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Volumn 3, Issue 9, 1996, Pages 782-787

Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE; HYDROGEN; RIBONUCLEASE H;

EID: 0029746061     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0996-782     Document Type: Article
Times cited : (331)

References (29)
  • 1
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim, P.S. & Baldwin, R.L Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59, 631-660 (1990).
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 2
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima, K. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins 6, 87-103 (1989).
    • (1989) Proteins , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 3
    • 0025212107 scopus 로고
    • Evidence for a molten globule state as a general intermediate in protein folding
    • Ptitsyn, O.B., Pain, R.H., Semisotnov, G.V., Zerovnik, E. & Razgulyaev, O.I. Evidence for a molten globule state as a general intermediate in protein folding. Febs. Lett. 262, 20-24 (1990).
    • (1990) Febs. Lett. , vol.262 , pp. 20-24
    • Ptitsyn, O.B.1    Pain, R.H.2    Semisotnov, G.V.3    Zerovnik, E.4    Razgulyaev, O.I.5
  • 4
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings, P.A. & Wright, P.E. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 262, 892-896 (1993).
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 5
    • 0028466243 scopus 로고
    • Protein folding. Solid evidence for molten globules
    • Dobson, C.M. Protein folding. Solid evidence for molten globules. Curr. Biol. 4, 636-40 (1994).
    • (1994) Curr. Biol. , vol.4 , pp. 636-640
    • Dobson, C.M.1
  • 6
    • 0027730340 scopus 로고
    • Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A
    • Mayo, S.L & Baldwin, R.L Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A. Science 262, 873-876 (1993).
    • (1993) Science , vol.262 , pp. 873-876
    • Mayo, S.L.1    Baldwin, R.L.2
  • 7
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai, Y., Sosnick, T.R, Mayne, L. & Englander, S.W. Protein folding intermediates: native-state hydrogen exchange. Science 269, 192-197 (1995).
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 8
    • 0025162621 scopus 로고
    • Three-dimensional structure of ribonuclease H from E. coli
    • Katayanagi, K. et al. Three-dimensional structure of ribonuclease H from E. coli. Nature 347, 306-309 (1990).
    • (1990) Nature , vol.347 , pp. 306-309
    • Katayanagi, K.1
  • 9
    • 0029598779 scopus 로고
    • Folding pathway of Escherichia coli ribonuclease HI: A circular dichroism, fluorescence, and NMR study
    • Yamasaki, K., Ogasahara, K., Yutani, K, Oobatake, M. & Kanaya, S. Folding pathway of Escherichia coli ribonuclease HI: a circular dichroism, fluorescence, and NMR study. Biochemistry 34, 16552-16562 (1995).
    • (1995) Biochemistry , vol.34 , pp. 16552-16562
    • Yamasaki, K.1    Ogasahara, K.2    Yutani, K.3    Oobatake, M.4    Kanaya, S.5
  • 10
    • 16044372028 scopus 로고    scopus 로고
    • Structure of the acid state of E.coli ribonuclease HI
    • in the press
    • Dabora, J.M., Pelton, J.G. & Marqusee, S. Structure of the acid state of E.coli ribonuclease HI. Biochemistry, in the press.
    • Biochemistry
    • Dabora, J.M.1    Pelton, J.G.2    Marqusee, S.3
  • 11
    • 44949286953 scopus 로고
    • Comparison of techniques for H-1-detected heteronuclear H-1-N-15 spectroscopy
    • Norwood, T.J., Boyd, J., Heritage, J., Soffe, N. & Campbell, I.D. Comparison of techniques for H-1-detected heteronuclear H-1-N-15 spectroscopy.J. Magn. Reson. 87, 488-501 (1990).
    • (1990) J. Magn. Reson. , vol.87 , pp. 488-501
    • Norwood, T.J.1    Boyd, J.2    Heritage, J.3    Soffe, N.4    Campbell, I.D.5
  • 12
    • 45149138663 scopus 로고
    • Comparison of different modes of 2-dimensional reverse-correlation NMR for the study of proteins
    • Bax, A., Ikura, M., Kay, L.E., Torchia, D.A. & Tschudin, R. Comparison of different modes of 2-dimensional reverse-correlation NMR for the study of proteins.J. Magn. Reson. 86, 304-318 (1990).
    • (1990) J. Magn. Reson. , vol.86 , pp. 304-318
    • Bax, A.1    Ikura, M.2    Kay, L.E.3    Torchia, D.A.4    Tschudin, R.5
  • 13
    • 0027787894 scopus 로고
    • 2O in protein NMR. Application to sensitivity enhancement and NOE measurements
    • 2O in protein NMR. Application to sensitivity enhancement and NOE measurements. J. Am. Chem. Soc. 115, 12593-12594 (1993).
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12593-12594
    • Grzesieki, S.1    Bax, A.2
  • 14
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • Hvidt, A. & Nielsen, S.O. Hydrogen exchange in proteins. Adv. Prot. Chem. 21, 288-386 (1966).
    • (1966) Adv. Prot. Chem. , vol.21 , pp. 288-386
