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Volumn 9, Issue 1, 2000, Pages 20-28

NMR analysis of cleaved Escherichia coli thioredoxin (1-73/74-108) and its P76A variant: Cis/trans peptide isomerization

Author keywords

Cis trans proline isomerization; Fragment complementation; Reassembled thioredoxin

Indexed keywords

THIOREDOXIN;

EID: 0033970021     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.1.20     Document Type: Article
Times cited : (22)

References (51)
  • 1
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A, Davis DG. 1985. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J Magn Reson 65:335-360.
    • (1985) J Magn Reson , vol.65 , pp. 335-360
    • Bax, A.1    Davis, D.G.2
  • 2
    • 0031430923 scopus 로고    scopus 로고
    • Recognition between disordered states: Kinetics of the self-assembly of complementary thioredoxin fragments (1-73, 74-108)
    • Chaffotte A, Li JH, Goldberg M, Tasayco ML. 1997. Recognition between disordered states: Kinetics of the self-assembly of complementary thioredoxin fragments (1-73, 74-108). Biochemistry 36:16040-16048.
    • (1997) Biochemistry , vol.36 , pp. 16040-16048
    • Chaffotte, A.1    Li, J.H.2    Goldberg, M.3    Tasayco, M.L.4
  • 4
    • 0024469970 scopus 로고
    • Assignment of the proton NMR spectrum of reduced and oxidized thioredoxin: Sequence-specific assignments, secondary structure, and global fold
    • Dyson HJ, Holmgren A, Wright PE. 1989. Assignment of the proton NMR spectrum of reduced and oxidized thioredoxin: Sequence-specific assignments, secondary structure, and global fold. Biochemistry 28:7074-7087.
    • (1989) Biochemistry , vol.28 , pp. 7074-7087
    • Dyson, H.J.1    Holmgren, A.2    Wright, P.E.3
  • 5
    • 0023218558 scopus 로고
    • Proline isomerism in staphylococcal nuclease characterised by NMR and site-directed mutagenesis
    • Evans PA, Dobson CM, Kautz RA, Hatfull G, Fox RO. 1987. Proline isomerism in staphylococcal nuclease characterised by NMR and site-directed mutagenesis. Nature 329:266-270.
    • (1987) Nature , vol.329 , pp. 266-270
    • Evans, P.A.1    Dobson, C.M.2    Kautz, R.A.3    Hatfull, G.4    Fox, R.O.5
  • 6
    • 0032833032 scopus 로고    scopus 로고
    • Energetics of assembling an artificial heterodimer with an α/β motif: Cleaved versus uncleaved Escherichia coli thioredoxin
    • Georgescu RE, Braswell EH, Zhu D, Tasayco ML. 1999. Energetics of assembling an artificial heterodimer with an α/β motif: Cleaved versus uncleaved Escherichia coli thioredoxin. Biochemistry 38:13355-13366.
    • (1999) Biochemistry , vol.38 , pp. 13355-13366
    • Georgescu, R.E.1    Braswell, E.H.2    Zhu, D.3    Tasayco, M.L.4
  • 7
    • 0026055156 scopus 로고
    • Analysis of the steric strain in the polypeptide backbone of protein molecules
    • Herzberg O, Moult J. 1991. Analysis of the steric strain in the polypeptide backbone of protein molecules. Proteins Struct Funct Genet 11:223-229.
    • (1991) Proteins Struct Funct Genet , vol.11 , pp. 223-229
    • Herzberg, O.1    Moult, J.2
  • 8
    • 0027366421 scopus 로고
    • NMR strategy for determining Xaa-pro peptide bond configurations in proteins: Mutants of staphylococcal nuclease with altered configuration at proline-117
    • Hinck AP, Eberhardt ES, Markley JL. 1993. NMR strategy for determining Xaa-pro peptide bond configurations in proteins: Mutants of staphylococcal nuclease with altered configuration at proline-117. Biochemistry 32:11810-11818.
    • (1993) Biochemistry , vol.32 , pp. 11810-11818
    • Hinck, A.P.1    Eberhardt, E.S.2    Markley, J.L.3
  • 9
    • 0028269722 scopus 로고
    • The importance of anchorage in determining a strained protein loop conformation
    • Hodel A, Kautz RA, Adelman DM, Fox RO. 1994. The importance of anchorage in determining a strained protein loop conformation. Protein Sci 3:549-556.
    • (1994) Protein Sci , vol.3 , pp. 549-556
    • Hodel, A.1    Kautz, R.A.2    Adelman, D.M.3    Fox, R.O.4
