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Volumn 16, Issue 9, 2007, Pages 1946-1956

Branching in the sequential folding pathway of cytochrome c

Author keywords

Cytochrome c; Foldon; Partially unfolded form; Predetermined pathway; Protein folding; Sequential stabilization

Indexed keywords

CYTOCHROME C; HYDROGEN;

EID: 34548406580     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.072922307     Document Type: Article
Times cited : (29)

References (69)
  • 1
    • 0029865938 scopus 로고    scopus 로고
    • Future directions in folding: The multi-state nature of protein structure
    • Bai, Y. and Englander, S.W. 1996. Future directions in folding: The multi-state nature of protein structure. Proteins 24: 145-151.
    • (1996) Proteins , vol.24 , pp. 145-151
    • Bai, Y.1    Englander, S.W.2
  • 2
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai, Y., Milne, J.S., Mayne, L., and Englander, S.W. 1993. Primary structure effects on peptide group hydrogen exchange. Proteins 17: 75-86.
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 3
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai, Y., Sosnick, T.R., Mayne, L., and Englander, S.W. 1995. Protein folding intermediates: Native-state hydrogen exchange. Science 269: 192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 4
    • 0029249945 scopus 로고
    • The nature of protein folding pathways: The classical versus the new view
    • Baldwin, R.L. 1995. The nature of protein folding pathways: The classical versus the new view. J. Biomol. NMR 5: 103-109.
    • (1995) J. Biomol. NMR , vol.5 , pp. 103-109
    • Baldwin, R.L.1
  • 5
    • 0033592403 scopus 로고    scopus 로고
    • A salt-induced kinetic intermediate is on a new parallel pathway of lysozyme folding
    • Bieri, O., Wildegger, G., Bachmann, A., Wagner, C., and Kiefhaber, T. 1999. A salt-induced kinetic intermediate is on a new parallel pathway of lysozyme folding. Biochemistry 38: 12460-12470.
    • (1999) Biochemistry , vol.38 , pp. 12460-12470
    • Bieri, O.1    Wildegger, G.2    Bachmann, A.3    Wagner, C.4    Kiefhaber, T.5
  • 6
    • 0034581629 scopus 로고    scopus 로고
    • Barriers in protein folding reactions
    • Bilsel, O. and Matthews, C.R. 2000. Barriers in protein folding reactions. Adv. Protein Chem. 53: 153-207.
    • (2000) Adv. Protein Chem , vol.53 , pp. 153-207
    • Bilsel, O.1    Matthews, C.R.2
  • 7
    • 0032053619 scopus 로고    scopus 로고
    • Simulations of protein folding and unfolding
    • Brooks III, C.L. 1998. Simulations of protein folding and unfolding. Curr. Opin. Struct. Biol. 8: 222-226.
    • (1998) Curr. Opin. Struct. Biol , vol.8 , pp. 222-226
    • Brooks III, C.L.1
  • 8
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson, J.D., Onuchic, J.N., Socci, N.D., and Wolynes, P.G. 1995. Funnels, pathways, and the energy landscape of protein folding: A synthesis. Proteins 21: 167-195.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 9
    • 0025007598 scopus 로고
    • High-resolution three-dimensional structure of horse heart cytochrome c
    • Bushnell, G.W., Louie, G.V., and Brayer, G.D. 1990. High-resolution three-dimensional structure of horse heart cytochrome c. J. Mol. Biol. 214: 585-595.
    • (1990) J. Mol. Biol , vol.214 , pp. 585-595
    • Bushnell, G.W.1    Louie, G.V.2    Brayer, G.D.3
  • 10
    • 25444512161 scopus 로고    scopus 로고
    • Direct observation of the three-state folding of a single protein molecule
    • Cecconi, C., Shank, E.A., Bustamante, C., and Marqusee, S. 2005. Direct observation of the three-state folding of a single protein molecule. Science 309: 2057-2060.
    • (2005) Science , vol.309 , pp. 2057-2060
    • Cecconi, C.1    Shank, E.A.2    Bustamante, C.3    Marqusee, S.4
  • 11
    • 0034581325 scopus 로고    scopus 로고
    • Comparison of equilibrium and kinetic approaches for determining protein folding mechanisms
    • Chamberlain, A.K. and Marqusee, S. 2000. Comparison of equilibrium and kinetic approaches for determining protein folding mechanisms. Adv. Protein Chem. 53: 283-328.