    • Hvidt, A.1    Nielsen, S.O.2
  • 15
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • Englander, S.W. & Kallenbach, N.R. Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q. Rev. Biophys. 16, 521-655 (1983).
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 16
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai, Y., Milne, J.S., Mayne, L & Englander, S.W. Primary structure effects on peptide group hydrogen exchange. Proteins 17, 75-86 (1993).
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 17
  • 18
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea, E.K, Klemm, J.D., Kim, P.S. S Alber, T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254, 539-544 (1991).
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.S.3    Alber, T.4
  • 19
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
    • Mandel, A.M., Akke, M. & Palmer, A.3. Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme. J. Mol. Biol. 246, 144-63 (1995).
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer III, A.3
  • 20
    • 0029031765 scopus 로고
    • Characterization of the internal motions of Escherichia coli ribonuclease HI by a combination of 15N-NMR relaxation analysis and molecular dynamics simulation: Examination of dynamic models
    • Yamasaki, K., Saito, M., Oobatake, M. & Kanaya, S. Characterization of the internal motions of Escherichia coli ribonuclease HI by a combination of 15N-NMR relaxation analysis and molecular dynamics simulation: examination of dynamic models. Biochemistry 34, 6587-601 (1995).
    • (1995) Biochemistry , vol.34 , pp. 6587-6601
    • Yamasaki, K.1    Saito, M.2    Oobatake, M.3    Kanaya, S.4
  • 21
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein folding
    • Myer, J.K., Pace, C.N. & Scholtz, J.M. Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein folding. Prot. Sci. 4, 2138-2148 (1995).
    • (1995) Prot. Sci. , vol.4 , pp. 2138-2148
    • Myer, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 22
    • 0028061986 scopus 로고
    • Equilibrium unfolding of Escherichia coli ribonuclease H: Characterization of a partially folded state
    • Dabora, J.M. & Marqusee, S. Equilibrium unfolding of Escherichia coli ribonuclease H: characterization of a partially folded state. Prot. Sci. 3, 1401-1408 (1994).
    • (1994) Prot. Sci. , vol.3 , pp. 1401-1408
    • Dabora, J.M.1    Marqusee, S.2
  • 23
    • 0027313673 scopus 로고
    • Pathways of protein folding
    • Matthews, C.R. Pathways of protein folding. Ann. Rev. Biochem. 62, 653-683 (1993).
    • (1993) Ann. Rev. Biochem. , vol.62 , pp. 653-683
    • Matthews, C.R.1
  • 24
    • 0027384196 scopus 로고
    • Hydrogen exchange in unligated and ligated staphylococcal nuclease
    • Loh, S.L., Prehoda, K.E., Wang, J. & Markley, J.L Hydrogen exchange in unligated and ligated staphylococcal nuclease. Biochemistry 32, 11022-11028 (1993).
    • (1993) Biochemistry , vol.32 , pp. 11022-11028
    • Loh, S.L.1    Prehoda, K.E.2    Wang, J.3    Markley, J.L.4
  • 25
    • 0028236501 scopus 로고
    • Hydrogen-deuterium exchange in the free and immunoglobulin G-bound protein G B-domain
    • Orban, J., Alexander, P. & Bryan, P. Hydrogen-deuterium exchange in the free and immunoglobulin G-bound protein G B-domain, Biochemistry 33, 5702-5710 (1994).
    • (1994) Biochemistry , vol.33 , pp. 5702-5710
    • Orban, J.1    Alexander, P.2    Bryan, P.3
  • 26
    • 0029153539 scopus 로고
    • Relationship between equilibrium amide proton exchange behavior and the folding pathway of barnase
    • Perret, S., Clark, J., Hounslow, A.M. & Fersht. A.R. Relationship between equilibrium amide proton exchange behavior and the folding pathway of barnase. Biochemistry 34, 9288-9298 (1995).
    • (1995) Biochemistry , vol.34 , pp. 9288-9298
    • Perret, S.1    Clark, J.2    Hounslow, A.M.3    Fersht, A.R.4
  • 27
    • 0030047378 scopus 로고    scopus 로고
    • Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain
    • Swint-Kruse, L. & Robertson, A.D. Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain. Biochemistry 35, 171-180 (1996).
    • (1996) Biochemistry , vol.35 , pp. 171-180
    • Swint-Kruse, L.1    Robertson, A.D.2
  • 29
    • 0029931004 scopus 로고    scopus 로고
    • IVE(Image Visualization Environment): A software platform for all three-dimensional microscopy applications
    • Chen, H, Hughes, D.D., Chan, T.-A., Sedat, J.W. & Agard, D.A. IVE(Image Visualization Environment): A software platform for all three-dimensional microscopy applications. J. Struct. Biol. 116, 56-60 (1996).
    • (1996) J. Struct. Biol. , vol.116 , pp. 56-60
    • Chen, H.1    Hughes, D.D.2    Chan, T.-A.3    Sedat, J.W.4    Agard, D.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.