메뉴 건너뛰기




Volumn 5, Issue 10, 2012, Pages 1774-1786

Pressure Dependence of 15N Chemical Shifts in Model Peptides Ac-Gly-Gly-X-Ala-NH2

Author keywords

Amide group; Backbone; Chemical shift; High pressure; J coupling; Nitrogen; NMR spectroscopy; Random coil; Tetrapeptide

Indexed keywords

AMIDES; NITROGEN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES;

EID: 84870042822     PISSN: None     EISSN: 19961944     Source Type: Journal    
DOI: 10.3390/ma5101774     Document Type: Article
Times cited : (26)

References (23)
  • 1
    • 33646900712 scopus 로고    scopus 로고
    • Probing conformational fluctuations by pressure perturbations
    • Akasaka, K. Probing conformational fluctuations by pressure perturbations. Chem. Rev. 2006, 106, 1814-1835.
    • (2006) Chem. Rev. , vol.106 , pp. 1814-1835
    • Akasaka, K.1
  • 2
    • 0032477750 scopus 로고    scopus 로고
    • Effect of pressure on individual hydrogen bonds in proteins Basic pancreatic trypsin inhibitor
    • Li, H.; Yamada, H.; Akasaka, K. Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor. Biochemistry 1998, 37, 1167-1173.
    • (1998) Biochemistry , vol.37 , pp. 1167-1173
    • Li, H.1    Yamada, H.2    Akasaka, K.3
  • 3
    • 0033624703 scopus 로고    scopus 로고
    • 15N and 1H NMR study of Histidine containing protein (HPr) from Staphylococcus carnosus at high-pressure
    • Kalbitzer, H.R.; Görler, A.; Li, H. 15N and 1H NMR study of Histidine containing protein (HPr) from Staphylococcus carnosus at high-pressure. Protein Sci. 2000, 9, 693-703.
    • (2000) Protein Sci , vol.9 , pp. 693-703
    • Kalbitzer, H.R.1    Görler, A.2    Li, H.3
  • 4
    • 70350348011 scopus 로고    scopus 로고
    • NMR spectroscopy brings invisible protein states into focus
    • Baldwin, A.J.; Kay, L.E. NMR spectroscopy brings invisible protein states into focus. Nat. Chem. Biol. 2009, 11, 808-814.
    • (2009) Nat. Chem. Biol. , vol.11 , pp. 808-814
    • Baldwin, A.J.1    Kay, L.E.2
  • 5
    • 0037007467 scopus 로고    scopus 로고
    • 1H-NMR parameters of common amino acid residues measured in aqueous solutions of the linear tetrapeptides Gly-Gly-X-Ala at pressures between 0 1 and 200 MPa
    • Arnold, M.A.; Kremer, W.; Luedemann, H.D.; Kalbitzer, H.R. 1H-NMR parameters of common amino acid residues measured in aqueous solutions of the linear tetrapeptides Gly-Gly-X-Ala at pressures between 0.1 and 200 MPa. Biophys. Chem. 2002, 96, 129-140.
    • (2002) Biophys. Chem. , vol.96 , pp. 129-140
    • Arnold, M.A.1    Kremer, W.2    Luedemann, H.D.3    Kalbitzer, H.R.4
  • 6
    • 34547947101 scopus 로고    scopus 로고
    • Species specific differences in the intermediate states of human and Syrian hamster prion protein detected by high pressure NMR spectroscopy
    • Kremer, W.; Kachel, N.; Kuwata, K.; Akasaka, K.; Kalbitzer, H.R. Species specific differences in the intermediate states of human and Syrian hamster prion protein detected by high pressure NMR spectroscopy. J. Biol. Chem. 2007, 282, 22689-22698.
    • (2007) J. Biol. Chem. , vol.282 , pp. 22689-22698
    • Kremer, W.1    Kachel, N.2    Kuwata, K.3    Akasaka, K.4    Kalbitzer, H.R.5
  • 7
    • 84985733652 scopus 로고
    • 1H-NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH
    • Bundi, A.; Wuethrich, K. 1H-NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH. Biopolymers 1979, 18, 285-297.
    • (1979) Biopolymers , vol.18 , pp. 285-297
    • Bundi, A.1    Wuethrich, K.2
  • 9
    • 79954427635 scopus 로고    scopus 로고
    • Random coil chemical shift for intrinsically disordered proteins: Effects of temperature and pH
    • Kjaergaard, M.; Brander, S.; Poulsen, F.M. Random coil chemical shift for intrinsically disordered proteins: Effects of temperature and pH. J. Biomol. NMR 2011, 49, 139-149.
    • (2011) J. Biomol. NMR , vol.49 , pp. 139-149
    • Kjaergaard, M.1    Brander, S.2    Poulsen, F.M.3
  • 10
    • 33645943697 scopus 로고    scopus 로고
    • High-pressure NMR studies in proteins
    • Kremer, W. High-pressure NMR studies in proteins. Ann. Reports NMR Spectr. 2006, 57, 177-203.
    • (2006) Ann. Reports NMR Spectr. , vol.57 , pp. 177-203
    • Kremer, W.1
  • 11
    • 84985653913 scopus 로고
    • Use of amide 1H-NMR titration shifts for studies of polypeptide conformation
    • Bundi, A.; Wuethrich, K. Use of amide 1H-NMR titration shifts for studies of polypeptide conformation. Biopolymers 1979, 18, 299-311.
