메뉴 건너뛰기




Volumn 143, Issue 2, 2000, Pages 411-416

Sample Optimization and Identification of Signal Patterns of Amino Acid Side Chains in 2D RFDR Spectra of the α-Spectrin SH3 Domain

Author keywords

13 C linewidth; High magnetic fields; Protein structure determination; Resolution; RFDR spectroscopy; Solid state NMR spectroscopy

Indexed keywords

ALANINE; AMINO ACID; CARBON; ISOLEUCINE; NITROGEN; PROLINE; SERINE; SPECTRIN; THREONINE; VALINE;

EID: 0034167578     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmre.2000.2029     Document Type: Editorial
Times cited : (147)

References (28)
  • 1
    • 0030272669 scopus 로고    scopus 로고
    • High-resolution NMR of biological solids
    • L. M. McDowell and J. Schaefer, High-resolution NMR of biological solids, Curr. Opin. Struct. Biol. 6(5), 624-629 (1996).
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , Issue.5 , pp. 624-629
    • McDowell, L.M.1    Schaefer, J.2
  • 2
    • 0031853671 scopus 로고    scopus 로고
    • Dipolar recoupling in MAS spectra of biological solids
    • R. G. Griffin, Dipolar recoupling in MAS spectra of biological solids, Nat. Struct. Biol. NMR Suppl. 7, 508-512 (1998).
    • (1998) Nat. Struct. Biol. NMR Suppl. , vol.7 , pp. 508-512
    • Griffin, R.G.1
  • 3
    • 0029398795 scopus 로고
    • Three-dimensional solid-state NMR spectroscopy of a peptide oriented in membrane bilayers
    • A. Ramamoorthy, F. M. Marassi, M. Zasloff, and S. J. Opella, Three-dimensional solid-state NMR spectroscopy of a peptide oriented in membrane bilayers, J. Biomol. NMR 6, 329-334 (1995).
    • (1995) J. Biomol. NMR , vol.6 , pp. 329-334
    • Ramamoorthy, A.1    Marassi, F.M.2    Zasloff, M.3    Opella, S.J.4
  • 6
    • 0033144286 scopus 로고    scopus 로고
    • 15 N shift solid-state NMR correlation spectroscopy
    • 15 N shift solid-state NMR correlation spectroscopy, J. Magn. Reson. 138, 193-198 (1999).
    • (1999) J. Magn. Reson. , vol.138 , pp. 193-198
    • Gu, Z.1    Opella, S.J.2
  • 7
    • 0029332135 scopus 로고
    • Membrane protein structure: The contribution and potential of novel solid state NMR approaches
    • A. Watts, A. S. Ulrich, and D. A. Middleton, Membrane protein structure: The contribution and potential of novel solid state NMR approaches, Mol. Membr. Biol. 12, 233-246 (1995).
    • (1995) Mol. Membr. Biol. , vol.12 , pp. 233-246
    • Watts, A.1    Ulrich, A.S.2    Middleton, D.A.3
  • 8
    • 33846595904 scopus 로고
    • High resolution heteronuclear dipolar solid-state NMR spectroscopy
    • C. H. Wu, A. Ramamoorthy, and S. J. Opella, High resolution heteronuclear dipolar solid-state NMR spectroscopy, J. Magn. Reson. A 109, 270-272 (1994).
    • (1994) J. Magn. Reson. A , vol.109 , pp. 270-272
    • Wu, C.H.1    Ramamoorthy, A.2    Opella, S.J.3
  • 9
    • 0346168028 scopus 로고
    • Orientation of tensorial interactions determined from two-dimensional NMR powder spec-tra
    • M. Lindner, A. Höhener, and R. R. Ernst, Orientation of tensorial interactions determined from two-dimensional NMR powder spec-tra, J. Chem. Phys. 73, 4949-4970 (1980).
    • (1980) J. Chem. Phys. , vol.73 , pp. 4949-4970
    • Lindner, M.1    Höhener, A.2    Ernst, R.R.3
  • 10
    • 0031189051 scopus 로고    scopus 로고
    • Site-resolved determination of peptide torsion angle phi from the relative orientations of backbone N-H and C-H bonds by solid-state NMR
    • M. Hong, J. D. Gross, and R. G. Griffin, Site-resolved determination of peptide torsion angle phi from the relative orientations of backbone N-H and C-H bonds by solid-state NMR, J. Phys. Chem. B 101, 5869-5874 (1997).
    • (1997) J. Phys. Chem. B , vol.101 , pp. 5869-5874
    • Hong, M.1    Gross, J.D.2    Griffin, R.G.3
  • 11
    • 0029766182 scopus 로고    scopus 로고
    • 13 C-labeled amino acids and peptides by separated-local-field double-quantum NMR
    • 13 C-labeled amino acids and peptides by separated-local-field double-quantum NMR, J. Am. Chem. Soc. 118, 7601-7603 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7601-7603
    • Schmidt-Rohr, K.1
  • 13
    • 0001121265 scopus 로고
