메뉴 건너뛰기




Volumn 334, Issue 5, 2003, Pages 1063-1076

Solution Structure of the C-terminal Antiparallel coiled-coil Domain from Escherichia coli Osmosensor ProP

Author keywords

Antiparallel coiled coil; Escherichia coli; Nuclear magnetic resonance spectroscopy; Osmosensor; Transporter ProP

Indexed keywords

ADENOSINE TRIPHOSPHATASE INHIBITOR; CARRIER PROTEIN; HEPATITIS DELTA ANTIGEN; INHIBITOR PROTEIN; PEPTIDE DERIVATIVE; PROTEIN PROP; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE INHIBITOR PROTEIN; UNCLASSIFIED DRUG;

EID: 0344010237     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.10.020     Document Type: Article
Times cited : (30)

References (68)
  • 2
    • 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., Wood J.M. Osmosensor ProP of Escherichia coli responds to the concentration, chemistry, and molecular size of osmolytes in the proteoliposome lumen. Biochemistry. 42:2003;410-420.
    • (2003) Biochemistry , vol.42 , pp. 410-420
    • Culham, D.E.1    Henderson, J.2    Crane, R.A.3    Wood, J.M.4
  • 5
    • 0037373068 scopus 로고    scopus 로고
    • Structural model for 12-helix transporters belonging to the major facilitator superfamily
    • Hirai T., Heymann J.A., Maloney P.C., Subramaniam S. Structural model for 12-helix transporters belonging to the major facilitator superfamily. J. Bacteriol. 185:2003;1712-1718.
    • (2003) J. Bacteriol. , vol.185 , pp. 1712-1718
    • Hirai, T.1    Heymann, J.A.2    Maloney, P.C.3    Subramaniam, S.4
  • 6
    • 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., Wood J.M. Isolation and sequencing of Escherichia coli gene proP reveals unusual structural features of the osmoregulatory proline/betaine transporter, ProP. J. Mol. Biol. 229:1993;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
  • 7
    • 0141988874 scopus 로고    scopus 로고
    • Creation of a fully functional cysteine-less variant of osmosensor and proton-osmoprotectant symporter ProP from Escherichia coli and its application to assess the transporter's membrane orientation
    • Culham D.E., Hillar A., Henderson J., Ly A., Vernikovska Y.I., Racher K.I., Boggs J.M., Wood J.M. Creation of a fully functional cysteine-less variant of osmosensor and proton-osmoprotectant symporter ProP from Escherichia coli and its application to assess the transporter's membrane orientation. Biochemistry. 42:2003;11815-11823.
    • (2003) Biochemistry , vol.42 , pp. 11815-11823
    • Culham, D.E.1    Hillar, A.2    Henderson, J.3    Ly, A.4    Vernikovska, Y.I.5    Racher, K.I.6    Boggs, J.M.7    Wood, J.M.8
  • 8
    • 0033833792 scopus 로고    scopus 로고
    • The role of the carboxyl terminal alpha-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., Wood J.M. The role of the carboxyl terminal alpha-helical coiled-coil domain in osmosensing by transporter ProP of Escherichia coli. J. Mol. Recognit. 13:2000;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
  • 9
    • 0024614224 scopus 로고
    • Insertion proQ220Tn5 alters regulation of proline porter II, a transporter of proline and glycine betaine in Escherichia coli
    • Milner J.L., Wood J.M. Insertion proQ220Tn5 alters regulation of proline porter II, a transporter of proline and glycine betaine in Escherichia coli. J. Bacteriol. 171:1989;947-951.
    • (1989) J. Bacteriol. , vol.171 , pp. 947-951
    • Milner, J.L.1    Wood, J.M.2
  • 10
    • 0033057057 scopus 로고    scopus 로고
    • Protein ProQ influences osmotic activation of compatible solute transporter ProP in Escherichia coli K-12
    • Kunte H.J., Crane R.A., Culham D.E., Richmond D., Wood J.M. Protein ProQ influences osmotic activation of compatible solute transporter ProP in Escherichia coli K-12. J. Bacteriol. 181:1999;1537-1543.
