3
  • 48
    • 84877989130 scopus 로고    scopus 로고
    • Orphan spin operators enable the acquisition of multiple 2D and 3D magic angle spinning solid-state NMR spectra
    • Gopinath, T.; Veglia, G. Orphan spin operators enable the acquisition of multiple 2D and 3D magic angle spinning solid-state NMR spectra J. Chem. Phys. 2013, 138, 184201
    • (2013) J. Chem. Phys. , vol.138 , pp. 184201
    • Gopinath, T.1    Veglia, G.2
  • 49
    • 84863312621 scopus 로고    scopus 로고
    • 3D DUMAS: Simultaneous Acquisition of Three Dimensional Magic Angle Spinning Solid State NMR Experiments of Proteins
    • Gopinath, T.; Veglia, G. 3D DUMAS: Simultaneous Acquisition of Three Dimensional Magic Angle Spinning Solid State NMR Experiments of Proteins J. Magn. Reson. 2012, 220, 79-84
    • (2012) J. Magn. Reson. , vol.220 , pp. 79-84
    • Gopinath, T.1    Veglia, G.2
  • 50
    • 84858058799 scopus 로고    scopus 로고
    • Dual Acquistion Magic-Angle Spinning Solid State NMR-Spectroscopy: Simultaneous Acquisition of Multidimensional Spectra of Biomolecules
    • Gopinath, T.; Veglia, G. Dual Acquistion Magic-Angle Spinning Solid State NMR-Spectroscopy: Simultaneous Acquisition of Multidimensional Spectra of Biomolecules Angew. Chem., Int. Ed. 2012, 51, 2731-2735
    • (2012) Angew. Chem., Int. Ed. , vol.51 , pp. 2731-2735
    • Gopinath, T.1    Veglia, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.