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Volumn 330, Issue 2, 2003, Pages 397-407

Rapid formation of non-native contacts during the folding of HPr revealed by real-time photo-CIDNP NMR and stopped-flow fluorescence experiments

Author keywords

Fluorescence; Non native contacts; Photo CIDNP; Protein folding; Real time NMR

Indexed keywords

ENZYME; GLOBULAR PROTEIN; HISTIDINE; IODIDE; MEMBRANE ENZYME; MUTANT PROTEIN; PHENYLALANINE; PROTEIN F 2 W; PROTEIN F 29 W; PROTEIN F 48 W; PROTEIN HPR; QUERCETIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 0038461959     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00507-2     Document Type: Article
Times cited : (35)

References (31)
  • 1
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24:1999;329-332.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 2
    • 0033617266 scopus 로고    scopus 로고
    • From computer simulations to human disease: Emerging themes in protein folding
    • Radford S.E., Dobson C.M. From computer simulations to human disease: emerging themes in protein folding. Cell. 97:1999;291-298.
    • (1999) Cell , vol.97 , pp. 291-298
    • Radford, S.E.1    Dobson, C.M.2
  • 3
    • 0037102362 scopus 로고    scopus 로고
    • Getting out of shape
    • Dobson C.M. Getting out of shape. Nature. 418:2002;729-730.
    • (2002) Nature , vol.418 , pp. 729-730
    • Dobson, C.M.1
  • 4
    • 0037154980 scopus 로고    scopus 로고
    • Protein folding and unfolding at atomic resolution
    • Fersht A.R., Daggett V. Protein folding and unfolding at atomic resolution. Cell. 108:2002;573-582.
    • (2002) Cell , vol.108 , pp. 573-582
    • Fersht, A.R.1    Daggett, V.2
  • 5
    • 0037041441 scopus 로고    scopus 로고
    • Medicine: Danger - Misfolding proteins
    • Ellis R.J., Pinheiro T.J.T. Medicine: danger - misfolding proteins. Nature. 416:2002;483-484.
    • (2002) Nature , vol.416 , pp. 483-484
    • Ellis, R.J.1    Pinheiro, T.J.T.2
  • 9
    • 0013177063 scopus 로고    scopus 로고
    • Millisecond time resolved Photo-CIDNP NMR reveals a non-native folding intermediate on the ion induced refolding pathway of bovine-Lactalbumin
    • Wirmer J., Kühn T., Schwalbe H. Millisecond time resolved Photo-CIDNP NMR reveals a non-native folding intermediate on the ion induced refolding pathway of bovine-Lactalbumin. Angew. Chem. 113:2001;4378-4381.
    • (2001) Angew. Chem. , vol.113 , pp. 4378-4381
    • Wirmer, J.1    Kühn, T.2    Schwalbe, H.3
  • 10
    • 0001690074 scopus 로고
    • Photo-CIDNP of amino acids and proteins: Effects of competition for flavin triplets
    • Winder S.L., Broadhurst R.W., Hore P.J. Photo-CIDNP of amino acids and proteins: effects of competition for flavin triplets. Spectrochim. Acta part A. 51:1995;1753-1761.
    • (1995) Spectrochim. Acta Part A , vol.51 , pp. 1753-1761
    • Winder, S.L.1    Broadhurst, R.W.2    Hore, P.J.3
  • 11
    • 0028360724 scopus 로고
    • The high-resolution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from nuclear magnetic resonance nuclear Overhauser effect data
    • Van Nuland N.A.J., Hangyi I.W., Van Schaik R.C., Berendsen H.J.C., Van Gunsteren W.F., Scheek R.M., Robillard G.T. The high-resolution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from nuclear magnetic resonance nuclear Overhauser effect data. J. Mol. Biol. 237:1994;544-559.
    • (1994) J. Mol. Biol. , vol.237 , pp. 544-559
    • Van Nuland, N.A.J.1    Hangyi, I.W.2    Van Schaik, R.C.3    Berendsen, H.J.C.4    Van Gunsteren, W.F.5    Scheek, R.M.6    Robillard, G.T.7
  • 12
    • 0027291428 scopus 로고
    • Phosphoenol-pyruvate:carbohydrate phosphotransferase systems of bacteria
    • Postma P.W., Lengeler J.W., Jacobson G.R. Phosphoenol-pyruvate:carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 57:1993;543-594.
    • (1993) Microbiol. Rev. , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 13
    • 0022404159 scopus 로고
    • Reactivities of tyrosine, histidine, tryptophan, and methionine in radical pair formation in flavin triplet induced protein nuclear magnetic polarization
    • Muszkat K.A., Wismontski-Knittel T. Reactivities of tyrosine, histidine, tryptophan, and methionine in radical pair formation in flavin triplet induced protein nuclear magnetic polarization. Biochemistry. 24:1985;5416-5421.
    • (1985) Biochemistry , vol.24 , pp. 5416-5421
    • Muszkat, K.A.1    Wismontski-Knittel, T.2
  • 14
    • 0036629168 scopus 로고    scopus 로고
    • Mechanisms of reactions of flavin mononucleotide triplet with aromatic amino acids