    • (2000) Adv. Protein Chem , vol.53 , pp. 283-328
    • Chamberlain, A.K.1    Marqusee, S.2
  • 12
    • 0029746061 scopus 로고    scopus 로고
    • Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH
    • Chamberlain, A.K., Handel, T.M., and Marqusee, S. 1996. Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. Nat. Struct. Biol. 3: 782-787.
    • (1996) Nat. Struct. Biol , vol.3 , pp. 782-787
    • Chamberlain, A.K.1    Handel, T.M.2    Marqusee, S.3
  • 14
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • Chi, E.Y., Krishnan, S., Randolph, T.W., and Carpenter, J.F. 2003. Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation. Pharm. Res. 20: 1325-1336.
    • (2003) Pharm. Res , vol.20 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 15
    • 0037172787 scopus 로고    scopus 로고
    • Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein
    • Chu, R., Pei, W., Takei, J., and Bai, Y. 2002. Relationship between the native-state hydrogen exchange and folding pathways of a four-helix bundle protein. Biochemistry 41: 7998-8003.
    • (2002) Biochemistry , vol.41 , pp. 7998-8003
    • Chu, R.1    Pei, W.2    Takei, J.3    Bai, Y.4
  • 16
    • 0016273628 scopus 로고
    • Nuclear magnetic resonance titration curves of histidine ring protons. V. Comparative study of cytochrome c from three species and the assignment of individual proton resonances
    • Cohen, J.S. and Hayes, M.B. 1974. Nuclear magnetic resonance titration curves of histidine ring protons. V. Comparative study of cytochrome c from three species and the assignment of individual proton resonances. J. Biol. Chem. 249: 5472-5477.
    • (1974) J. Biol. Chem , vol.249 , pp. 5472-5477
    • Cohen, J.S.1    Hayes, M.B.2
  • 17
    • 0028847055 scopus 로고
    • Entropic stabilization of cytochrome c upon reduction
    • Cohen, D.S. and Pielak, G.J. 1995. Entropic stabilization of cytochrome c upon reduction. J. Am. Chem. Soc. 117: 1675-1677.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 1675-1677
    • Cohen, D.S.1    Pielak, G.J.2
  • 18
    • 0027169975 scopus 로고
    • Isotope effects in peptide group hydrogen exchange
    • Connelly, G.P., Bai, Y., Jeng, M.-F., and Englander, S.W. 1993. Isotope effects in peptide group hydrogen exchange. Proteins 17: 87-92.
    • (1993) Proteins , vol.17 , pp. 87-92
    • Connelly, G.P.1    Bai, Y.2    Jeng, M.-F.3    Englander, S.W.4
  • 19
    • 27344436619 scopus 로고    scopus 로고
    • Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level
    • DelMar, C., Greenbaum, E.A., Mayne, L., Englander, S.W., and Woods, V.L. 2005. Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level. Proc. Natl. Acad. Sci. 102: 15477-15482.
    • (2005) Proc. Natl. Acad. Sci , vol.102 , pp. 15477-15482
    • DelMar, C.1    Greenbaum, E.A.2    Mayne, L.3    Englander, S.W.4    Woods, V.L.5
  • 20
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K.A. and Chan, H.S. 1997. From Levinthal to pathways to funnels. Nat. Struct. Biol. 4: 10-19.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 21
    • 0344301982 scopus 로고    scopus 로고
    • Protein folding: A perspective from theory and experiment
    • Dobson, C.M., Sǎli, A., and Karplus, M. 1998. Protein folding: A perspective from theory and experiment. Angew. Chem. Int. Ed. Engl. 37: 868-893.
    • (1998) Angew. Chem. Int. Ed. Engl , vol.37 , pp. 868-893
    • Dobson, C.M.1    Sǎli, A.2    Karplus, M.3
  • 22
    • 0037059032 scopus 로고    scopus 로고
    • Submolecular cooperativity produces multi-state protein unfolding and refolding
    • Englander, S.W., Mayne, L., and Rumbley, J.N. 2002. Submolecular cooperativity produces multi-state protein unfolding and refolding. Biophys. Chem. 101-102: 57-65.