    • (1999) J. Bacteriol. , vol.181 , pp. 1537-1543
    • Kunte, H.J.1    Crane, R.A.2    Culham, D.E.3    Richmond, D.4    Wood, J.M.5
  • 11
    • 0032720311 scopus 로고    scopus 로고
    • The role of position a in determining the stability and oligomerization state of alpha-helical coiled coils: 20 amino acid stability coefficients in the hydrophobic core of proteins
    • Wagschal K., Tripet B., Lavigne P., Mant C., Hodges R.S. The role of position a in determining the stability and oligomerization state of alpha-helical coiled coils: 20 amino acid stability coefficients in the hydrophobic core of proteins. Protein Sci. 8:1999;2312-2329.
    • (1999) Protein Sci. , vol.8 , pp. 2312-2329
    • Wagschal, K.1    Tripet, B.2    Lavigne, P.3    Mant, C.4    Hodges, R.S.5
  • 12
    • 0034616959 scopus 로고    scopus 로고
    • Effects of side-chain characteristics on stability and oligomerization state of a de novo-designed model coiled-coil: 20 amino acid substitutions in position "d"
    • Tripet B., Wagschal K., Lavigne P., Mant C.T., Hodges R.S. Effects of side-chain characteristics on stability and oligomerization state of a de novo-designed model coiled-coil: 20 amino acid substitutions in position "d" J. Mol. Biol. 300:2000;377-402.
    • (2000) J. Mol. Biol. , vol.300 , pp. 377-402
    • Tripet, B.1    Wagschal, K.2    Lavigne, P.3    Mant, C.T.4    Hodges, R.S.5
  • 13
    • 0000747247 scopus 로고
    • The Fourier transform of a coiled-coil
    • Crick F.H.C. The Fourier transform of a coiled-coil. Acta Crystallog. 6:1953;685-689.
    • (1953) Acta Crystallog. , vol.6 , pp. 685-689
    • Crick, F.H.C.1
  • 14
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled-coils
    • Crick F.H.C. The packing of α-helices: simple coiled-coils. Acta Crystallog. 6:1953;689-697.
    • (1953) Acta Crystallog. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 15
    • 0034700087 scopus 로고    scopus 로고
    • A computationally directed screen identifying interacting coiled coils from Saccharomyces cerevisiae
    • Newman J.R., Wolf E., Kim P.S. A computationally directed screen identifying interacting coiled coils from Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA. 97:2000;13203-13208.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13203-13208
    • Newman, J.R.1    Wolf, E.2    Kim, P.S.3
  • 16
    • 0035853291 scopus 로고    scopus 로고
    • Socket: A program for identifying and analysing coiled-coil motifs within protein structures
    • Walshaw J., Woolfson D.N. Socket: a program for identifying and analysing coiled-coil motifs within protein structures. J. Mol. Biol. 307:2001;1427-1450.
    • (2001) J. Mol. Biol. , vol.307 , pp. 1427-1450
    • Walshaw, J.1    Woolfson, D.N.2
  • 17
    • 0015463470 scopus 로고
    • Amino-acid sequence of rabbit skeletal tropomyosin and its coiled-coil structure
    • Sodek J., Hodges R.S., Smillie L.B., Jurasek L. Amino-acid sequence of rabbit skeletal tropomyosin and its coiled-coil structure. Proc. Natl Acad. Sci. USA. 69:1972;3800-3804.
    • (1972) Proc. Natl Acad. Sci. USA , vol.69 , pp. 3800-3804
    • Sodek, J.1    Hodges, R.S.2    Smillie, L.B.3    Jurasek, L.4
  • 18
    • 0015302936 scopus 로고
    • Cysteine sequences of rabbit skeletal tropomyosin
    • Hodges R.S., Smillie L.B. Cysteine sequences of rabbit skeletal tropomyosin. Can. J. Biochem. 50:1972;330-343.