    • (1979) Biopolymers , vol.18 , pp. 299-311
    • Bundi, A.1    Wuethrich, K.2
  • 12
    • 18144366989 scopus 로고    scopus 로고
    • Baroresistant buffer mixtures for biochemical analyses
    • Quinlan, R.J.; Reinhart, G.D. Baroresistant buffer mixtures for biochemical analyses. Anal. Biochem. 2005, 341, 69-76.
    • (2005) Anal. Biochem. , vol.341 , pp. 69-76
    • Quinlan, R.J.1    Reinhart, G.D.2
  • 13
    • 85172064119 scopus 로고    scopus 로고
    • Diploma thesis in Physics, University of Regensburg July 2011
    • Huberth, A. Hochdruck-NMR am Ras-Protein. Diploma thesis in Physics, University of Regensburg, July 2011.
    • Hochdruck-NMR am Ras-Protein
    • Huberth, A.1
  • 14
    • 25844460047 scopus 로고    scopus 로고
    • Self-contained high-pressure cell, apparatus, and procedure for the preparation of encapsulated proteins dissolved in low viscosity fluids for nuclear magnetic resonance spectroscopy
    • 76 094101 1-094101:7
    • Peterson, R.W.; Wand, A.J. Self-contained high-pressure cell, apparatus, and procedure for the preparation of encapsulated proteins dissolved in low viscosity fluids for nuclear magnetic resonance spectroscopy. Rev. Sci. Instrum. 2005, 76, 094101:1-094101:7.
    • (2005) Rev. Sci. Instrum.
    • Peterson, R.W.1    Wand, A.J.2
  • 16
    • 0016056448 scopus 로고
    • Pressure-resisting glass cell for high pressure, high resolution NMR measurement
    • Yamada, H. Pressure-resisting glass cell for high pressure, high resolution NMR measurement. Rev. Sci. Instrum. 1974, 45, 640-642
    • (1974) Rev. Sci. Instrum. , vol.45 , pp. 640-642
    • Yamada, H.1
  • 17
    • 33845561778 scopus 로고
    • Calibration of methanol and ethylene glycol nuclear magnetic resonance thermometers
    • Raiford, D.S.; Fisk, C.L.; Becker, E.D. Calibration of methanol and ethylene glycol nuclear magnetic resonance thermometers. Anal. Chem. 1979, 51, 2050-2051.
    • (1979) Anal. Chem. , vol.51 , pp. 2050-2051
    • Raiford, D.S.1    Fisk, C.L.2    Becker, E.D.3
  • 18
    • 44049118259 scopus 로고
    • Experiments for recording pure-absorption heteronuclear correlation spectra using pulsed field gradients
    • Davis, A.L.; Keeler, J.; Laue, E.D.; Moskau, D. Experiments for recording pure-absorption heteronuclear correlation spectra using pulsed field gradients. J. Magn. Reson. 1992, 98, 207-216.
    • (1992) J. Magn. Reson. , vol.98 , pp. 207-216
    • Davis, A.L.1    Keeler, J.2    Laue, E.D.3    Moskau, D.4
  • 19
    • 0034004318 scopus 로고    scopus 로고
    • Sequential assignment of proline-rich regions in proteins: Application to modular binding domain complexes
    • Kanelisa, V.; Donaldson, L.; Muhandiram, D.R.; Rotin, D.; Forman-Kay, J.D.; Kay, L.E. Sequential assignment of proline-rich regions in proteins: Application to modular binding domain complexes. J. Biomol. NMR 2000, 16, 253-259.
    • (2000) J. Biomol. NMR , vol.16 , pp. 253-259
    • Kanelisa, V.1    Donaldson, L.2    Muhandiram, D.R.3    Rotin, D.4    Forman-Kay, J.D.5    Kay, L.E.6
  • 20
    • 0029317175 scopus 로고
    • Sequential backbone assignment of isotopically enriched proteins in D2O by deuterium-decoupled HA(CA)N and HA(CACO)N
    • Wang, A.C.; Grzesiek, S.; Tschudin, R.; Lodi, P.J.; Bax, A. Sequential backbone assignment of isotopically enriched proteins in D2O by deuterium-decoupled HA(CA)N and HA(CACO)N. J. Biomol. NMR 1995, 5, 376-382.
    • (1995) J. Biomol. NMR , vol.5 , pp. 376-382
    • Wang, A.C.1    Grzesiek, S.2    Tschudin, R.3    Lodi, P.J.4    Bax, A.5
  • 21
    • 21244439545 scopus 로고    scopus 로고
    • Purge NMR: Effective and easy solvent suppression
    • Simpson, A.J.; Brown, S.A. Purge NMR: Effective and easy solvent suppression. J. Magn. Reson. 2005, 175, 340-346.
    • (2005) J. Magn. Reson. , vol.175 , pp. 340-346
    • Simpson, A.J.1    Brown, S.A.2
  • 23
    • 33748176879 scopus 로고    scopus 로고
    • Observation of intermediate states of the human prion protein by high pressure NMR spectroscopy
    • Kachel, N.; Kremer, W.; Zahn, R.; Kalbitzer, H.R. Observation of intermediate states of the human prion protein by high pressure NMR spectroscopy. BMC Struct. Biol. 2006, 6, 16:1-16:18.
    • (2006) BMC Struct. Biol , vol.6 , pp. 161-216
    • Kachel, N.1    Kremer, W.2    Zahn, R.3    Kalbitzer, H.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.