    • Tsentalovich Y.P., Lopez J.J., Hore P.J., Sagdeev R.Z. Mechanisms of reactions of flavin mononucleotide triplet with aromatic amino acids. Spectrochim. Acta part A. 58:2002;2043-2050.
    • (2002) Spectrochim. Acta part A , vol.58 , pp. 2043-2050
    • Tsentalovich, Y.P.1    Lopez, J.J.2    Hore, P.J.3    Sagdeev, R.Z.4
  • 18
    • 0028227296 scopus 로고
    • Tertiary interactions in the folding pathway of hen lysozyme: Kinetic studies using fluorescent probes
    • Itzhaki L.S., Evans P.A., Dobson C.M., Radford S.E. Tertiary interactions in the folding pathway of hen lysozyme: kinetic studies using fluorescent probes. Biochemistry. 33:1994;5212-5220.
    • (1994) Biochemistry , vol.33 , pp. 5212-5220
    • Itzhaki, L.S.1    Evans, P.A.2    Dobson, C.M.3    Radford, S.E.4
  • 19
    • 0032539580 scopus 로고    scopus 로고
    • A collapsed intermediate with nonnative packing of hydrophobic residues in the folding of TEM-1 beta-lactamase
    • Vanhove M., Lejeune A., Guillaume G., Virden R., Pain R.H., Schmid F.X., Frere J.M. A collapsed intermediate with nonnative packing of hydrophobic residues in the folding of TEM-1 beta-lactamase. Biochemistry. 37:1998;1941-1950.
    • (1998) Biochemistry , vol.37 , pp. 1941-1950
    • Vanhove, M.1    Lejeune, A.2    Guillaume, G.3    Virden, R.4    Pain, R.H.5    Schmid, F.X.6    Frere, J.M.7
  • 20
    • 0027448054 scopus 로고
    • The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system
    • Van Nuland N.A.J., Kroon G.J.A., Dijkstra K., Wolters G.K., Scheek R.M., Robillard G.T. The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system. FEBS Letters. 315:1993;11-15.
    • (1993) FEBS Letters , vol.315 , pp. 11-15
    • Van Nuland, N.A.J.1    Kroon, G.J.A.2    Dijkstra, K.3    Wolters, G.K.4    Scheek, R.M.5    Robillard, G.T.6
  • 21
    • 0028905499 scopus 로고
    • High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data
    • Van Nuland N.A.J., Boelens R., Scheek R.M., Robillard G.T. High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data. J. Mol. Biol. 246:1995;180-193.
    • (1995) J. Mol. Biol. , vol.246 , pp. 180-193
    • Van Nuland, N.A.J.1    Boelens, R.2    Scheek, R.M.3    Robillard, G.T.4
  • 23
    • 0036183221 scopus 로고    scopus 로고
    • Im7 folding mechanism: Misfolding on a path to the native state
    • Capaldi A.P., Kleanthous C., Radford S.E. Im7 folding mechanism: misfolding on a path to the native state. Nature Struct. Biol. 3:2002;209-216.
    • (2002) Nature Struct. Biol. , vol.3 , pp. 209-216
    • Capaldi, A.P.1    Kleanthous, C.2    Radford, S.E.3
  • 25
    • 0017896443 scopus 로고
    • Laser photo-CIDNP as a surface probe for proteins in solution
    • Kaptein R., Dijkstra K., Nicolay K. Laser photo-CIDNP as a surface probe for proteins in solution. Nature. 274:1978;293-294.
    • (1978) Nature , vol.274 , pp. 293-294
    • Kaptein, R.1    Dijkstra, K.2    Nicolay, K.3
  • 26
    • 0001073545 scopus 로고
    • An inexpensive, versatile sample illuminator for photo-CIDNP on any NMR spectrometer
    • Scheffler J.E., Cottrell C.E., Berliner L.J. An inexpensive, versatile sample illuminator for photo-CIDNP on any NMR spectrometer. J. Magn. Reson. 63:1985;199-201.
    • (1985) J. Magn. Reson. , vol.63 , pp. 199-201
    • Scheffler, J.E.1    Cottrell, C.E.2    Berliner, L.J.3
  • 29
    • 0035067076 scopus 로고    scopus 로고
    • High-sensitivity fluorescence anisotropy detection of protein-folding events: Application to alpha-lactalbumin
    • Canet D., Doering K., Dobson C.M., Dupont Y. High-sensitivity fluorescence anisotropy detection of protein-folding events: application to alpha-lactalbumin. Biophys. J. 80:2001;1996-2003.
    • (2001) Biophys. J. , vol.80 , pp. 1996-2003
    • Canet, D.1    Doering, K.2    Dobson, C.M.3    Dupont, Y.4
  • 30
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 31
    • 0038031767 scopus 로고    scopus 로고
    • Characterization of single-tryptophan mutants of Histidine-containing Phosphocarrier Protein: Evidence for local rearrangements during folding from high concentrations of denaturant
    • Azuaga A.I., Canet D., Smeenk G., Berends R., Titgemeyer F., Duurkens R., et al. Characterization of single-tryptophan mutants of Histidine-containing Phosphocarrier Protein: Evidence for local rearrangements during folding from high concentrations of denaturant. Biochemistry. 42:2003;4883-4895.
    • (2003) Biochemistry , vol.42 , pp. 4883-4895
    • Azuaga, A.I.1    Canet, D.2    Smeenk, G.3    Berends, R.4    Titgemeyer, F.5    Duurkens, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.