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Volumn 44, Issue 23, 2005, Pages 8230-8243

Secondary structure formation of a transmembrane segment in Kv channels

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRIC POTENTIAL; MEMBRANES; POLYPEPTIDES;

EID: 20444430500     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050372q     Document Type: Article
Times cited : (87)

References (56)
  • 7
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban, N., Nissen, P., Hansen, J., Moore, P. B., and Steitz, T. A. (2000) The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution, Science 289, 905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 8
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • Nissen, P., Hansen, J., Ban, N., Moore, P. B., and Steitz, T. A. (2000) The structural basis of ribosome activity in peptide bond synthesis, Science 289, 920-930.
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 10
    • 0035798359 scopus 로고    scopus 로고
    • Architecture of the protein-conducting channel associated with the translating 80S ribosome
    • Beckmann, R., Spahn, C. M., Eswar, N., Helmers, J., Penczek, P. A., Sali, A., Frank, J., and Blobel, G. (2001) Architecture of the protein-conducting channel associated with the translating 80S ribosome, Cell 107, 361-372.
    • (2001) Cell , vol.107 , pp. 361-372
    • Beckmann, R.1    Spahn, C.M.2    Eswar, N.3    Helmers, J.4    Penczek, P.A.5    Sali, A.6    Frank, J.7    Blobel, G.8
  • 11
    • 0003932766 scopus 로고
    • W. H. Freeman and Company, New York
    • Creighton, T. E. (1993) in Proteins, pp 171-199, W. H. Freeman and Company, New York.
    • (1993) Proteins , pp. 171-199
    • Creighton, T.E.1
  • 13
    • 0031939208 scopus 로고    scopus 로고
    • Protein folding and assembly in a cell-free expression system
    • Fedorov, A. N., and Baldwin, T. O. (1998) Protein folding and assembly in a cell-free expression system, Methods Enzymol. 290, 1-17.
    • (1998) Methods Enzymol. , vol.290 , pp. 1-17
    • Fedorov, A.N.1    Baldwin, T.O.2
  • 14
    • 0012249596 scopus 로고    scopus 로고
    • Different conformations of nascent polypeptides during translocation across the ER membrane
    • Mingarro, I., Nilsson, I., Whitley, P., and von Heijne, G. (2000) Different conformations of nascent polypeptides during translocation across the ER membrane, BMC Cell Biol. 1, 3.
    • (2000) BMC Cell Biol. , vol.1 , pp. 3
    • Mingarro, I.1    Nilsson, I.2    Whitley, P.3    Von Heijne, G.4
  • 15
    • 1542358892 scopus 로고    scopus 로고
    • Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins
    • Woolhead, C. A., McCormick, P. J., and Johnson, A. E. (2004) Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins, Cell 116, 725-736.
    • (2004) Cell , vol.116 , pp. 725-736
    • Woolhead, C.A.1    McCormick, P.J.2    Johnson, A.E.3
  • 16
    • 0036810271 scopus 로고    scopus 로고
    • Protein folding during cotranslational translocation in the endoplasmic reticulum
    • Kowarik, M., Kung, S., Martoglio, B., and Helenius, A. (2002) Protein folding during cotranslational translocation in the endoplasmic reticulum, Mol. Cell 10, 769-778.
    • (2002) Mol. Cell , vol.10 , pp. 769-778
    • Kowarik, M.1    Kung, S.2    Martoglio, B.3    Helenius, A.4
  • 17
    • 5144234840 scopus 로고    scopus 로고
    • Structure acquisition of the T1 domain of Kv1.3 during biogenesis
    • Kosolapov, A., Tu, L., Wang, J., and Deutsch, C. (2004) Structure Acquisition of the T1 Domain of Kv1.3 During Biogenesis, Neuron 44, 295-307.
    • (2004) Neuron , vol.44 , pp. 295-307
    • Kosolapov, A.1    Tu, L.2    Wang, J.3    Deutsch, C.4
  • 19
    • 0028955427 scopus 로고
    • The 70 carboxyl-terminal amino acids of nascent secretory proteins are protected from proteolysis by the ribosome and the protein translocation apparatus of the endoplasmic reticulum membrane
    • Matlack, K. E., and Walter, P. (1995) The 70 carboxyl-terminal amino acids of nascent secretory proteins are protected from proteolysis by the ribosome and the protein translocation apparatus of the endoplasmic reticulum membrane, J. Biol. Chem. 270, 6170-6180.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6170-6180
    • Matlack, K.E.1    Walter, P.2
  • 20
    • 0031471055 scopus 로고    scopus 로고
    • Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration
    • Liao, S., Lin, J., Do, H., and Johnson, A. E. (1997) Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration, Cell 90, 31-41.
