메뉴 건너뛰기




Volumn 9, Issue 1, 2000, Pages 145-157

Apoflavodoxin (un)folding followed at the residue level by NMR

Author keywords

Apoflavodoxin; Cooperative and noncooperative unfolding; Equilibrium (un)folding; Guanidinium hydrochloride; Molten globule; NMR; Protein aggregation; Residue level

Indexed keywords

FLAVODOXIN;

EID: 0033980811     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.1.145     Document Type: Article
Times cited : (39)

References (40)
  • 1
    • 0015495465 scopus 로고
    • Flavine-protein interactions in flavoenzymes. Temperature-jump and stopped-flow studies of flavine analog binding to the apoprotein of Azotobacter flavodoxin
    • Barman BG, Tollin G. 1972. Flavine-protein interactions in flavoenzymes. Temperature-jump and stopped-flow studies of flavine analog binding to the apoprotein of Azotobacter flavodoxin. Biochemistry 11:4746-4754.
    • (1972) Biochemistry , vol.11 , pp. 4746-4754
    • Barman, B.G.1    Tollin, G.2
  • 3
    • 0030983386 scopus 로고    scopus 로고
    • Population statistics of protein structures. Lessons from structural classifications
    • Brenner SE. 1997. Population statistics of protein structures. Lessons from structural classifications. Curr Opin Struct Biol 7:369-376.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 369-376
    • Brenner, S.E.1
  • 4
    • 84985653913 scopus 로고
    • 1H-NMR titration shifts for studies of polypeptide conformation
    • 1H-NMR titration shifts for studies of polypeptide conformation. Biopolymers 18:299-311.
    • (1979) Biopolymers , vol.18 , pp. 299-311
    • Bundi, A.1    Wüthrich, K.2
  • 5
    • 44949289665 scopus 로고
    • Sensitivity improvement in isotropic mixing (TOCSY) experiments
    • Cavanagh J, Rance M. 1990. Sensitivity improvement in isotropic mixing (TOCSY) experiments. J Magn Reson 88:72-85.
    • (1990) J Magn Reson , vol.88 , pp. 72-85
    • Cavanagh, J.1    Rance, M.2
  • 6
    • 0032842870 scopus 로고    scopus 로고
    • The fundamentals of protein folding: Bringing together theory and experiment
    • Dobson C. Karplus M. 1999. The fundamentals of protein folding: Bringing together theory and experiment. Curr Opin Struct Biol 9:92-101.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 92-101
    • Dobson, C.1    Karplus, M.2
  • 7
    • 0015210981 scopus 로고
    • Chemical and physical characterization of the Shethna flavoprotein and apoprotein and kinetics and thermodynamics of flavin analog binding to the apoprotein
    • Edmondson DE, Tollin G. 1971. Chemical and physical characterization of the Shethna flavoprotein and apoprotein and kinetics and thermodynamics of flavin analog binding to the apoprotein. Biochemistry 10:124-132.
    • (1971) Biochemistry , vol.10 , pp. 124-132
    • Edmondson, D.E.1    Tollin, G.2
  • 8
    • 0027384577 scopus 로고
    • Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2
    • Jackson SE, Moracci M, elMasry N, Johnson CM, Fersht AR. 1993. Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2. Biochemistry 32:11259-11269.
    • (1993) Biochemistry , vol.32 , pp. 11259-11269
    • Jackson, S.E.1    Moracci, M.2    ElMasry, N.3    Johnson, C.M.4    Fersht, A.R.5
  • 9
    • 0014010861 scopus 로고
    • Viscosity and density of aqueous solutions of urea and guanidinium hydrochloride
    • Kawahara K, Tanford C. 1966. Viscosity and density of aqueous solutions of urea and guanidinium hydrochloride. J Biol Chem 241:3228-3232.
    • (1966) J Biol Chem , vol.241 , pp. 3228-3232
    • Kawahara, K.1    Tanford, C.2
  • 10
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced hetero-nuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay LE, Keifer P, Saarinen T. 1992. Pure absorption gradient enhanced hetero-nuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 114:10663-10665.
    • (1992) J Am Chem Soc , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 11
    • 0026244229 scopus 로고
    • MOLSCRlPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRlPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 12
    • 0000340142 scopus 로고
    • Improving the signal-to-noise ratio of NMR signals by reduction of inductive losses
    • Kugel H. 1991. Improving the signal-to-noise ratio of NMR signals by reduction of inductive losses. J Magn Reson 91:179-185.
    • (1991) J Magn Reson , vol.91 , pp. 179-185
    • Kugel, H.1
  • 13
    • 0000323018 scopus 로고