    • (1972) Can. J. Biochem. , vol.50 , pp. 330-343
    • Hodges, R.S.1    Smillie, L.B.2
  • 19
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea E.K., Klemm J.D., Kim P.S., Alber T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science. 254:1991;539-544.
    • (1991) Science , vol.254 , pp. 539-544
    • O'shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 20
    • 0030014013 scopus 로고    scopus 로고
    • Investigation of electrostatic interactions in two-stranded coiled-coils through residue shuffling
    • Yu Y., Monera O.D., Hodges R.S., Privalov P.L. Investigation of electrostatic interactions in two-stranded coiled-coils through residue shuffling. Biophys. Chem. 59:1996;299-314.
    • (1996) Biophys. Chem. , vol.59 , pp. 299-314
    • Yu, Y.1    Monera, O.D.2    Hodges, R.S.3    Privalov, P.L.4
  • 21
    • 0029919676 scopus 로고    scopus 로고
    • Ion pairs significantly stabilize coiled-coils in the absence of electrolyte
    • Yu Y., Monera O.D., Hodges R.S., Privalov P.L. Ion pairs significantly stabilize coiled-coils in the absence of electrolyte. J. Mol. Biol. 255:1996;367-372.
    • (1996) J. Mol. Biol. , vol.255 , pp. 367-372
    • Yu, Y.1    Monera, O.D.2    Hodges, R.S.3    Privalov, P.L.4
  • 22
    • 0031133303 scopus 로고    scopus 로고
    • Positional dependence of the effects of negatively charged Glu side chains on the stability of two-stranded alpha-helical coiled-coils
    • Kohn W.D., Kay C.M., Hodges R.S. Positional dependence of the effects of negatively charged Glu side chains on the stability of two-stranded alpha-helical coiled-coils. J. Pept. Sci. 3:1997;209-223.
    • (1997) J. Pept. Sci. , vol.3 , pp. 209-223
    • Kohn, W.D.1    Kay, C.M.2    Hodges, R.S.3
  • 23
    • 0031564608 scopus 로고    scopus 로고
    • Salt effects on protein stability: Two-stranded alpha-helical coiled-coils containing inter- or intrahelical ion pairs
    • Kohn W.D., Kay C.M., Hodges R.S. Salt effects on protein stability: two-stranded alpha-helical coiled-coils containing inter- or intrahelical ion pairs. J. Mol. Biol. 267:1997;1039-1052.
    • (1997) J. Mol. Biol. , vol.267 , pp. 1039-1052
    • Kohn, W.D.1    Kay, C.M.2    Hodges, R.S.3
  • 24
    • 0032514952 scopus 로고    scopus 로고
    • Orientation, positional, additivity, and oligomerization-state effects of interhelical ion pairs in alpha-helical coiled-coils
    • Kohn W.D., Kay C.M., Hodges R.S. Orientation, positional, additivity, and oligomerization-state effects of interhelical ion pairs in alpha-helical coiled-coils. J. Mol. Biol. 283:1998;993-1012.
    • (1998) J. Mol. Biol. , vol.283 , pp. 993-1012
    • Kohn, W.D.1    Kay, C.M.2    Hodges, R.S.3
  • 25
    • 0033556283 scopus 로고    scopus 로고
    • De novo design of a model peptide sequence to examine the effects of single amino acid substitutions in the hydrophobic core on both stability and oligomerization state of coiled-coils
    • Wagschal K., Tripet B., Hodges R.S. De novo design of a model peptide sequence to examine the effects of single amino acid substitutions in the hydrophobic core on both stability and oligomerization state of coiled-coils. J. Mol. Biol. 285:1999;785-803.