    • (1997) Cell , vol.90 , pp. 31-41
    • Liao, S.1    Lin, J.2    Do, H.3    Johnson, A.E.4
  • 21
    • 0031043161 scopus 로고    scopus 로고
    • Nucleation mechanisms in protein folding
    • Fersht, A. R. (1997) Nucleation mechanisms in protein folding, Curr. Opin. Struct. Biol. 7, 3-9.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 3-9
    • Fersht, A.R.1
  • 22
    • 0031059496 scopus 로고    scopus 로고
    • Theoretical studies of protein-folding thermodynamics and kinetics
    • Shakhnovich, E. I. (1997) Theoretical studies of protein-folding thermodynamics and kinetics, Curr. Opin. Struct. Biol. 7, 29-40.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 29-40
    • Shakhnovich, E.I.1
  • 23
    • 0028889120 scopus 로고
    • Contribution of cotranslational folding to the rate of formation of native protein structure
    • Fedorov, A. N., and Baldwin, T. O. (1995) Contribution of cotranslational folding to the rate of formation of native protein structure, Proc. Natl. Acad. Sci. U.S.A. 92, 1227-1231.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 1227-1231
    • Fedorov, A.N.1    Baldwin, T.O.2
  • 25
    • 0031468437 scopus 로고    scopus 로고
    • Cotranslational protein folding
    • Fedorov, A. N., and Baldwin, T. O. (1997) Cotranslational protein folding, J. Biol. Chem. 272, 32715-32718.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32715-32718
    • Fedorov, A.N.1    Baldwin, T.O.2
  • 26
    • 0035909067 scopus 로고    scopus 로고
    • T1-T1 interactions occur in ER membranes while nascent Kv peptides are still attached to ribosomes
    • Lu, J., Robinson, J. M., Edwards, D., and Deutsch, C. (2001) T1-T1 interactions occur in ER membranes while nascent Kv peptides are still attached to ribosomes, Biochemistry 40, 10934-10946.
    • (2001) Biochemistry , vol.40 , pp. 10934-10946
    • Lu, J.1    Robinson, J.M.2    Edwards, D.3    Deutsch, C.4
  • 27
    • 0035818431 scopus 로고    scopus 로고
    • Pegylation: A method for assessing topological accessibilities in Kv1.3
    • Lu, J., and Deutsch, C. (2001) Pegylation: A method for assessing topological accessibilities in Kv1.3, Biochemistry 40, 13288-13301.
    • (2001) Biochemistry , vol.40 , pp. 13288-13301
    • Lu, J.1    Deutsch, C.2
  • 28
    • 0032321487 scopus 로고    scopus 로고
    • Substituted-cysteine accessibility method
    • Karlin, A., and Akabas, M. H. (1998) Substituted-cysteine accessibility method, Methods Enzymol. 293, 123-145.
    • (1998) Methods Enzymol. , vol.293 , pp. 123-145
    • Karlin, A.1    Akabas, M.H.2
  • 29
    • 0037026489 scopus 로고    scopus 로고
    • The voltage-gated potassium channels and their relatives
    • Yellen, G. (2002) The voltage-gated potassium channels and their relatives, Nature 419, 35-42.
    • (2002) Nature , vol.419 , pp. 35-42
    • Yellen, G.1
  • 31
    • 0032580205 scopus 로고    scopus 로고
    • Crystal structure of the tetramerization domain of the Shaker potassium channel
    • Kreusch, A., Pfaffinger, P. J., Stevens, C. F., and Choe, S. (1998) Crystal structure of the tetramerization domain of the Shaker potassium channel, Nature 392, 945-948.
    • (1998) Nature , vol.392 , pp. 945-948
    • Kreusch, A.1    Pfaffinger, P.J.2    Stevens, C.F.3    Choe, S.4
  • 32
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the AGADIR model of α-helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms
    • Munoz, V., and Serrano, L. (1997) Development of the multiple sequence approximation within the AGADIR model of α-helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms, Biopolymers 41, 495-509.