    • (2002) Biophys. Chem , vol.101-102 , pp. 57-65
    • Englander, S.W.1    Mayne, L.2    Rumbley, J.N.3
  • 23
    • 0242318402 scopus 로고    scopus 로고
    • Specific nonnative hydrophobic interactions in a hidden folding intermediate: Implications for protein folding
    • Feng, H., Takei, J., Lipsitz, R., Tjandra, N., and Bai, Y. 2003. Specific nonnative hydrophobic interactions in a hidden folding intermediate: Implications for protein folding. Biochemistry 42: 12461-12465.
    • (2003) Biochemistry , vol.42 , pp. 12461-12465
    • Feng, H.1    Takei, J.2    Lipsitz, R.3    Tjandra, N.4    Bai, Y.5
  • 24
    • 17044438189 scopus 로고    scopus 로고
    • A protein folding pathway with multiple folding intermediates at atomic resolution
    • Feng, H., Zhou, Z., and Bai, Y. 2005. A protein folding pathway with multiple folding intermediates at atomic resolution. Proc. Natl. Acad. Sci. 102: 5026-5031.
    • (2005) Proc. Natl. Acad. Sci , vol.102 , pp. 5026-5031
    • Feng, H.1    Zhou, Z.2    Bai, Y.3
  • 25
    • 0034703375 scopus 로고    scopus 로고
    • A rapid test for identification of autonomous folding units in proteins
    • Fischer, K.F. and Marqusee, S. 2000. A rapid test for identification of autonomous folding units in proteins. J. Mol. Biol. 302: 701-712.
    • (2000) J. Mol. Biol , vol.302 , pp. 701-712
    • Fischer, K.F.1    Marqusee, S.2
  • 26
    • 0032539953 scopus 로고    scopus 로고
    • Local dynamics and stability of apocytochrome b562 examined by hydrogen exchange
    • Fuentes, E.J. and Wand, A.J. 1998a. Local dynamics and stability of apocytochrome b562 examined by hydrogen exchange. Biochemistry 37: 3687-3698.
    • (1998) Biochemistry , vol.37 , pp. 3687-3698
    • Fuentes, E.J.1    Wand, A.J.2
  • 27
    • 0032516448 scopus 로고    scopus 로고
    • Local stability and dynamics of apocytochrome b562 examined by the dependence of hydrogen exchange on hydrostatic pressure
    • Fuentes, E.J. and Wand, A.J. 1998b. Local stability and dynamics of apocytochrome b562 examined by the dependence of hydrogen exchange on hydrostatic pressure. Biochemistry 37: 9877-9883.
    • (1998) Biochemistry , vol.37 , pp. 9877-9883
    • Fuentes, E.J.1    Wand, A.J.2
  • 31
    • 0026009213 scopus 로고
    • Stable submolecular folding units in a non-compact form of cytochrome c
    • Jeng, M.-F. and Englander, S.W. 1991. Stable submolecular folding units in a non-compact form of cytochrome c. J. Mol. Biol. 221: 1045-1061.
    • (1991) J. Mol. Biol , vol.221 , pp. 1045-1061
    • Jeng, M.-F.1    Englander, S.W.2
  • 32
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24: 945-949.
    • (1991) J. Appl. Crystallogr , vol.24 , pp. 945-949
    • Kraulis, P.J.1
  • 33
    • 33847306593 scopus 로고    scopus 로고
    • A unified mechanism for protein folding: Predetermined pathways with optional errors
    • Krishna, M.M.G. and Englander, S.W. 2007. A unified mechanism for protein folding: Predetermined pathways with optional errors. Protein Sci. 16: 449-464.
    • (2007) Protein Sci , vol.16 , pp. 449-464
    • Krishna, M.M.G.1    Englander, S.W.2
  • 34
    • 0242578172 scopus 로고    scopus 로고
    • Intimate view of a kinetic protein folding intermediate: Residue-resolved structure, interactions, stability, folding and unfolding rates, homogeneity
    • Krishna, M.M.G., Lin, Y., Mayne, L., and Englander, S.W. 2003a. Intimate view of a kinetic protein folding intermediate: Residue-resolved structure, interactions, stability, folding and unfolding rates, homogeneity. J. Mol. Biol. 334: 501-513.
