메뉴 건너뛰기




Volumn 42, Issue 51, 2003, Pages 15170-15178

Detection of α-Helical Coiled-Coil Dimer Formation by Spin-Labeled Synthetic Peptides: A Model Parallel Coiled-Coil Peptide and the Antiparallel Coiled Coil Formed by a Replica of the ProP C-Terminus

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; PARAMAGNETIC RESONANCE; PROTEINS; SPECTROSCOPIC ANALYSIS;

EID: 0348224027     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035122t     Document Type: Article
Times cited : (24)

References (26)
  • 2
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell, W. L., Cafiso, D. S., and Altenbach, C. (2000) Identifying conformational changes with site-directed spin labeling, Nat. Struct. Biol. 7. 735-739.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 3
    • 0028838458 scopus 로고
    • A peptide from the heptad repeat of human immunodeficiency virus gp41 show both membrane binding and coiled-coil formation
    • Rabenstein, M., and Shin, Y.-K. (1995) A peptide from the heptad repeat of human immunodeficiency virus gp41 show both membrane binding and coiled-coil formation, Biochemistry 34, 13390-13397.
    • (1995) Biochemistry , vol.34 , pp. 13390-13397
    • Rabenstein, M.1    Shin, Y.-K.2
  • 4
    • 0029665093 scopus 로고    scopus 로고
    • On the dynamics and conformation of the HA2 domain of the influenza virus hemagglutinin
    • Kim, C.-H., Macosko, J. C., Yu, Y. G., and Shin, Y.-K. (1996) On the dynamics and conformation of the HA2 domain of the influenza virus hemagglutinin, Biochemistry 35, 5359-5365.
    • (1996) Biochemistry , vol.35 , pp. 5359-5365
    • Kim, C.-H.1    Macosko, J.C.2    Yu, Y.G.3    Shin, Y.-K.4
  • 6
    • 0035066645 scopus 로고    scopus 로고
    • The neuronal t-snare complex is a parallel four-helix bundle
    • Xiao, W., Poirier, M. A., Bennett, M. K., and Shin, Y.-K. (2001) The neuronal t-snare complex is a parallel four-helix bundle, Nat. Struct. Biol. 8, 308-311.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 308-311
    • Xiao, W.1    Poirier, M.A.2    Bennett, M.K.3    Shin, Y.-K.4
  • 7
    • 0035918302 scopus 로고    scopus 로고
    • Homo- and heterooligomeric SNARE complexes studied by site-directed spin labeling
    • Margittai, M., Fasshauer, D., Pabst, S., Jahn, R., and Langen, R. (2001) Homo- and heterooligomeric SNARE complexes studied by site-directed spin labeling, J. Biol. Chem. 276, 13169-13177.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13169-13177
    • Margittai, M.1    Fasshauer, D.2    Pabst, S.3    Jahn, R.4    Langen, R.5
  • 8
    • 0033596861 scopus 로고    scopus 로고
    • Biochemical and biophysical characterization of the trimerization domain from the heat shock transcription factor
    • Peteranderl, R., Rabenstein, M., Shin, Y.-K., Liu, C. W., Wemmer, D. E., King, D. S., and Nelson, H. C. M. (1999) Biochemical and biophysical characterization of the trimerization domain from the heat shock transcription factor, Biochemistry 38, 3559-3569.
    • (1999) Biochemistry , vol.38 , pp. 3559-3569
    • Peteranderl, R.1    Rabenstein, M.2    Shin, Y.-K.3    Liu, C.W.4    Wemmer, D.E.5    King, D.S.6    Nelson, H.C.M.7
  • 9
    • 0032042825 scopus 로고    scopus 로고
    • An NMR investigation of the conformational effect of nitroxide spin labels on Ala-rich helical peptides
    • Bolin, K. A., Hanson, P., Wright, S. J., and Millhauser, G. L. (1998) An NMR investigation of the conformational effect of nitroxide spin labels on Ala-rich helical peptides, J. Magn. Reson. 131, 248-253.
    • (1998) J. Magn. Reson. , vol.131 , pp. 248-253
    • Bolin, K.A.1    Hanson, P.2    Wright, S.J.3    Millhauser, G.L.4
  • 10