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Munoz, V.1    Serrano, L.2
  • 33
    • 0026591728 scopus 로고
    • Fluorescence characterization of the environment encountered by nascent polyalanine and polyserine as they exit Escherichia coli ribosomes during translation
    • Picking, W. D., Picking, W. L., Odom, O. W., and Hardesty, B. (1992) Fluorescence characterization of the environment encountered by nascent polyalanine and polyserine as they exit Escherichia coli ribosomes during translation, Biochemistry 31, 2368-2375.
    • (1992) Biochemistry , vol.31 , pp. 2368-2375
    • Picking, W.D.1    Picking, W.L.2    Odom, O.W.3    Hardesty, B.4
  • 34
    • 0020134907 scopus 로고
    • Nascent polypeptide chains emerge from the exit domain of the large ribosomal subunit: Immune mapping of the nascent chain
    • Bernabeu, C., and Lake, J. A. (1982) Nascent polypeptide chains emerge from the exit domain of the large ribosomal subunit: Immune mapping of the nascent chain, Proc. Natl. Acad. Sci. U.S.A. 79, 3111-3115.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 3111-3115
    • Bernabeu, C.1    Lake, J.A.2
  • 35
    • 0141884309 scopus 로고    scopus 로고
    • The birth of a channel
    • Deutsch, C. (2003) The birth of a channel, Neuron 40, 265-276.
    • (2003) Neuron , vol.40 , pp. 265-276
    • Deutsch, C.1
  • 36
    • 0036193888 scopus 로고    scopus 로고
    • Potassium channel ontogeny
    • Deutsch, C. (2002) Potassium channel ontogeny, Annu. Rev. Physiol. 64, 19-46.
    • (2002) Annu. Rev. Physiol. , vol.64 , pp. 19-46
    • Deutsch, C.1
  • 37
    • 0030611388 scopus 로고    scopus 로고
    • The aqueous pore through the translocon has a diameter of 40-60 Å during cotranslational protein translocation at the ER membrane
    • Hamman, B. D., Chen, J. C., Johnson, E. E., and Johnson, A. E. (1997) The aqueous pore through the translocon has a diameter of 40-60 Å during cotranslational protein translocation at the ER membrane, Cell 89, 535-544.
    • (1997) Cell , vol.89 , pp. 535-544
    • Hamman, B.D.1    Chen, J.C.2    Johnson, E.E.3    Johnson, A.E.4
  • 38
    • 0014202553 scopus 로고
    • Partial resistance of nascent polypeptide chains to proteolytic digestion due to ribosomal shielding
    • Malkin, L. I., and Rich, A. (1967) Partial resistance of nascent polypeptide chains to proteolytic digestion due to ribosomal shielding, J. Mol. Biol. 26, 329-346.
    • (1967) J. Mol. Biol. , vol.26 , pp. 329-346
    • Malkin, L.I.1    Rich, A.2
  • 39
    • 0014770988 scopus 로고
    • Controlled proteolysis of nascent polypeptides in rat liver cell fractions. I. Location of the polypeptides within ribosomes
    • Blobel, G., and Sabatini, D. D. (1970) Controlled proteolysis of nascent polypeptides in rat liver cell fractions. I. Location of the polypeptides within ribosomes, J. Cell Biol. 45, 130-145.
    • (1970) J. Cell Biol. , vol.45 , pp. 130-145
    • Blobel, G.1    Sabatini, D.D.2
  • 40
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil, K. T., and DeGrado, W. F. (1990) A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids, Science 250, 646-651.
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 44
    • 0037059044 scopus 로고    scopus 로고
    • Relation between peptide backbone solvation and the energetics of peptide hydrogen bonds
    • Baldwin, R. L. (2002) Relation between peptide backbone solvation and the energetics of peptide hydrogen bonds, Biophys. Chem. 101-102, 203-210.