    • (1999) J. Mol. Biol. , vol.285 , pp. 785-803
    • Wagschal, K.1    Tripet, B.2    Hodges, R.S.3
  • 28
    • 85030948592 scopus 로고    scopus 로고
    • Detection of α-helical coiled-coil dimer formation by spin-labeled synthetic peptides: A model coiled-coil peptide and a peptide replica of the c-terminal of ProP
    • in the press.
    • A. Hillar, B.T., D. Zoetewey, J. M. Wood, R. S. Hodges, and J. M. Boggs., (2003). Detection of α-helical coiled-coil dimer formation by spin-labeled synthetic peptides: a model coiled-coil peptide and a peptide replica of the c-terminal of ProP. Biochemistry, in the press.
    • (2003) Biochemistry
    • A. Hillar, B.T.1    Zoetewey, D.2    Wood, J.M.3    Hodges, R.S.4    Boggs, J.M.5
  • 29
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Bruce A., Johnson R.A.B. NMRView: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR. 4:1994;604-613.
    • (1994) J. Biomol. NMR , vol.4 , pp. 604-613
    • Bruce, A.1    Johnson, R.A.B.2
  • 31
    • 0036682314 scopus 로고    scopus 로고
    • The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA recombination and repair
    • Hopfner K.P., Craig L., Moncalian G., Zinkel R.A., Usui T., Owen B.A., et al. The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA recombination and repair. Nature. 418:2002;562-566.
    • (2002) Nature , vol.418 , pp. 562-566
    • Hopfner, K.P.1    Craig, L.2    Moncalian, G.3    Zinkel, R.A.4    Usui, T.5    Owen, B.A.6
  • 33
    • 0028105601 scopus 로고
    • The 2.9 Å crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser)
    • Biou V., Yaremchuk A., Tukalo M., Cusack S. The 2.9 Å crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser). Science. 263:1994;1404-1410.
    • (1994) Science , vol.263 , pp. 1404-1410
    • Biou, V.1    Yaremchuk, A.2    Tukalo, M.3    Cusack, S.4
  • 34
    • 0027491528 scopus 로고
    • Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 Å resolution
    • Fujinaga M., Berthet-Colominas C., Yaremchuk A.D., Tukalo M.A., Cusack S. Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 Å resolution. J. Mol. Biol. 234:1993;222-233.
    • (1993) J. Mol. Biol. , vol.234 , pp. 222-233
    • Fujinaga, M.1    Berthet-Colominas, C.2    Yaremchuk, A.D.3    Tukalo, M.A.4    Cusack, S.5
  • 35
    • 0037199975 scopus 로고    scopus 로고
    • The coiled coil region (amino acids 129-250) of the tumor suppressor protein adenomatous polyposis coli (APC). Its structure and its interaction with chromosome maintenance region 1 (Crm-1)
    • Tickenbrock L., Cramer J., Vetter I.R., Muller O. The coiled coil region (amino acids 129-250) of the tumor suppressor protein adenomatous polyposis coli (APC). Its structure and its interaction with chromosome maintenance region 1 (Crm-1). J. Biol. Chem. 277:2002;32332-32338.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32332-32338
    • Tickenbrock, L.1    Cramer, J.2    Vetter, I.R.3    Muller, O.4
  • 36
  • 37
    • 0030581175 scopus 로고    scopus 로고
    • NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone
    • Pellecchia M., Szyperski T., Wall D., Georgopoulos C., Wuthrich K. NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone. J. Mol. Biol. 260:1996;236-250.
    • (1996) J. Mol. Biol. , vol.260 , pp. 236-250
    • Pellecchia, M.1    Szyperski, T.2    Wall, D.3    Georgopoulos, C.4    Wuthrich, K.5
  • 38
    • 0033680802 scopus 로고    scopus 로고
    • Structure of the molecular chaperone prefoldin: Unique interaction of multiple coiled coil tentacles with unfolded proteins
    • Siegert R., Leroux M.R., Scheufler C., Hartl F.U., Moarefi I. Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins. Cell. 103:2000;621-632.