  • 11
    • 0025877987 scopus 로고
    • The crystal structure of staphylococcal nuclease refined at 1.7 Å resolution
    • Hynes TR, Fox RO. 1991. The crystal structure of staphylococcal nuclease refined at 1.7 Å resolution. Proteins Struct Funct Genet 10:92-105.
    • (1991) Proteins Struct Funct Genet , vol.10 , pp. 92-105
    • Hynes, T.R.1    Fox, R.O.2
  • 12
    • 0028174179 scopus 로고
    • Engineering alternative - Turn types in staphylococcal nuclease
    • Hynes TR, Hodel A. Fox RO. 1994. Engineering alternative - Turn types in staphylococcal nuclease. Biochemistry 33:5021-5030.
    • (1994) Biochemistry , vol.33 , pp. 5021-5030
    • Hynes, T.R.1    Hodel, A.2    Fox, R.O.3
  • 13
    • 0033548058 scopus 로고    scopus 로고
    • Non-proline cis peptide bonds in proteins
    • Jabs A, Weiss MS, Hilgenfeld R. 1999. Non-proline cis peptide bonds in proteins. J Mol Biol 286:291-304.
    • (1999) J Mol Biol , vol.286 , pp. 291-304
    • Jabs, A.1    Weiss, M.S.2    Hilgenfeld, R.3
  • 15
    • 0030010605 scopus 로고    scopus 로고
    • Experimentally observed conformation-dependent geometry and hidden strain in proteins
    • Karplus PA. 1996. Experimentally observed conformation-dependent geometry and hidden strain in proteins. Protein Sci 5:1406-1420.
    • (1996) Protein Sci , vol.5 , pp. 1406-1420
    • Karplus, P.A.1
  • 16
    • 0025319619 scopus 로고
    • Crystal structure ot thioredoxin from Escherichia coli at 1.68 Å resolution
    • Katti SK, LeMaster DL, Eklund H. 1990. Crystal structure ot thioredoxin from Escherichia coli at 1.68 Å resolution. J Mol Biol 212:167-184.
    • (1990) J Mol Biol , vol.212 , pp. 167-184
    • Katti, S.K.1    LeMaster, D.L.2    Eklund, H.3
  • 18
    • 0023660997 scopus 로고
    • Replacement of proline-76 with alanine eliminates the slowest kinetic phase in thioredoxin folding
    • Kelley RF, Richards FM. 1987. Replacement of proline-76 with alanine eliminates the slowest kinetic phase in thioredoxin folding. Biochemistry 26: 6765-6774.
    • (1987) Biochemistry , vol.26 , pp. 6765-6774
    • Kelley, R.F.1    Richards, F.M.2
  • 19
    • 0025287813 scopus 로고
    • The rate and structural consequences of proline cis-trans isomerization in calbinding D9k: NMR studies of the minor (cis-pro43) isoform and the Pro43Gly mutant
    • Kordel J, Forsen S, Drakenberg T, Chazin WJ. 1990. The rate and structural consequences of proline cis-trans isomerization in calbinding D9k: NMR studies of the minor (cis-pro43) isoform and the Pro43Gly mutant. Biochemistry 29:4400-4409.
    • (1990) Biochemistry , vol.29 , pp. 4400-4409
    • Kordel, J.1    Forsen, S.2    Drakenberg, T.3    Chazin, W.J.4
  • 20
    • 0024603939 scopus 로고
    • Escherichia coli thioredoxin folds into two compact forms of different stability to urea denaturation
    • Langsetmo K, Fuchs J, Woodward C. 1989. Escherichia coli thioredoxin folds into two compact forms of different stability to urea denaturation. Biochemistry 28:3211-3220.
    • (1989) Biochemistry , vol.28 , pp. 3211-3220
    • Langsetmo, K.1    Fuchs, J.2    Woodward, C.3
  • 21
    • 0028022578 scopus 로고
    • 13C-HMQC-NOESY experiment for extracting intermolecular NOE contacts in molecular complexes
    • 13C-HMQC-NOESY experiment for extracting intermolecular NOE contacts in molecular complexes. FEBS Lett 350:87-90.
    • (1994) FEBS Lett , vol.350 , pp. 87-90
    • Lee, W.1    Revington, M.J.2    Arrowsmith, C.3    Kay, L.E.4
  • 23
    • 0033573854 scopus 로고    scopus 로고
    • Effect of proline mutations on the folding ot staphylococcal nuclease
    • Maki K, Ikura T, Takahashi N, Kuwajima K. 1999. Effect of proline mutations on the folding ot staphylococcal nuclease. Biochemistry 38:2213-2223.
    • (1999) Biochemistry , vol.38 , pp. 2213-2223
    • Maki, K.1    Ikura, T.2    Takahashi, N.3    Kuwajima, K.4
  • 24
    • 0028111284 scopus 로고
    • Generation of a non-prolyl cis peptide bond in ribonuclease T1
    • Mayr LM, Willbold D, Rösch P, Schmid FX. 1994. Generation of a non-prolyl cis peptide bond in ribonuclease T1. J Mol Biol 240:288-293.
    • (1994) J Mol Biol , vol.240 , pp. 288-293
    • Mayr, L.M.1    Willbold, D.2    Rösch, P.3    Schmid, F.X.4
  • 26
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solution
    • Piotto M, Saudek U, Sklenar U. 1992. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solution. J Biomol NMR 2:661-666.
    • (1992) J Biomol NMR , vol.2 , pp. 661-666
    • Piotto, M.1    Saudek, U.2    Sklenar, U.3
  • 28
    • 0000527952 scopus 로고
    • 1H NMR spectra of proteins using multiple-quantum coherence
    • 1H NMR spectra of proteins using multiple-quantum coherence. J Magn Reson 66:372-378.
    • (1986) J Magn Reson , vol.66 , pp. 372-378
    • Ranee, M.1    Wright, P.E.2
  • 30
    • 0032513016 scopus 로고    scopus 로고
    • Modulation of high affinity hormone binding: Human choriogonadotropin binding to the exodomain of the receptor is influenced by exoloop 2 of the receptor
    • Ryu KS, Lee H Y, Kim SP, Beauchamp J, Tung CS, Issacs NW, Ji I, Ji TH. 1998. Modulation of high affinity hormone binding: Human choriogonadotropin binding to the exodomain of the receptor is influenced by exoloop 2 of the receptor. J Biol Chem 273:6285-6291.
    • (1998) J Biol Chem , vol.273 , pp. 6285-6291
    • Ryu, K.S.1    Lee H, Y.2    Kim, S.P.3    Beauchamp, J.4    Tung, C.S.5    Issacs, N.W.6    Ji, I.7    Ji, T.H.8
  • 31
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1100 kDa
    • Schägger H, von Jagow G. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1100 kDa. Anal Biochem 166:368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 32
    • 0027050499 scopus 로고
    • Cis proline mutants of ribonuclease A. I. Thermal stability
    • Schultz DA, Baldwin RL. 1992. Cis proline mutants of ribonuclease A. I. Thermal stability. Protein Sci 1:910-916.
    • (1992) Protein Sci , vol.1 , pp. 910-916
    • Schultz, D.A.1    Baldwin, R.L.2
  • 33
    • 0027049568 scopus 로고
    • Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms by mutation
    • Schultz DA, Schmid FX, Baldwin RL. 1992. Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms by mutation. Protein Sci 1:911-924.
    • (1992) Protein Sci , vol.1 , pp. 911-924
    • Schultz, D.A.1    Schmid, F.X.2    Baldwin, R.L.3
  • 34
  • 35
    • 13444269041 scopus 로고
    • Computer-optimized decoupling scheme for wideband applications and low-level operation
    • Shaka AJ, Barker PB, Freeman R. 1985. Computer-optimized decoupling scheme for wideband applications and low-level operation. J Magn Reson 64:547-552.
    • (1985) J Magn Reson , vol.64 , pp. 547-552
    • Shaka, A.J.1    Barker, P.B.2    Freeman, R.3
  • 36
    • 45449123980 scopus 로고
    • Iterative schemes for bilinear operators: Application to spin decoupling
    • Shaka AJ, Lee CJ, Pines A. 1988. Iterative schemes for bilinear operators: Application to spin decoupling. J Magn Reson 77:274-293.
    • (1988) J Magn Reson , vol.77 , pp. 274-293
    • Shaka, A.J.1    Lee, C.J.2    Pines, A.3
  • 37
    • 58149365344 scopus 로고
    • WET solvent suppression and its applications to LC NMR and high-resolution NMR spectroscopy
    • Smallcombe SH, Patt SL, Keifer PA. 1995. WET solvent suppression and its applications to LC NMR and high-resolution NMR spectroscopy. J Magn Reson 117:295-303.
    • (1995) J Magn Reson , vol.117 , pp. 295-303
    • Smallcombe, S.H.1    Patt, S.L.2    Keifer, P.A.3
  • 38
    • 0025299887 scopus 로고
    • Occurrence and role of cis peptide bonds in protein structures
    • Stewart DE, Sarkar A, Wampler JE. 1990. Occurrence and role of cis peptide bonds in protein structures. J Mol Biol 214:253-260.
    • (1990) J Mol Biol , vol.214 , pp. 253-260
    • Stewart, D.E.1    Sarkar, A.2    Wampler, J.E.3
  • 39
    • 0026503169 scopus 로고
    • Proline cis-trans isomers in calbindin d9k observed by X-ray crystallography