    • (2002) Biophys. Chem. , vol.101-102 , pp. 203-210
    • Baldwin, R.L.1
  • 45
    • 0000562064 scopus 로고
    • Induction of peptide conformation at apolar/water interfaces. 1. A study with model peptides of defined hydrophobic periodicity
    • DeGrado, W. F., and Lear, J. D. (1985) Induction of Peptide Conformation at Apolar/Water Interfaces. 1. A study with model peptides of defined hydrophobic periodicity, J. Am. Chem. Soc. 107, 7684-7689.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 7684-7689
    • DeGrado, W.F.1    Lear, J.D.2
  • 46
    • 0002617993 scopus 로고    scopus 로고
    • A simple model of chaperonin-mediated protein folding
    • Chan, H. S., and Dill, K. A. (1996) A simple model of chaperonin-mediated protein folding, Proteins 24, 345-351.
    • (1996) Proteins , vol.24 , pp. 345-351
    • Chan, H.S.1    Dill, K.A.2
  • 47
    • 0033515436 scopus 로고    scopus 로고
    • Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity
    • Betancourt, M. R., and Thirumalai, D. (1999) Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity, J. Mol. Biol. 287, 627-644.
    • (1999) J. Mol. Biol. , vol.287 , pp. 627-644
    • Betancourt, M.R.1    Thirumalai, D.2
  • 48
    • 0037181484 scopus 로고    scopus 로고
    • The chicken-egg scenario of protein folding revisited
    • Uversky, V. N., and Fink, A. L. (2002) The chicken-egg scenario of protein folding revisited, FEBS Lett. 515, 79-83.
    • (2002) FEBS Lett. , vol.515 , pp. 79-83
    • Uversky, V.N.1    Fink, A.L.2
  • 49
    • 0037221599 scopus 로고    scopus 로고
    • Is there a unifying mechanism for protein folding?
    • Daggett, V., and Fersht, A. R. (2003) Is there a unifying mechanism for protein folding? Trends Biochem. Sci. 28, 18-25.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 18-25
    • Daggett, V.1    Fersht, A.R.2
  • 50
    • 0037040411 scopus 로고    scopus 로고
    • The ribosomal exit tunnel functions as a discriminating gate
    • Nakatogawa, H., and Ito, K. (2002) The ribosomal exit tunnel functions as a discriminating gate, Cell 108, 629-636.
    • (2002) Cell , vol.108 , pp. 629-636
    • Nakatogawa, H.1    Ito, K.2
  • 51
    • 0026730739 scopus 로고
    • Confinement as a determinant of macromolecular structure and reactivity
    • Minton, A. P. (1992) Confinement as a determinant of macromolecular structure and reactivity, Biophys. J. 63, 1090-1100.
    • (1992) Biophys. J. , vol.63 , pp. 1090-1100
    • Minton, A.P.1
  • 52
    • 0035949430 scopus 로고    scopus 로고
    • Stabilization of proteins in confined spaces
    • Zhou, H. X., and Dill, K. A. (2001) Stabilization of proteins in confined spaces, Biochemistry 40, 11289-11293.
    • (2001) Biochemistry , vol.40 , pp. 11289-11293
    • Zhou, H.X.1    Dill, K.A.2
  • 53
    • 0037062480 scopus 로고    scopus 로고
    • Simulations of β-hairpin folding confined to spherical pores using distributed computing
    • Klimov, D. K., Newfield, D., and Thirumalai, D. (2002) Simulations of β-hairpin folding confined to spherical pores using distributed computing, Proc. Natl. Acad. Sci. U.S.A. 99, 8019-8024.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 8019-8024
    • Klimov, D.K.1    Newfield, D.2    Thirumalai, D.3
  • 54
    • 0141482088 scopus 로고    scopus 로고
    • How protein thermodynamics and folding mechanisms are altered by the chaperonin cage: Molecular simulations
    • Takagi, F., Koga, N., and Takada, S. (2003) How protein thermodynamics and folding mechanisms are altered by the chaperonin cage: Molecular simulations, Proc. Natl. Acad. Sci. U.S.A. 100, 11367-11372.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 11367-11372
    • Takagi, F.1    Koga, N.2    Takada, S.3
  • 55
    • 19744382834 scopus 로고    scopus 로고
    • Entropically driven helix formation
    • Snir, Y., and Kamien, R. D. (2005) Entropically driven helix formation, Science 307, 1067.
    • (2005) Science , vol.307 , pp. 1067
    • Snir, Y.1    Kamien, R.D.2


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