    • (2000) Cell , vol.103 , pp. 621-632
    • Siegert, R.1    Leroux, M.R.2    Scheufler, C.3    Hartl, F.U.4    Moarefi, I.5
  • 39
    • 0035930345 scopus 로고    scopus 로고
    • Crystal structure of colicin E3: Implications for cell entry and ribosome inactivation
    • Soelaiman S., Jakes K., Wu N., Li C., Shoham M. Crystal structure of colicin E3: implications for cell entry and ribosome inactivation. Mol. Cell. 8:2001;1053-1062.
    • (2001) Mol. Cell. , vol.8 , pp. 1053-1062
    • Soelaiman, S.1    Jakes, K.2    Wu, N.3    Li, C.4    Shoham, M.5
  • 40
    • 0030611634 scopus 로고    scopus 로고
    • Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli
    • Uhlin U., Cox G.B., Guss J.M. Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli. Structure. 5:1997;1219-1230.
    • (1997) Structure , vol.5 , pp. 1219-1230
    • Uhlin, U.1    Cox, G.B.2    Guss, J.M.3
  • 43
    • 0037126590 scopus 로고    scopus 로고
    • The structure of bovine IF(1), the regulatory subunit of mitochondrial F-ATPase
    • Cabezon E., Runswick M.J., Leslie A.G., Walker J.E. The structure of bovine IF(1), the regulatory subunit of mitochondrial F-ATPase. EMBO J. 20:2001;6990-6996.
    • (2001) EMBO J. , vol.20 , pp. 6990-6996
    • Cabezon, E.1    Runswick, M.J.2    Leslie, A.G.3    Walker, J.E.4
  • 44
    • 0027275516 scopus 로고
    • Comparison of antiparallel and parallel two-stranded alpha-helical coiled-coils. Design, synthesis, and characterization
    • Monera O.D., Zhou N.E., Kay C.M., Hodges R.S. Comparison of antiparallel and parallel two-stranded alpha-helical coiled-coils. Design, synthesis, and characterization. J. Biol. Chem. 268:1993;19218-19227.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19218-19227
    • Monera, O.D.1    Zhou, N.E.2    Kay, C.M.3    Hodges, R.S.4
  • 45
    • 0028330850 scopus 로고
    • Electrostatic interactions control the parallel and antiparallel orientation of alpha-helical chains in two-stranded alpha-helical coiled-coils
    • Monera O.D., Kay C.M., Hodges R.S. Electrostatic interactions control the parallel and antiparallel orientation of alpha-helical chains in two-stranded alpha-helical coiled-coils. Biochemistry. 33:1994;3862-3871.
    • (1994) Biochemistry , vol.33 , pp. 3862-3871
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 46
    • 0030003190 scopus 로고    scopus 로고
    • The relative positions of alanine residues in the hydrophobic core control the formation of two-stranded or four-stranded alpha-helical coiled-coils
    • Monera O.D., Sonnichsen F.D., Hicks L., Kay C.M., Hodges R.S. The relative positions of alanine residues in the hydrophobic core control the formation of two-stranded or four-stranded alpha-helical coiled-coils. Protein Eng. 9:1996;353-363.
    • (1996) Protein Eng. , vol.9 , pp. 353-363
    • Monera, O.D.1    Sonnichsen, F.D.2    Hicks, L.3    Kay, C.M.4    Hodges, R.S.5
  • 47
    • 0030029835 scopus 로고    scopus 로고
    • Formation of parallel and antiparallel coiled-coils controlled by the relative positions of alanine residues in the hydrophobic core
    • Monera O.D., Zhou N.E., Lavigne P., Kay C.M., Hodges R.S. Formation of parallel and antiparallel coiled-coils controlled by the relative positions of alanine residues in the hydrophobic core. J. Biol. Chem. 271:1996;3995-4001.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3995-4001
    • Monera, O.D.1    Zhou, N.E.2    Lavigne, P.3    Kay, C.M.4    Hodges, R.S.5
  • 48
    • 0031028937 scopus 로고    scopus 로고
    • Protein dissection of the antiparallel coiled coil from Escherichia coli seryl tRNA synthetase
    • Oakley M.G., Kim P.S. Protein dissection of the antiparallel coiled coil from Escherichia coli seryl tRNA synthetase. Biochemistry. 36:1997;2544-2549.
