메뉴 건너뛰기




Volumn 12, Issue 3, 2003, Pages 403-411

Simultaneous assignment and structure determination of a membrane protein from NMR orientational restraints

Author keywords

Fd coat protein; Membrane protein; Pisa wheels; Protein structure determination; Solid state NMR

Indexed keywords

COAT PROTEIN; MEMBRANE PROTEIN;

EID: 0037372352     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0211503     Document Type: Article
Times cited : (168)

References (35)
  • 1
    • 0031577283 scopus 로고    scopus 로고
    • fd coat protein structure in membrane environments: Structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix
    • Almeida, F.C. and Opella, S.J. 1997. fd coat protein structure in membrane environments: Structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix. J. Mol. Biol. 270: 481-495.
    • (1997) J. Mol. Biol. , vol.270 , pp. 481-495
    • Almeida, F.C.1    Opella, S.J.2
  • 3
    • 0023755798 scopus 로고
    • Comparison of the dynamics of the membrane bound form of fd coat protein in micelles and in bilayers
    • Bogusky, M.J., Leo, G.C., and Opella, S.J. 1988. Comparison of the dynamics of the membrane bound form of fd coat protein in micelles and in bilayers. Proteins: Struct. Funct. Genetics 4: 123-130.
    • (1988) Proteins: Struct. Funct. Genetics , vol.4 , pp. 123-130
    • Bogusky, M.J.1    Leo, G.C.2    Opella, S.J.3
  • 4
    • 0019334854 scopus 로고
    • Structural properties of fd coat protein in sodium dodecyl sulfate micelles
    • Cross, T.A. and Opella. S.J. 1980. Structural properties of fd coat protein in sodium dodecyl sulfate micelles. Biochem. Biophys. Res. Commun. 92: 478-484.
    • (1980) Biochem. Biophys. Res. Commun. , vol.92 , pp. 478-484
    • Cross, T.A.1    Opella, S.J.2
  • 5
    • 0000397184 scopus 로고
    • Protein structure by solid-state NMR
    • -. 1983. Protein structure by solid-state NMR. J. Am. Chem. Soc. 105: 306-308.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 306-308
  • 6
    • 0022342799 scopus 로고
    • Protein structure by solid-state NMR: Residues 40-45 of bacteriophage fd coat protein
    • -. 1985. Protein structure by solid-state NMR: Residues 40-45 of bacteriophage fd coat protein. J. Mol. Biol. 182: 367-381.
    • (1985) J. Mol. Biol. , vol.182 , pp. 367-381
  • 7
    • 0026638315 scopus 로고
    • Three-dimensional structure of a cloning vector: X-ray diffraction studies of filamentous bacteriophage M13 at 7 Å resolution
    • Glucksman, M.J., Bhattacharjee, S., and Makowski, L. 1992. Three-dimensional structure of a cloning vector: X-ray diffraction studies of filamentous bacteriophage M13 at 7 Å resolution. J. Mol. Biol. 226: 455-470.
    • (1992) J. Mol. Biol. , vol.226 , pp. 455-470
    • Glucksman, M.J.1    Bhattacharjee, S.2    Makowski, L.3
  • 8
    • 0026610833 scopus 로고
    • 15N NMR resonances in detergent-solubilized M13 coat protein: A model for the coat protein dimer
    • 15N NMR resonances in detergent-solubilized M13 coat protein: A model for the coat protein dimer. Biochemistry 31: 5284.
    • (1992) Biochemistry , vol.31 , pp. 5284
    • Henry, G.D.1    Sykes, B.D.2
  • 9
    • 0027360175 scopus 로고
    • High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR
    • Ketchem, R.R., Hu, W., and Cross, T.A. 1993. High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR. Science 261: 1457-1460.
    • (1993) Science , vol.261 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 10
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. 1996. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graphics 14: 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 12
    • 0035142956 scopus 로고    scopus 로고
    • A simple approach to membrane protein secondary structure and topology based on NMR spectroscopy
    • Marassi, F.M. 2001. A simple approach to membrane protein secondary structure and topology based on NMR spectroscopy. Biophys. J. 80: 994-1003.
    • (2001) Biophys. J. , vol.80 , pp. 994-1003
    • Marassi, F.M.1
  • 13
    • 0034186215 scopus 로고    scopus 로고
    • A solid-state NMR index of membrane protein helical structure and topology
    • Marassi, F.M. and Opella, S.J. 2000. A solid-state NMR index of membrane protein helical structure and topology. J. Magn. Reson. 144: 150-155.
    • (2000) J. Magn. Reson. , vol.144 , pp. 150-155
    • Marassi, F.M.1    Opella, S.J.2
  • 14
    • 0036361158 scopus 로고    scopus 로고
    • Using Pisa pies to resolve ambiguities in angular constraints from PISEMA spectra of aligned proteins
    • -. 2002. Using Pisa pies to resolve ambiguities in angular constraints from PISEMA spectra of aligned proteins. J. Biomol. NMR 23: 239-242.
    • (2002) J. Biomol. NMR , vol.23 , pp. 239-242
  • 16
    • 0028058295 scopus 로고
    • Molecular models and structural comparisons of native and mutant class I filamentous bacteriophages Ff (fd, fl, M13), Ifl and Ike
    • Marvin, D.A., Hale, R.D., Nave, C., and Citterich, M.A. 1994. Molecular models and structural comparisons of native and mutant class I filamentous bacteriophages Ff (fd, fl, M13), Ifl and Ike. J. Mol. Biol. 235: 260-286.