    • Flat-coil probe for NMR spectroscopy of oriented membrane samples
    • B. Bechinger and S. J. Opella, Flat-coil probe for NMR spectroscopy of oriented membrane samples, J. Magn. Reson. 95, 585-588 (1991).
    • (1991) J. Magn. Reson. , vol.95 , pp. 585-588
    • Bechinger, B.1    Opella, S.J.2
  • 14
    • 0031993272 scopus 로고    scopus 로고
    • Magic angle-oriented sample spinning (MAOSS): A new approach toward biomembrane studies
    • C. Glaubitz and A. Watts, Magic angle-oriented sample spinning (MAOSS): A new approach toward biomembrane studies, J. Magn. Reson. 130, 305-316 (1998).
    • (1998) J. Magn. Reson. , vol.130 , pp. 305-316
    • Glaubitz, C.1    Watts, A.2
  • 16
    • 0028972073 scopus 로고
    • 13 C-enriched chlorosomes and isolated bacteriochlorophyll c aggregates of chlorobium tedium: The self-organization of pigments is the main structural feature of chlorosomes
    • 13 C-enriched chlorosomes and isolated bacteriochlorophyll c aggregates of chlorobium tedium: The self-organization of pigments is the main structural feature of chlorosomes, Biochemistry 34, 15259-15266 (1995).
    • (1995) Biochemistry , vol.34 , pp. 15259-15266
    • Balaban, T.S.1    Holzwarth, A.R.2    Schaffner, K.3    Boender, G.J.4    De Groot, H.J.M.5
  • 19
    • 0030014748 scopus 로고    scopus 로고
    • Long-range distance measurements of protein binding sites by rotational-echo double-resonance NMR
    • D. R. Studelska, C. A. Klug, D. D. Beusen, L. M. McDowell, and J. Schaefer, Long-range distance measurements of protein binding sites by rotational-echo double-resonance NMR, J. Am. Chem. Soc. 118, 5476-5477 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 5476-5477
    • Studelska, D.R.1    Klug, C.A.2    Beusen, D.D.3    McDowell, L.M.4    Schaefer, J.5
  • 20
    • 0032175923 scopus 로고    scopus 로고
    • Effects of sample preparation conditions on biomolecular solid-state NMR lineshapes
    • D. L. Jakeman, D. J. Mitchell, W. A. Shuttleworth, and J. N. S. Evans, Effects of sample preparation conditions on biomolecular solid-state NMR lineshapes, J. Biomol. NMR 12, 417-421 (1998).
    • (1998) J. Biomol. NMR , vol.12 , pp. 417-421
    • Jakeman, D.L.1    Mitchell, D.J.2    Shuttleworth, W.A.3    Evans, J.N.S.4
  • 21
    • 0001666654 scopus 로고    scopus 로고
    • Side-chain conformation and dynamics in a solid peptide
    • S. K. Straus, T. Bremi, and R. R. Ernst, Side-chain conformation and dynamics in a solid peptide, J. Biomol. NMR 10, 119-128 (1997).
    • (1997) J. Biomol. NMR , vol.10 , pp. 119-128
    • Straus, S.K.1    Bremi, T.2    Ernst, R.R.3
  • 23
    • 0031160370 scopus 로고    scopus 로고
    • 15 N NMR assignment and solution structure of the SH3 domain of spectrin: Comparison of unrefined and refined structure sets with the crystal structure
    • 15 N NMR assignment and solution structure of the SH3 domain of spectrin: Comparison of unrefined and refined structure sets with the crystal structure, J. Biomol. NMR 9, 347-357 (1997).
    • (1997) J. Biomol. NMR , vol.9 , pp. 347-357
    • Blanco, F.J.1    Ortiz, A.R.2    Serrano, L.3
  • 24
    • 43949161069 scopus 로고
    • Ramped-amplitude cross polarization in magic-angle-spinning NMR
    • G. Metz, X. Wu, and S. O. Smith, Ramped-amplitude cross polarization in magic-angle-spinning NMR, J. Magn. Reson. A 110, 219-227 (1994).
    • (1994) J. Magn. Reson. A , vol.110 , pp. 219-227
    • Metz, G.1    Wu, X.2    Smith, S.O.3
  • 25
    • 0000321871 scopus 로고
    • Chemical shift correlation spectroscopy in rotating solids: Radio frequency-driven dipolar recoupling and longitudinal exchange
    • A. E. Bennett, J. H. Ok, R. G. Griffin, and S. Vega, Chemical shift correlation spectroscopy in rotating solids: Radio frequency-driven dipolar recoupling and longitudinal exchange, J. Chem. Phys. 96, 8624-8627 (1992).
    • (1992) J. Chem. Phys. , vol.96 , pp. 8624-8627
    • Bennett, A.E.1    Ok, J.H.2    Griffin, R.G.3    Vega, S.4
  • 28
    • 85031556819 scopus 로고    scopus 로고
    • personal communication
    • B. Simon, personal communication.
    • Simon, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.