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Volumn 5, Issue 9, 1996, Pages 1898-1906

A dynamic bundle of four adjacent hydrophobic segments in the denatured state of staphylococcal nuclease

Author keywords

folding intermediates; hydrogen exchange; hydrophobic interactions; non native structure

Indexed keywords

NUCLEASE;

EID: 0029786948     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050916     Document Type: Article
Times cited : (47)

References (22)
  • 1
    • 0028274250 scopus 로고
    • Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: A heteronuclear NMR study
    • Alexandrescu AT, Abeygunawardana C, Shortle D. 1994. Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: A heteronuclear NMR study. Biochemistry 33:1063-1072.
    • (1994) Biochemistry , vol.33 , pp. 1063-1072
    • Alexandrescu, A.T.1    Abeygunawardana, C.2    Shortle, D.3
  • 2
    • 0027988297 scopus 로고
    • Backbone dynamics of a highly disordered 131-residue fragment of staphylococcal nuclease
    • Alexandrescu AT, Shortle D. 1994. Backbone dynamics of a highly disordered 131-residue fragment of staphylococcal nuclease. J Mol Biol 242:527-546.
    • (1994) J Mol Biol , vol.242 , pp. 527-546
    • Alexandrescu, A.T.1    Shortle, D.2
  • 3
    • 0028857598 scopus 로고
    • Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements
    • Altieri AS, Hinton DP, Byrd RA. 1995. Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements. J Am Chem Soc 117:7566-7567.
    • (1995) J Am Chem Soc , vol.117 , pp. 7566-7567
    • Altieri, A.S.1    Hinton, D.P.2    Byrd, R.A.3
  • 6
    • 0022423920 scopus 로고
    • Theory of the folding and stability of globular proteins
    • Dill KA. 1985. Theory of the folding and stability of globular proteins. Biochemistry 24:1501-1509.
    • (1985) Biochemistry , vol.24 , pp. 1501-1509
    • Dill, K.A.1
  • 7
    • 0026653655 scopus 로고
    • Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR
    • Englander SW, Mayne L. 1992. Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR. Annu Rev Biophys Biomol Struct 21:243-265
    • (1992) Annu Rev Biophys Biomol Struct , vol.21 , pp. 243-265
    • Englander, S.W.1    Mayne, L.2
  • 8
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear quantum correlation spectroscopy with improved sensitivity
    • Kay LE, Keifer P, Saarinen T. 1992. Pure absorption gradient enhanced heteronuclear 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
  • 9
    • 0027384196 scopus 로고
    • Hydrogen exchange in unligated and ligated staphylococcal nuclease
    • Loh SN, Prehoda KE, Wang J, Markley JL. 1993. Hydrogen exchange in unligated and ligated staphylococcal nuclease. Biochemistry 32:11022-11028
    • (1993) Biochemistry , vol.32 , pp. 11022-11028
    • Loh, S.N.1    Prehoda, K.E.2    Wang, J.3    Markley, J.L.4
  • 10
  • 11
    • 0029338320 scopus 로고
    • Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation
    • Mori S, Abeygunawardana C, Johnson MO, van Zijl PCM 1995. Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation. J Magn Reson B 108:94-98.
    • (1995) J Magn Reson B , vol.108 , pp. 94-98
    • Mori, S.1    Abeygunawardana, C.2    Johnson, M.O.3    Van Zijl, P.C.M.4
  • 12
    • 0029685015 scopus 로고    scopus 로고
    • Water exchange filter with improved sensitivity (WEXII) to study solvent-exchangeable protons: Application to a zinc finger peptide
    • Forthcoming
    • Mori S, Abeygunawardana C, van Zijl PCM, Berg JM 1996. Water exchange filter with improved sensitivity (WEXII) to study solvent-exchangeable protons: Application to a zinc finger peptide. J Magn Reson B. Forthcoming.