    • (1994) J. Mol. Biol. , vol.235 , pp. 260-286
    • Marvin, D.A.1    Hale, R.D.2    Nave, C.3    Citterich, M.A.4
  • 17
    • 0027438626 scopus 로고
    • fd coat protein structure in membrane environments
    • McDonnell, P.A., Shon, K., Kim, Y., and Opella, S.J. 1993. fd coat protein structure in membrane environments. J. Mol. Biol. 233: 447-463.
    • (1993) J. Mol. Biol. , vol.233 , pp. 447-463
    • McDonnell, P.A.1    Shon, K.2    Kim, Y.3    Opella, S.J.4
  • 21
    • 0032919444 scopus 로고    scopus 로고
    • Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy
    • Opella, S.J., Marassi, F.M., Gesell, J.J., Valente, A.P., Kim, Y., Oblatt-Montal, M., and Montal, M. 1999. Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy. Nat. Struct. Biol. 6: 374-379.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 374-379
    • Opella, S.J.1    Marassi, F.M.2    Gesell, J.J.3    Valente, A.P.4    Kim, Y.5    Oblatt-Montal, M.6    Montal, M.7
  • 22
    • 0034926431 scopus 로고    scopus 로고
    • NMR of membrane associated peptides and proteins
    • Opella, S.J., Ma, C., and Marassi, F.M. 2001. NMR of membrane associated peptides and proteins. Methods Enzymol. 339: 285-313.
    • (2001) Methods Enzymol. , vol.339 , pp. 285-313
    • Opella, S.J.1    Ma, C.2    Marassi, F.M.3
  • 23
    • 0032544545 scopus 로고    scopus 로고
    • Solution structure of the M13 major coat protein in detergent micelles: A basis for a model of phage assembly involving specific residues
    • Papavoine, C.H.M., Christiaans, B.E.C., Folmer, R.H.A., Konings, R.N.H., and Hilbers. C.W. 1998. Solution structure of the M13 major coat protein in detergent micelles: A basis for a model of phage assembly involving specific residues. J. Mol. Biol. 282: 401-419.
    • (1998) J. Mol. Biol. , vol.282 , pp. 401-419
    • Papavoine, C.H.M.1    Christiaans, B.E.C.2    Folmer, R.H.A.3    Konings, R.N.H.4    Hilbers, C.W.5
  • 24
    • 0034383566 scopus 로고    scopus 로고
    • Transmembrane protein structure from NMR
    • Quine, J.R. and Cross, T.A. 2000. Transmembrane protein structure from NMR. Concepts Magn. Reson. 12: 71.
    • (2000) Concepts Magn. Reson. , vol.12 , pp. 71
    • Quine, J.R.1    Cross, T.A.2
  • 25
    • 0030698391 scopus 로고    scopus 로고
    • 15N-histidine side chains determined by three-dimensional solid-state NMR spectroscopy
    • 15N-histidine side chains determined by three-dimensional solid-state NMR spectroscopy. J. Am. Chem. Soc. 119: 10479-10486.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 10479-10486
    • Ramamoorthy, A.1    Wu, C.H.2    Opella, S.J.3
  • 26
  • 27
    • 0026557830 scopus 로고
    • The functions of tryptophan residues in membrane proteins
    • Schiffer, M., Chang, C.H., and Stevens, F.J. 1992. The functions of tryptophan residues in membrane proteins. Protein Eng. 5: 213-214.
    • (1992) Protein Eng. , vol.5 , pp. 213-214
    • Schiffer, M.1    Chang, C.H.2    Stevens, F.J.3
  • 28
    • 0000368696 scopus 로고
    • Peptide plane orientations determination by fundamental and overtone nitrogen 14 NMR
    • Tycko, R., Stewart, P.L., and Opella, S.J. 1986. Peptide plane orientations determination by fundamental and overtone nitrogen 14 NMR. J. Am. Chem. Soc. 108: 5419-5425.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 5419-5425
    • Tycko, R.1    Stewart, P.L.2    Opella, S.J.3
  • 32
    • 0016958780 scopus 로고
    • Uncoupling of local field spectra in nuclear magnetic resonance: Determination of atomic positions in solids
    • Waugh, J.S. 1976. Uncoupling of local field spectra in nuclear magnetic resonance: Determination of atomic positions in solids. Proc. Natl. Acad. Sci. 73: 1394.
    • (1976) Proc. Natl. Acad. Sci. , vol.73 , pp. 1394
    • Waugh, J.S.1
  • 33
    • 0029996040 scopus 로고    scopus 로고
    • Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by solution NMR
    • Williams, K.A., Farrow, N.A., Deber, C.M., and Kay, L.E. 1996. Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by solution NMR. Biochemistry 35: 5145-5157.
    • (1996) Biochemistry , vol.35 , pp. 5145-5157
    • Williams, K.A.1    Farrow, N.A.2    Deber, C.M.3    Kay, L.E.4
  • 34
    • 33846595904 scopus 로고
    • High-resolution heteronuclear dipolar solid-state NMR spectroscopy
    • Wu, C., Ramamoorthy, A., and Opella, S.J. 1994. High-resolution heteronuclear dipolar solid-state NMR spectroscopy. J. Magn. Reson. A 109: 270-272.
    • (1994) J. Magn. Reson. A , vol.109 , pp. 270-272
    • Wu, C.1    Ramamoorthy, A.2    Opella, S.J.3
  • 35
    • 0001125152 scopus 로고
    • 15N chemical shift interaction tensors in a peptide bond by three-dimensional solid-state NMR spectroscopy
    • 15N chemical shift interaction tensors in a peptide bond by three-dimensional solid-state NMR spectroscopy. J. Am. Chem. Soc. 117: 6148-6149.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6148-6149
    • Wu, C.1    Ramamoorthy, A.2    Gierasch, L.M.3    Opella, S.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.