    • (1997) Biochemistry , vol.36 , pp. 2544-2549
    • Oakley, M.G.1    Kim, P.S.2
  • 49
    • 0032497322 scopus 로고    scopus 로고
    • A buried polar interaction can direct the relative orientation of helices in a coiled coil
    • Oakley M.G., Kim P.S. A buried polar interaction can direct the relative orientation of helices in a coiled coil. Biochemistry. 37:1998;12603-12610.
    • (1998) Biochemistry , vol.37 , pp. 12603-12610
    • Oakley, M.G.1    Kim, P.S.2
  • 50
    • 0034837959 scopus 로고    scopus 로고
    • Design and characterization of a heterodimeric coiled coil that forms exclusively with an antiparallel relative helix orientation
    • McClain D.L., Woods H.L., Oakley M.G. Design and characterization of a heterodimeric coiled coil that forms exclusively with an antiparallel relative helix orientation. J. Am. Chem. Soc. 123:2001;3151-3152.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3151-3152
    • Mcclain, D.L.1    Woods, H.L.2    Oakley, M.G.3
  • 52
    • 0020172455 scopus 로고
    • Alpha-Helix dipole model and electrostatic stabilization of 4-alpha-helical proteins
    • Sheridan R.P., Levy R.M., Salemme F.R. alpha-Helix dipole model and electrostatic stabilization of 4-alpha-helical proteins. Proc. Natl Acad. Sci. USA. 79:1982;4545-4549.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 4545-4549
    • Sheridan, R.P.1    Levy, R.M.2    Salemme, F.R.3
  • 53
    • 0019776488 scopus 로고
    • Dipoles of the alpha-helix and beta-sheet: Their role in protein folding
    • Hol W.G., Halie L.M., Sander C. Dipoles of the alpha-helix and beta-sheet: their role in protein folding. Nature. 294:1981;532-536.
    • (1981) Nature , vol.294 , pp. 532-536
    • Hol, W.G.1    Halie, L.M.2    Sander, C.3
  • 54
    • 0033043121 scopus 로고    scopus 로고
    • Purification and reconstitution of an osmosensor: Transporter ProP of Escherichia coli senses and responds to osmotic shifts
    • Racher K.I., Voegele R.T., Marshall E.V., Culham D.E., Wood J.M., Jung H., et al. Purification and reconstitution of an osmosensor: transporter ProP of Escherichia coli senses and responds to osmotic shifts. Biochemistry. 38:1999;1676-1684.
    • (1999) Biochemistry , vol.38 , pp. 1676-1684
    • Racher, K.I.1    Voegele, R.T.2    Marshall, E.V.3    Culham, D.E.4    Wood, J.M.5    Jung, H.6
  • 55
    • 0342545957 scopus 로고    scopus 로고
    • Osmosensor and osmoregulator properties of the betaine carrier BetP from Corynebacterium glutamicum in proteoliposomes
    • Rubenhagen R., Ronsch H., Jung H., Kramer R., Morbach S. Osmosensor and osmoregulator properties of the betaine carrier BetP from Corynebacterium glutamicum in proteoliposomes. J. Biol. Chem. 275:2000;735-741.
    • (2000) J. Biol. Chem. , vol.275 , pp. 735-741
    • Rubenhagen, R.1    Ronsch, H.2    Jung, H.3    Kramer, R.4    Morbach, S.5
  • 56
    • 0033988625 scopus 로고    scopus 로고
    • Glycine betaine transport in Lactococcus lactis is osmotically regulated at the level of expression and translocation activity
    • van Der Heide T., Poolman B. Glycine betaine transport in Lactococcus lactis is osmotically regulated at the level of expression and translocation activity. J. Bacteriol. 182:2000;203-206.