    • 0027480940 scopus 로고
    • Disulfide bond contribution to protein stability: Positional effects of substitution in the hydrophobic core of the two-stranded α-helical coiled-coil
    • Zhou, N. E., Kay, C. M., and Hodges, R. S. (1993) Disulfide bond contribution to protein stability: Positional effects of substitution in the hydrophobic core of the two-stranded α-helical coiled-coil, Biochemistry 32, 3178-3187.
    • (1993) Biochemistry , vol.32 , pp. 3178-3187
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 11
    • 0033014719 scopus 로고    scopus 로고
    • Osmosensing by bacteria: Signals and membrane-based sensors
    • Wood, J. M. (1999) Osmosensing by bacteria: signals and membrane-based sensors, Microbiol. Mol. Biol. Rev. 63, 230-262.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 230-262
    • Wood, J.M.1
  • 12
    • 0037457916 scopus 로고    scopus 로고
    • Osmosensor ProP of Escherichia coli responds to the concentration, chemistry, and molecular size of osmolytes in the proteoliposome lumen
    • Culham, D. E., Henderson, J., Crane, R. A., and Wood, J. M. (2003) Osmosensor ProP of Escherichia coli responds to the concentration, chemistry, and molecular size of osmolytes in the proteoliposome lumen, Biochemistry 42, 410-420.
    • (2003) Biochemistry , vol.42 , pp. 410-420
    • Culham, D.E.1    Henderson, J.2    Crane, R.A.3    Wood, J.M.4
  • 13
    • 0027507351 scopus 로고
    • Isolation and sequencing of Escherichia coli gene proP reveals unusual structural features of the osmoregulatory proline/betaine transporter, ProP
    • Culham, D. E., Lasby, B., Marangoni, A. G., Milner, J. L., Steer, B. A., van Nues, R. W., and Wood, J. M. (1993) Isolation and sequencing of Escherichia coli gene proP reveals unusual structural features of the osmoregulatory proline/betaine transporter, ProP, J. Mol. Biol. 229, 268-276.
    • (1993) J. Mol. Biol. , vol.229 , pp. 268-276
    • Culham, D.E.1    Lasby, B.2    Marangoni, A.G.3    Milner, J.L.4    Steer, B.A.5    Van Nues, R.W.6    Wood, J.M.7
  • 14
    • 0033833792 scopus 로고    scopus 로고
    • The role of the carboxyl terminal α-helical coiled-coil domain in osmosensing by transporter ProP of Escherichia coli
    • Culham, D. E., Tripet, B., Racher, K. I., Voegele, R. T., Hodges, R. S., and Wood, J. M. (2000) The role of the carboxyl terminal α-helical coiled-coil domain in osmosensing by transporter ProP of Escherichia coli, J. Mol. Recognit. 13, 309-322.
    • (2000) J. Mol. Recognit. , vol.13 , pp. 309-322
    • Culham, D.E.1    Tripet, B.2    Racher, K.I.3    Voegele, R.T.4    Hodges, R.S.5    Wood, J.M.6
  • 16
    • 0017880207 scopus 로고
    • Effects of basic protein from human CNS myelin on lipid bilayer structure
    • Boggs, J. M., and Moscarello M. A. (1978) Effects of basic protein from human CNS myelin on lipid bilayer structure, J. Membr. Biol. 39, 75-96.
    • (1978) J. Membr. Biol. , vol.39 , pp. 75-96
    • Boggs, J.M.1    Moscarello, M.A.2
  • 17
    • 0030732692 scopus 로고    scopus 로고
    • Site-directed spin-labeling study of the structure and subunit interactions along a conserved sequence in the α-crystallin domain of heat-shock protein 27. Evidence of a conserved subunit interface
    • Mchaourab, H. S., Berengian, A. R., and Koteiche, H. A. (1997) Site-directed spin-labeling study of the structure and subunit interactions along a conserved sequence in the α-crystallin domain of heat-shock protein 27. Evidence of a conserved subunit interface, Biochemistry 36, 14627-14634.
    • (1997) Biochemistry , vol.36 , pp. 14627-14634
    • Mchaourab, H.S.1    Berengian, A.R.2    Koteiche, H.A.3
  • 18
    • 1842326248 scopus 로고    scopus 로고