    • (2003) J. Mol. Biol , vol.334 , pp. 501-513
    • Krishna, M.M.G.1    Lin, Y.2    Mayne, L.3    Englander, S.W.4
  • 35
    • 0038786579 scopus 로고    scopus 로고
    • Cooperative omega loops in cytochrome c: Role in folding and function
    • Krishna, M.M.G., Lin, Y., Rumbley, J.N., and Englander, S.W. 2003b. Cooperative omega loops in cytochrome c: Role in folding and function. J. Mol. Biol. 331: 29-36.
    • (2003) J. Mol. Biol , vol.331 , pp. 29-36
    • Krishna, M.M.G.1    Lin, Y.2    Rumbley, J.N.3    Englander, S.W.4
  • 36
    • 5144229665 scopus 로고    scopus 로고
    • Protein misfolding: Optional barriers, misfolded intermediates, and pathway heterogeneity
    • Krishna, M.M.G., Lin, Y., and Englander, S.W. 2004a. Protein misfolding: Optional barriers, misfolded intermediates, and pathway heterogeneity. J. Mol. Biol. 343: 1095-1109.
    • (2004) J. Mol. Biol , vol.343 , pp. 1095-1109
    • Krishna, M.M.G.1    Lin, Y.2    Englander, S.W.3
  • 37
    • 3342993181 scopus 로고    scopus 로고
    • Hydrogen exchange methods to study protein folding
    • Krishna, M.M.G., Hoang, L., Lin, Y., and Englander, S.W. 2004b. Hydrogen exchange methods to study protein folding. Methods 34: 51-64.
    • (2004) Methods , vol.34 , pp. 51-64
    • Krishna, M.M.G.1    Hoang, L.2    Lin, Y.3    Englander, S.W.4
  • 38
    • 33745137861 scopus 로고    scopus 로고
    • Order of steps in the cytochrome c folding pathway: Evidence for a sequential stabilization mechanism
    • Krishna, M.M.G., Maity, H., Rumbley, J.N., Lin, Y., and Englander, S.W. 2006. Order of steps in the cytochrome c folding pathway: Evidence for a sequential stabilization mechanism. J. Mol. Biol. 359: 1411-1420.
    • (2006) J. Mol. Biol , vol.359 , pp. 1411-1420
    • Krishna, M.M.G.1    Maity, H.2    Rumbley, J.N.3    Lin, Y.4    Englander, S.W.5
  • 39
    • 0022981913 scopus 로고
    • Loops in globular proteins: A novel category of secondary structure
    • Leszczynski, J.F. and Rose, G.D. 1986. Loops in globular proteins: A novel category of secondary structure. Science 234: 849-855.
    • (1986) Science , vol.234 , pp. 849-855
    • Leszczynski, J.F.1    Rose, G.D.2
  • 40
    • 0000333671 scopus 로고
    • On the theory of the helix-coil transition in polypeptides
    • Lifson, S. and Roig, A. 1961. On the theory of the helix-coil transition in polypeptides. J. Chem. Phys. 34: 1963-1974.
    • (1961) J. Chem. Phys , vol.34 , pp. 1963-1974
    • Lifson, S.1    Roig, A.2
  • 41
    • 4644359012 scopus 로고    scopus 로고
    • How cytochrome c folds, and why: Submolecular foldon units and their stepwise sequential stabilization
    • Maity, H., Maity, M., and Englander, S.W. 2004. How cytochrome c folds, and why: Submolecular foldon units and their stepwise sequential stabilization. J. Mol. Biol. 343: 223-233.
    • (2004) J. Mol. Biol , vol.343 , pp. 223-233
    • Maity, H.1    Maity, M.2    Englander, S.W.3
  • 42
    • 33645277619 scopus 로고    scopus 로고
    • Functional role of a protein foldon - An Ω-loop foldon controls the alkaline transition in ferricytochrome c
    • Maity, H., Rumbley, J.N., and Englander, S.W. 2006. Functional role of a protein foldon - An Ω-loop foldon controls the alkaline transition in ferricytochrome c. Proteins 63: 349-355.