    • (2000) J. Bacteriol. , vol.182 , pp. 203-206
    • Van Der Heide, T.1    Poolman, B.2
  • 57
    • 0036904138 scopus 로고    scopus 로고
    • Body shaping under water stress: Osmosensing and osmoregulation of solute transport in bacteria
    • Morbach S., Kramer R. Body shaping under water stress: osmosensing and osmoregulation of solute transport in bacteria. ChemBiochem. 3:2002;384-397.
    • (2002) ChemBiochem , vol.3 , pp. 384-397
    • Morbach, S.1    Kramer, R.2
  • 59
    • 0028569153 scopus 로고
    • Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions
    • Monera O.D., Kay C.M., Hodges R.S. Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions. Protein Sci. 3:1994;1984-1991.
    • (1994) Protein Sci. , vol.3 , pp. 1984-1991
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 60
    • 0001675109 scopus 로고
    • Relationship between amide proton chemical shifts and hydrogen bonding in amphipathic α-helical peptides
    • Nian E., Zhou B.-Y.Z., Sykes B.D., Hodges S. Relationship between amide proton chemical shifts and hydrogen bonding in amphipathic α-helical peptides. J. Am. Chem. Soc. 114:1992;4320-4326.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 4320-4326
    • Nian, E.1    Zhou, B.-Y.Z.2    Sykes, B.D.3    Hodges, S.4
  • 61
    • 0027275192 scopus 로고
    • Effect of the alpha-amino group on peptide retention behaviour in reversed-phase chromatography. Determination of the pK(a) values of the alpha-amino group of 19 different N-terminal amino acid residues
    • Sereda T.J., Mant C.T., Quinn A.M., Hodges R.S. Effect of the alpha-amino group on peptide retention behaviour in reversed-phase chromatography. Determination of the pK(a) values of the alpha-amino group of 19 different N-terminal amino acid residues. J. Chromatog. 646:1993;17-30.
    • (1993) J. Chromatog. , vol.646 , pp. 17-30
    • Sereda, T.J.1    Mant, C.T.2    Quinn, A.M.3    Hodges, R.S.4
  • 62
    • 0028959280 scopus 로고
    • Protein destabilization by electrostatic repulsions in the two-stranded alpha-helical coiled-coil/leucine zipper
    • Kohn W.D., Kay C.M., Hodges R.S. Protein destabilization by electrostatic repulsions in the two-stranded alpha-helical coiled-coil/leucine zipper. Protein Sci. 4:1995;237-250.
    • (1995) Protein Sci. , vol.4 , pp. 237-250
    • Kohn, W.D.1    Kay, C.M.2    Hodges, R.S.3
  • 63
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 Daltons
    • Karas M., Hillenkamp F. Laser desorption ionization of proteins with molecular masses exceeding 10,000 Daltons. Anal. Chem. 60:1988;2299-2301.
    • (1988) Anal. Chem. , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 65
    • 0023732144 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding
    • Nilges M., Clore G.M., Gronenborn A.M. Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding. FEBS Letters. 239:1988;129-136.
    • (1988) FEBS Letters , vol.239 , pp. 129-136
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 67
    • 0037986814 scopus 로고    scopus 로고
    • BioMagResBank database with sets of experimental NMR constraints corresponding to the structures of over 1400 biomolecules deposited in the Protein Data Bank
    • Doreleijers J.F., Mading S., Maziuk D., Sojourner K., Yin L., Zhu J., et al. BioMagResBank database with sets of experimental NMR constraints corresponding to the structures of over 1400 biomolecules deposited in the Protein Data Bank. J. Biomol. NMR. 26:2003;139-146.
    • (2003) J. Biomol. NMR , vol.26 , pp. 139-146
    • Doreleijers, J.F.1    Mading, S.2    Maziuk, D.3    Sojourner, K.4    Yin, L.5    Zhu, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.