    • (1996) J Magn Reson B
    • Mori, S.1    Abeygunawardana, C.2    Van Zijl, P.C.M.3    Berg, J.M.4
  • 13
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity
    • Muhandiram DR, Kay LE. 1994. Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity. J Magn Reson B 103:203-216.
    • (1994) J Magn Reson B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 14
    • 0029961647 scopus 로고    scopus 로고
    • Structural analysis of non-native states of proteins by NMR methods
    • Shortle D. 1996. Structural analysis of non-native states of proteins by NMR methods. Curr Opin Struct Biol 6:24-30.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 24-30
    • Shortle, D.1
  • 15
    • 0029900442 scopus 로고    scopus 로고
    • Protein folding for realists: A timeless phenomenon
    • Shortle D, Wang Y, Gillespie J, Wrabl JO 1996. Protein folding for realists: A timeless phenomenon. Protein Sci 5:991-1000.
    • (1996) Protein Sci , vol.5 , pp. 991-1000
    • Shortle, D.1    Wang, Y.2    Gillespie, J.3    Wrabl, J.O.4
  • 16
    • 0017678936 scopus 로고
    • Cleavage at cysteine after cyanylation
    • Stark GR. 1977. Cleavage at cysteine after cyanylation. Methods Enzymol 47:129-132.
    • (1977) Methods Enzymol , vol.47 , pp. 129-132
    • Stark, G.R.1
  • 17
    • 0024379348 scopus 로고
    • Staphylococcal nuclease: Sequential assignment and solution structure
    • Torchia DA, Sparks SW, Bax A 1989. Staphylococcal nuclease: Sequential assignment and solution structure. Biochemistry 28:5509-5524.
    • (1989) Biochemistry , vol.28 , pp. 5509-5524
    • Torchia, D.A.1    Sparks, S.W.2    Bax, A.3
  • 18
    • 0026584349 scopus 로고
    • 15N chemical shift assignments for the unligated enzyme and analysis of chemical shift changes that accompany formation of the nuclease-thymidine 3′,5′-bisphosphate-calcium ternary complex
    • 15N chemical shift assignments for the unligated enzyme and analysis of chemical shift changes that accompany formation of the nuclease-thymidine 3′,5′-bisphosphate-calcium ternary complex. Biochemistry 31:921-936.
    • (1992) Biochemistry , vol.31 , pp. 921-936
    • Wang, J.1    Hinck, A.P.2    Loh, S.N.3    Lemaster, D.M.4    Markley, J.L.5
  • 19
    • 0029653886 scopus 로고
    • Initial studies of the equilibrium folding pathway of staphylococcal nuclease
    • Wang Y, Alexandrescu AT, Shortle D. 1995 Initial studies of the equilibrium folding pathway of staphylococcal nuclease. Phil Trans R Soc Lond B 348:27-34.
    • (1995) Phil Trans R Soc Lond B , vol.348 , pp. 27-34
    • Wang, Y.1    Alexandrescu, A.T.2    Shortle, D.3
  • 20
    • 0028856228 scopus 로고
    • The equilibrium folding pathway of staphylococcal nuclease: Identification of the most stable chain-chain interactions by NMR and CD spectroscopy
    • Wang Y, Shortle D. 1995. The equilibrium folding pathway of staphylococcal nuclease: Identification of the most stable chain-chain interactions by NMR and CD spectroscopy. Biochemistry 34:15895-15905.
    • (1995) Biochemistry , vol.34 , pp. 15895-15905
    • Wang, Y.1    Shortle, D.2
  • 21
    • 0028673594 scopus 로고
    • Chemical shifts as a tool for structure determination
    • Wishart DS, Sykes BD. 1994. Chemical shifts as a tool for structure determination Method Enzymol 239:363-392
    • (1994) Method Enzymol , vol.239 , pp. 363-392
    • Wishart, D.S.1    Sykes, B.D.2
  • 22
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.