    • Conformation of T4 lysozyme in solution. Hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling
    • McHaourab, H. S., Oh, K. J., Fang, C. J., and Hubbell, W. L. (1997) Conformation of T4 lysozyme in solution. Hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling, Biochemistry 36, 307-316.
    • (1997) Biochemistry , vol.36 , pp. 307-316
    • McHaourab, H.S.1    Oh, K.J.2    Fang, C.J.3    Hubbell, W.L.4
  • 19
    • 0035951101 scopus 로고    scopus 로고
    • Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: Experimental strategies and practical limitations
    • Altenbach, C., Oh, K.-J., Trabanino, R. J., Hideg, K., and Hubbell, W. L. (2001) Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: Experimental strategies and practical limitations, Biochemistry 40, 15471-15482.
    • (2001) Biochemistry , vol.40 , pp. 15471-15482
    • Altenbach, C.1    Oh, K.-J.2    Trabanino, R.J.3    Hideg, K.4    Hubbell, W.L.5
  • 20
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics
    • Mchaourab, H. S., Lietzow, M. A., Hideg, K., and Hubbell, W. L. (1996) Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics, Biochemistry 35, 7692-7704.
    • (1996) Biochemistry , vol.35 , pp. 7692-7704
    • Mchaourab, H.S.1    Lietzow, M.A.2    Hideg, K.3    Hubbell, W.L.4
  • 21
    • 0037634019 scopus 로고    scopus 로고
    • Unique stabilizing interactions identified in the two-stranded α-helical coiled coil: Crystal structure of a cortexillin I/GCN4 hybrid coiled-coil peptide
    • Lee, D. L., Ivaninskii, S., Burkhard, P., and Hodges, R. S. (2003) Unique stabilizing interactions identified in the two-stranded α-helical coiled coil: crystal structure of a cortexillin I/GCN4 hybrid coiled-coil peptide, Protein Sci. 12, 1395-1405.
    • (2003) Protein Sci. , vol.12 , pp. 1395-1405
    • Lee, D.L.1    Ivaninskii, S.2    Burkhard, P.3    Hodges, R.S.4
  • 23
    • 0028330850 scopus 로고
    • Electrostatic interactions control the parallel and antiparallel orientation of α-helical chains in two-stranded α-helical coiled coils
    • Monera O. D., Kay, C. M., and Hodges, R. S. (1994) Electrostatic interactions control the parallel and antiparallel orientation of α-helical chains in two-stranded α-helical coiled coils, Biochemistry 33, 3862-3871.
    • (1994) Biochemistry , vol.33 , pp. 3862-3871
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 24
    • 0029115328 scopus 로고
    • Determination of the distance between two spin labels attached to a macromolecule
    • Rabenstein, M., and Shin Y.-K. (1995) Determination of the distance between two spin labels attached to a macromolecule, Proc. Natl. Acad. Sci. U.S.A. 92, 8239-8243.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8239-8243
    • Rabenstein, M.1    Shin, Y.-K.2
  • 25
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury, P. B., Zhang, T., Kim, P. S., and Alber, T. (1993) A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants, Science 262, 1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 26
    • 0344010237 scopus 로고    scopus 로고
    • Solution structure of the cytoplasmic antiparallel coiled-coil domain from Escherichia coli osmosensor ProP
    • Zoetewey, D. L., Tripet, B. P., Kutateladze, T. G., Overduin, M. J., Wood, J. M., and Hodges, R. S. (2003) Solution structure of the cytoplasmic antiparallel coiled-coil domain from Escherichia coli osmosensor ProP, J. Mol. Biol. 334, 1063-1076.
    • (2003) J. Mol. Biol. , vol.334 , pp. 1063-1076
    • Zoetewey, D.L.1    Tripet, B.P.2    Kutateladze, T.G.3    Overduin, M.J.4    Wood, J.M.5    Hodges, R.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.