    • Svensson LA, Thulin A, Forsten S. 1992. Proline cis-trans isomers in calbindin d9k observed by X-ray crystallography. J Mol Biol 223:601-606.
    • (1992) J Mol Biol , vol.223 , pp. 601-606
    • Svensson, L.A.1    Thulin, A.2    Forsten, S.3
  • 40
    • 0031580205 scopus 로고    scopus 로고
    • The rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2
    • Tan YJ, Oliveberg M, Otzen DE, Fersht AR. 1997. The rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2. J Mol Biol 269:611-622.
    • (1997) J Mol Biol , vol.269 , pp. 611-622
    • Tan, Y.J.1    Oliveberg, M.2    Otzen, D.E.3    Fersht, A.R.4
  • 41
    • 0029027777 scopus 로고
    • NMR study of the reconstitution of the β-sheet of thioredoxin by fragment complementation
    • Tasayco ML, Chao K. 1995. NMR study of the reconstitution of the β-sheet of thioredoxin by fragment complementation. Proteins Struct Funct Genet 22:41-44.
    • (1995) Proteins Struct Funct Genet , vol.22 , pp. 41-44
    • Tasayco, M.L.1    Chao, K.2
  • 42
    • 0024343074 scopus 로고
    • Proline assignments and identification of the cis K116/P117 peptide bond in liganded staphylococcal nuclease using isotope edited 2D NMR spectroscopy
    • Torchia DA, Sparks SW, Young PE, Bax A. 1989. Proline assignments and identification of the cis K116/P117 peptide bond in liganded staphylococcal nuclease using isotope edited 2D NMR spectroscopy. J Am Chem Soc 111:8315-8317.
    • (1989) J Am Chem Soc , vol.111 , pp. 8315-8317
    • Torchia, D.A.1    Sparks, S.W.2    Young, P.E.3    Bax, A.4
  • 43
    • 0031021456 scopus 로고    scopus 로고
    • A computational approach for modeling nucleic acid hairpin structures
    • Tung CS. 1997. A computational approach for modeling nucleic acid hairpin structures. Biophys J 72:876-885.
    • (1997) Biophys J , vol.72 , pp. 876-885
    • Tung, C.S.1
  • 44
    • 0027384569 scopus 로고
    • Structure and energetics of a non-proline cis-peptidyl linkage in a proline-202 alanine carbonic anhydrase II variant
    • Tweedy NB, Nair SK, Paterno SA, Fierke CA, Christianson DW. 1993. Structure and energetics of a non-proline cis-peptidyl linkage in a proline-202 alanine carbonic anhydrase II variant. Biochemistry 41:10944-10949.
    • (1993) Biochemistry , vol.41 , pp. 10944-10949
    • Tweedy, N.B.1    Nair, S.K.2    Paterno, S.A.3    Fierke, C.A.4    Christianson, D.W.5
  • 45
    • 0029888845 scopus 로고    scopus 로고
    • The rate-limiting step in the folding of the cis-Pro167Thr mutant of TEM-1-lactamaseis the trans to cis isomerization of a non-proline peptide bond
    • Vanhove M, Raquet X, Palzkill T, Pain RH, Frere JM. 1996. The rate-limiting step in the folding of the cis-Pro167Thr mutant of TEM-1-lactamaseis the trans to cis isomerization of a non-proline peptide bond. Proteins Struct Funct Genet 25:104-111.
    • (1996) Proteins Struct Funct Genet , vol.25 , pp. 104-111
    • Vanhove, M.1    Raquet, X.2    Palzkill, T.3    Pain, R.H.4    Frere, J.M.5
  • 47
    • 0031010618 scopus 로고    scopus 로고
    • Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease
    • Walkenhorst WF, Green SM, Roder H. 1997. Kinetic evidence for folding and unfolding intermediates in staphylococcal nuclease. Biochemistry 36:5795-5805.
    • (1997) Biochemistry , vol.36 , pp. 5795-5805
    • Walkenhorst, W.F.1    Green, S.M.2    Roder, H.3
  • 49
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart DS, Sykes BD, Richards FM. 1991. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J Mol Biol 222:311-333.
    • (1991) J Mol Biol , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 51
    • 0021764802 scopus 로고
    • Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances
    • Wüthrich K, Billete M, Braun W. 1984. Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances. J Mol Biol 180:715-740.
    • (1984) J Mol Biol , vol.180 , pp. 715-740
    • Wüthrich, K.1    Billete, M.2    Braun, W.3


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