    • (2006) Proteins , vol.63 , pp. 349-355
    • Maity, H.1    Rumbley, J.N.2    Englander, S.W.3
  • 44
    • 0030043913 scopus 로고    scopus 로고
    • Potent peptide analogues of a G protein receptor-binding region obtained with a combinatorial library
    • Martin, E.L., Rens-Domiano, S., Schatz, P.J., and Hamm, H.E. 1996. Potent peptide analogues of a G protein receptor-binding region obtained with a combinatorial library. J. Biol. Chem. 271: 361-366.
    • (1996) J. Biol. Chem , vol.271 , pp. 361-366
    • Martin, E.L.1    Rens-Domiano, S.2    Schatz, P.J.3    Hamm, H.E.4
  • 45
    • 0032766705 scopus 로고    scopus 로고
    • Experimental study of the protein folding landscape: Unfolding reactions in cytochrome c
    • Milne, J.S., Xu, Y., Mayne, L.C., and Englander, S.W. 1999. Experimental study of the protein folding landscape: Unfolding reactions in cytochrome c. J. Mol. Biol. 290: 811-822.
    • (1999) J. Mol. Biol , vol.290 , pp. 811-822
    • Milne, J.S.1    Xu, Y.2    Mayne, L.C.3    Englander, S.W.4
  • 47
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers, J.K., Pace, C.N., and Scholtz, J.M. 1995. Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4: 2138-2148.
    • (1995) Protein Sci , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 49
    • 0036023918 scopus 로고    scopus 로고
    • Understanding protein folding with energy landscape theory. Part I: Basic concepts
    • Plotkin, S.S. and Onuchic, J.N. 2002a. Understanding protein folding with energy landscape theory. Part I: Basic concepts. Q. Rev. Biophys. 35: 111-167.
    • (2002) Q. Rev. Biophys , vol.35 , pp. 111-167
    • Plotkin, S.S.1    Onuchic, J.N.2
  • 50
    • 0036706015 scopus 로고    scopus 로고
    • Understanding protein folding with energy landscape theory. Part II: Quantitative concepts
    • Plotkin, S.S. and Onuchic, J.N. 2002b. Understanding protein folding with energy landscape theory. Part II: Quantitative concepts. Q. Rev. Biophys. 35: 205-286.
    • (2002) Q. Rev. Biophys , vol.35 , pp. 205-286
    • Plotkin, S.S.1    Onuchic, J.N.2
  • 51
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR
    • Roder, H., Elöve, G.A., and Englander, S.W. 1988. Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR. Nature 335: 700-704.
    • (1988) Nature , vol.335 , pp. 700-704
    • Roder, H.1    Elöve, G.A.2    Englander, S.W.3
  • 52
    • 0037180383 scopus 로고    scopus 로고
    • Recombinant equine cytochrome c in Escherichia coli: High-level expression, characterization, and folding and assembly mutants
    • Rumbley, J.N., Hoang, L., and Englander, S.W. 2002. Recombinant equine cytochrome c in Escherichia coli: High-level expression, characterization, and folding and assembly mutants. Biochemistry 41: 13894-13901.
    • (2002) Biochemistry , vol.41 , pp. 13894-13901
    • Rumbley, J.N.1    Hoang, L.2    Englander, S.W.3
  • 55
    • 0037108164 scopus 로고    scopus 로고
    • Populating partially unfolded forms by hydrogen exchange-directed protein engineering
    • Takei, J., Pei, W., Vu, D., and Bai, Y. 2002. Populating partially unfolded forms by hydrogen exchange-directed protein engineering. Biochemistry 41: 12308-12312.
    • (2002) Biochemistry , vol.41 , pp. 12308-12312
    • Takei, J.1    Pei, W.2    Vu, D.3    Bai, Y.4
  • 56
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford, C. 1968. Protein denaturation. Adv. Protein Chem. 23: 121-282.
    • (1968) Adv. Protein Chem , vol.23 , pp. 121-282
    • Tanford, C.1
  • 57
    • 0014718113 scopus 로고
    • Protein denaturation. C. Theoretical models for the mechanism of denaturation
    • Tanford, C. 1970. Protein denaturation. C. Theoretical models for the mechanism of denaturation. Adv. Protein Chem. 24: 1-95.
    • (1970) