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Volumn 324, Issue 2, 2002, Pages 349-357

Transient structure formation in unfolded acyl-coenzyme A-binding protein observed by site-directed spin labelling

Author keywords

NMR; Paramagnetic relaxation enhancement; Protein folding; Spin labelling; Unfolded state

Indexed keywords

(1 OXYL 2,2,5,5 TETRAMETHYL 3 PYRROLINE 3 METHYL)METHANESULFONATE; ACYL COENZYME A BINDING PROTEIN; BINDING PROTEIN; CYSTEINE; SULFONIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0036438881     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01039-2     Document Type: Article
Times cited : (78)

References (36)
  • 1
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright, P. E. & Dyson, H. J. (1999). Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm. J. Mol. Biol. 293, 321-331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 2
    • 0009586942 scopus 로고    scopus 로고
    • Understanding protein folding via free-energy surfaces from theory and experiment
    • Dinner, A. R., Sali, A., Smith, L. J., Dobson, C. M. & Karplus, M. (2000). Understanding protein folding via free-energy surfaces from theory and experiment. Trends Biochem. Sci. 25, 331-339.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 331-339
    • Dinner, A.R.1    Sali, A.2    Smith, L.J.3    Dobson, C.M.4    Karplus, M.5
  • 3
    • 0035919635 scopus 로고    scopus 로고
    • Persistence of native-like topology in a denatured protein in 8 M urea
    • Shortle, D. & Ackerman, M. S. (2001). Persistence of native-like topology in a denatured protein in 8 M urea. Science, 293, 487-489.
    • (2001) Science , vol.293 , pp. 487-489
    • Shortle, D.1    Ackerman, M.S.2
  • 4
    • 0031932824 scopus 로고    scopus 로고
    • Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding
    • Eliezer, D., Yao, J., Dyson, H. J. & Wright, P. E. (1998). Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nature Struct. Biol. 5, 148-155.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 148-155
    • Eliezer, D.1    Yao, J.2    Dyson, H.J.3    Wright, P.E.4
  • 5
    • 0031585992 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures
    • Gillespie, J. R. & Shortle, D. (1997). Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures. J. Mol. Biol. 268, 170-184.
    • (1997) J. Mol. Biol. , vol.268 , pp. 170-184
    • Gillespie, J.R.1    Shortle, D.2
  • 6
    • 0034705338 scopus 로고    scopus 로고
    • NMR characterization of residual structure in the denatured state of protein L.
    • Yi, Q., Scalley-Kim, M. L., Alm, E. J. & Baker, D. (2000). NMR characterization of residual structure in the denatured state of protein L. J. Mol. Biol. 299, 1341-1351.
    • (2000) J. Mol. Biol. , vol.299 , pp. 1341-1351
    • Yi, Q.1    Scalley-Kim, M.L.2    Alm, E.J.3    Baker, D.4
  • 7
    • 0033546123 scopus 로고    scopus 로고
    • NOE data demonstrating a compact unfolded state for an SH3 domain under non-denaturing conditions
    • Mok, Y. K., Kay, C. M., Kay, L. E. & Forman-Kay, J. (1999). NOE data demonstrating a compact unfolded state for an SH3 domain under non-denaturing conditions. J. Mol. Biol. 289, 619-638.
    • (1999) J. Mol. Biol. , vol.289 , pp. 619-638
    • Mok, Y.K.1    Kay, C.M.2    Kay, L.E.3    Forman-Kay, J.4
  • 9
    • 0035005366 scopus 로고    scopus 로고
    • Preorganized secondary structure as an important determinant of fast protein folding
    • Myers, J. K. & Oas, T. G. (2001). Preorganized secondary structure as an important determinant of fast protein folding. Nature Struct. Biol. 8, 552-558.
    • (2001) Nature Struct. Biol. , vol.8 , pp. 552-558
    • Myers, J.K.1    Oas, T.G.2
  • 11
    • 0033012840 scopus 로고    scopus 로고
    • Hydration of denatured and molten globule proteins
    • Denisov, V. P., Jonsson, B. H. & Halle, B. (1999). Hydration of denatured and molten globule proteins. Nature Struct. Biol. 6, 253-260.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 253-260
    • Denisov, V.P.1    Jonsson, B.H.2    Halle, B.3
  • 12
    • 0033015989 scopus 로고    scopus 로고
    • The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP
    • Kragelund, B. B., Osmark, P., Neergård, T. B., Schiødt, J., Kristiansen, K., Knudsen, J. & Poulsen, F. M. (1999). The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. Nature Struct. Biol. 6, 594-601.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 594-601
    • Kragelund, B.B.1    Osmark, P.2    Neergård, T.B.3    Schiødt, J.4    Kristiansen, K.5    Knudsen, J.6    Poulsen, F.M.7
  • 13
    • 0034283356 scopus 로고    scopus 로고
    • Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP
    • Teilum, K., Kragelund, B. B., Knudsen, J. & Poulsen, F. M. (2000). Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP. J. Mol. Biol. 301, 1307-1314.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1307-1314
    • Teilum, K.1    Kragelund, B.B.2    Knudsen, J.3    Poulsen, F.M.4
  • 14
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart, D. S., Sykes, B. D. & Richards, F. M. (1992). The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry, 31, 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 15
    • 0027605077 scopus 로고
    • The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver: Structural refinement using heteronuclear multidimensional NMR spectroscopy
    • Andersen, K. V. & Poulsen, F. M. (1993). The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver: Structural refinement using heteronuclear multidimensional NMR spectroscopy. J. Biomol. NMR, 3, 271-284.
    • (1993) J. Biomol. NMR , vol.3 , pp. 271-284
    • Andersen, K.V.1    Poulsen, F.M.2
  • 16
    • 0035906650 scopus 로고    scopus 로고
    • Calculation of ensembles of structures representing the unfolded state of an SH3 domain
    • Choy, W.-Y. & Forman-Kay, J. D. (2001). Calculation of ensembles of structures representing the unfolded state of an SH3 domain. J. Mol. Biol. 308, 1011-1032.
    • (2001) J. Mol. Biol. , vol.308 , pp. 1011-1032
    • Choy, W.-Y.1    Forman-Kay, J.D.2
  • 17
    • 0030900199 scopus 로고    scopus 로고
    • NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions
    • Zhang, O. & Forman-Kay, J. D. (1997). NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions. Biochemistry, 36, 3959-3970.
    • (1997) Biochemistry , vol.36 , pp. 3959-3970
    • Zhang, O.1    Forman-Kay, J.D.2
  • 18
    • 0031735017 scopus 로고    scopus 로고
    • Mapping the lifetimes of local opening events in a native state protein
    • Kragelund, B. B., Heinemann, B., Knudsen, J. & Poulsen, F. M. (1998). Mapping the lifetimes of local opening events in a native state protein. Protein Sci. 7, 2237-2248.
    • (1998) Protein Sci. , vol.7 , pp. 2237-2248
    • Kragelund, B.B.1    Heinemann, B.2    Knudsen, J.3    Poulsen, F.M.4
  • 20
    • 0034714154 scopus 로고    scopus 로고
    • Two-state expansion and collapse of a polypeptide
    • Hagen, S. J. & Eaton, W. A. (2000). Two-state expansion and collapse of a polypeptide. J. Mol. Biol. 301, 1019-1027.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1019-1027
    • Hagen, S.J.1    Eaton, W.A.2
  • 21
    • 0032978994 scopus 로고    scopus 로고
    • Chain collapse can occur concomitantly with the rate-limiting step in protein folding
    • Plaxco, K. W., Millett, I. S., Segel, D. J., Doniach, S. & Baker, D. (1999). Chain collapse can occur concomitantly with the rate-limiting step in protein folding. Nature Struct. Biol. 6, 554-556.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 554-556
    • Plaxco, K.W.1    Millett, I.S.2    Segel, D.J.3    Doniach, S.4    Baker, D.5
  • 22
    • 0036301154 scopus 로고    scopus 로고
    • Transient intermediary states with high and low folding probabilities in the apparent two-state folding equilibrium of ACBP at low pH
    • Thomsen, J. K., Kragelund, B. B., Teilum, K., Knudsen, J. & Poulsen, F. M. (2002). Transient intermediary states with high and low folding probabilities in the apparent two-state folding equilibrium of ACBP at low pH. J. Mol. Biol. 318, 805-814.
    • (2002) J. Mol. Biol. , vol.318 , pp. 805-814
    • Thomsen, J.K.1    Kragelund, B.B.2    Teilum, K.3    Knudsen, J.4    Poulsen, F.M.5
  • 23
    • 0034646562 scopus 로고    scopus 로고
    • Similarities between the spectrin SH3 domain denatured state and its folding transition state
    • Kortemme, T., Kelly, M. J., Kay, L. E., Forman-Kay, J. & Serrano, L. (2000). Similarities between the spectrin SH3 domain denatured state and its folding transition state. J. Mol. Biol. 297, 1217-1229.
    • (2000) J. Mol. Biol. , vol.297 , pp. 1217-1229
    • Kortemme, T.1    Kelly, M.J.2    Kay, L.E.3    Forman-Kay, J.4    Serrano, L.5
  • 24
    • 0032750509 scopus 로고    scopus 로고
    • The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved
    • Martinez, J. C. & Serrano, L. (1999). The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nature Struct. Biol. 6, 1010-1016.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 1010-1016
    • Martinez, J.C.1    Serrano, L.2
  • 25
    • 0037162450 scopus 로고    scopus 로고
    • Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing
    • Teilum, K., Maki, K., Kragelund, B. B., Poulsen, F. M. & Roder, H. (2002). Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing. Proc. Natl. Acad. Sci. USA, 99, 9807-9812.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9807-9812
    • Teilum, K.1    Maki, K.2    Kragelund, B.B.3    Poulsen, F.M.4    Roder, H.5
  • 26
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
    • Jackson, S. E. & Fersht, A. R. (1991). Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry, 30, 10428-10435.
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 27
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J. & Bax, A. (1995). NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR, 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 28
    • 0028673711 scopus 로고
    • Automated and semiautomated analysis of homo-and heteronuclear multidimensional nuclear magnetic resonance spectra of proteins: The program Pronto
    • Kjær, M., Andersen, K. V. & Poulsen, F. M. (1994). Automated and semiautomated analysis of homo-and heteronuclear multidimensional nuclear magnetic resonance spectra of proteins: The program Pronto. Methods Enzymol., 288-307.
    • (1994) Methods Enzymol. , pp. 288-307
    • Kjær, M.1    Andersen, K.V.2    Poulsen, F.M.3
  • 29
    • 0024853292 scopus 로고
    • Spin labeling of proteins
    • Kosen, P. A. (1989). Spin labeling of proteins. Methods Enzymol. 177, 86-121.
    • (1989) Methods Enzymol. , vol.177 , pp. 86-121
    • Kosen, P.A.1
  • 30
    • 0034625121 scopus 로고    scopus 로고
    • Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data
    • Battiste, J. L. & Wagner, G. (2000). Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data. Biochemistry, 39, 5355-5365.
    • (2000) Biochemistry , vol.39 , pp. 5355-5365
    • Battiste, J.L.1    Wagner, G.2
  • 31
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR, 5, 67-81.
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 32
    • 0028873081 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides
    • Muñoz, V. & Serrano, L. (1995). Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides. J. Mol. Biol. 245, 275-296.
    • (1995) J. Mol. Biol. , vol.245 , pp. 275-296
    • Muñoz, V.1    Serrano, L.2
  • 33
    • 0028834210 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence
    • Muñoz, V. & Serrano, L. (1995). Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence. J. Mol. Biol. 245, 297-308.
    • (1995) J. Mol. Biol. , vol.245 , pp. 297-308
    • Muñoz, V.1    Serrano, L.2
  • 34
    • 0018093765 scopus 로고
    • Conformational preferences of amino acids in globular proteins
    • Levitt, M. (1978). Conformational preferences of amino acids in globular proteins. Biochemistry, 17, 4277-4285.
    • (1978) Biochemistry , vol.17 , pp. 4277-4285
    • Levitt, M.1
  • 35
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. & Doolittle, R. F. (1982). A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 36
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991). MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


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