    • General properties of flavodoxins
    • Müller F, ed. Boca Raton, Florida: CRC Press
    • Mayhew SG, Tollin G. 1992. General properties of flavodoxins. In: Müller F, ed. Chemistry and biochemistry of flavoenzymes, vol. 3, Boca Raton, Florida: CRC Press. pp 389-426.
    • (1992) Chemistry and Biochemistry of Flavoenzymes , vol.3 , pp. 389-426
    • Mayhew, S.G.1    Tollin, G.2
  • 14
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace CN. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 131:266-280.
    • (1986) Methods Enzymol , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 15
    • 0002343673 scopus 로고
    • Measuring the conformational stability of a protein
    • Creighton TE, eds. Oxford, UK: IRL Press
    • Pace CN, Shirley BA, Thomson JA. 1989. Measuring the conformational stability of a protein. In: Creighton TE, eds. Protein structure: A practical approach. Oxford, UK: IRL Press. pp 311-330.
    • (1989) Protein Structure: A Practical Approach , pp. 311-330
    • Pace, C.N.1    Shirley, B.A.2    Thomson, J.A.3
  • 16
    • 44949276869 scopus 로고
    • Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy
    • Palmer AG III, Cavanagh J, Wright PE, Rance M. 1991. Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy. J Magn Reson 93:151-170.
    • (1991) J Magn Reson , vol.93 , pp. 151-170
    • Palmer A.G. III1    Cavanagh, J.2    Wright, P.E.3    Rance, M.4
  • 17
    • 0001078545 scopus 로고    scopus 로고
    • The effects of guanidine hydrochloride on the "random coil" conformations and NMR chemical shifts of the peptide series GGXGG
    • Plaxco KW, Morton CJ, Grimshaw SB, Jones JA, Pitkeathly M, Campbell ID, Dobson CM. 1997. The effects of guanidine hydrochloride on the "random coil" conformations and NMR chemical shifts of the peptide series GGXGG. J Biom NMR 10:221-230.
    • (1997) J Biom NMR , vol.10 , pp. 221-230
    • Plaxco, K.W.1    Morton, C.J.2    Grimshaw, S.B.3    Jones, J.A.4    Pitkeathly, M.5    Campbell, I.D.6    Dobson, C.M.7
  • 18
    • 0002940127 scopus 로고
    • The molten globule state
    • Creighton TE, ed. New York: W.H. Freeman and Company
    • Ptitsyn OB. 1992. The molten globule state. In: Creighton TE, ed. Protein folding. New York: W.H. Freeman and Company, pp 243-300.
    • (1992) Protein Folding , pp. 243-300
    • Ptitsyn, O.B.1
  • 19
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn OB. 1995. Molten globule and protein folding. Adv Protein Chem 47:83-229.
    • (1995) Adv Protein Chem , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 20
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro MM, Bolen DW. 1988. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry 27:8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 21
    • 0000722070 scopus 로고
    • Spectral methods of characterizing protein conformation and conformational changes
    • Creighton TE, ed. Oxford, UK: IRL Press
    • Schmid FX. 1989. Spectral methods of characterizing protein conformation and conformational changes. In: Creighton TE, ed. Protein structure: A practical approach. Oxford, UK: IRL Press. pp 251-285.
    • (1989) Protein Structure: A Practical Approach , pp. 251-285
    • Schmid, F.X.1
  • 22
    • 0001340839 scopus 로고
    • Kinetics of unfolding and refolding of single-domain proteins
    • Creighton TE, ed. New York: W.H. Freeman and Company
    • Schmid FX. 1992. Kinetics of unfolding and refolding of single-domain proteins. In: Creighton TE, ed. Protein folding. New York: W.H. Freeman and Company. pp 197-241.
    • (1992) Protein Folding , pp. 197-241
    • Schmid, F.X.1
  • 23
    • 0030768045 scopus 로고    scopus 로고
    • A residue specific NMR view of the non cooperative unfolding of a molten globule
    • Schulman BA, Kim PS, Dobson CM, Redfield C. 1997. A residue specific NMR view of the non cooperative unfolding of a molten globule. Nat Struct Biol 4:630-634.
    • (1997) Nat Struct Biol , vol.4 , pp. 630-634
    • Schulman, B.A.1    Kim, P.S.2    Dobson, C.M.3    Redfield, C.4
  • 24
    • 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
  • 25
    • 0030060586 scopus 로고    scopus 로고
    • Redox properties of wild-type, cys69ala, and cys69ser azotobacter vinelandii flavodoxin II as measured by cyclic voltammetry and EPR spectroscopy
    • Steensma E, Heering HA, Hagen WR, van Mierlo CPM. 1996. Redox properties of wild-type, Cys69Ala, and Cys69Ser Azotobacter vinelandii flavodoxin II as measured by cyclic voltammetry and EPR spectroscopy. Eur J Biochem 235:167-172.
    • (1996) Eur J Biochem , vol.235 , pp. 167-172
    • Steensma, E.1    Heering, H.A.2    Hagen, W.R.3    Van Mierlo, C.P.M.4
  • 26
    • 0031952923 scopus 로고    scopus 로고
    • Apparent local stability of the secondary structure of azobacter vinelandi holoflavodoxin II as probed by hydrogen exchange: Implications for redox potential regulation and flavodoxin folding
    • Steensma E, Nijman MJM, Bollen YJM, de Jager PA, van den Berg WAM, van Dongen WMAM, van Mierlo CPM. 1998. Apparent local stability of the secondary structure of Azobacter vinelandi holoflavodoxin II as probed by hydrogen exchange: Implications for redox potential regulation and flavodoxin folding. Protein Sci 7:306-317.
    • (1998) Protein Sci , vol.7 , pp. 306-317
    • Steensma, E.1    Nijman, M.J.M.2    Bollen, Y.J.M.3    De Jager, P.A.4    Van Den Berg, W.A.M.5    Van Dongen, W.M.A.M.6    Van Mierlo, C.P.M.7
  • 27
    • 0032566696 scopus 로고    scopus 로고
    • Structural characterisation of apoflavodoxin shows that the location of the most stable nucleus differs among proteins with a flavodoxin-like topology
    • Steensma E, van Mierlo CPM. 1998. Structural characterisation of apoflavodoxin shows that the location of the most stable nucleus differs among proteins with a flavodoxin-like topology. J Mol Biol 282:653-666.
    • (1998) J Mol Biol , vol.282 , pp. 653-666
    • Steensma, E.1    Van Mierlo, C.P.M.2
  • 28
    • 0017382179 scopus 로고
    • Complete amino acid sequence of azotoflavin, a flavodoxin from azotobacter vinelandi
    • Tanaka M, Haniu M, Yasunobu KT, Yoch DC. 1977. Complete amino acid sequence of azotoflavin, a flavodoxin from Azotobacter vinelandi. Biochemistry 16:3525-3537.
    • (1977) Biochemistry , vol.16 , pp. 3525-3537
    • Tanaka, M.1    Haniu, M.2    Yasunobu, K.T.3    Yoch, D.C.4
  • 30
    • 0026736195 scopus 로고
    • The partially folded conformation of the Cys30-Cys51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor
    • van Mierlo CPM, Darby NJ, Creighton TE. 1992a. The partially folded conformation of the Cys30-Cys51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor. Proc Natl Acad Sci USA 89:6775-6779.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6775-6779
    • Van Mierlo, C.P.M.1    Darby, N.J.2    Creighton, T.E.3
  • 33
    • 0025193216 scopus 로고
    • 1H NMR study on Megasphaera elsdenii flavodoxin in the reduced state: Sequential assignments
    • 1H NMR study on Megasphaera elsdenii flavodoxin in the reduced state: Sequential assignments. Eur J Biochem 187:521-541.
    • (1990) Eur J Biochem , vol.187 , pp. 521-541
    • Van Mierlo, C.P.M.1    Vervoort, J.2    Müller, F.3    Bacher, A.4
  • 34
    • 0032868613 scopus 로고    scopus 로고
    • Stabilisation centres differ between structurally homologous proteins as shown by NMR spectroscopy
    • van Mierlo CPM, Steensma E. 1999. Stabilisation centres differ between structurally homologous proteins as shown by NMR spectroscopy. J Mol Cat B: Enzymatic 7:147-156.
    • (1999) J Mol Cat B: Enzymatic , vol.7 , pp. 147-156
    • Van Mierlo, C.P.M.1    Steensma, E.2
  • 35
    • 0342795995 scopus 로고    scopus 로고
    • NMR studies on apoflavodoxin II from azotobacter vinelandii
    • Stevenson KJ, Massey V, Williams CH Jr, eds. Calgary, Canada: University of Calgary Press
    • van Mierlo CPM, Steensma E, van Dongen WMAM, van Berkel WJH. 1997. NMR studies on apoflavodoxin II from Azotobacter vinelandii. In: Stevenson KJ, Massey V, Williams CH Jr, eds. Flavins and flavoproteins 1996. Calgary, Canada: University of Calgary Press. pp 449-452.
    • (1997) Flavins and Flavoproteins 1996. , pp. 449-452
    • Van Mierlo, C.P.M.1    Steensma, E.2    Van Dongen, W.M.A.M.3    Van Berkel, W.J.H.4
  • 36
    • 0031792027 scopus 로고    scopus 로고
    • The equilibrium unfolding of azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate
    • van Mierlo CPM, van Dongen WMAM, Vergeldt F, van Berkel WJH, Steensma E. 1998. The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate. Protein Sci 7:2331-2344.
    • (1998) Protein Sci , vol.7 , pp. 2331-2344
    • Van Mierlo Cpm1    Van Dongen, W.2    Vergeldt, F.3    Van Berkel, W.J.H.4    Steensma, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.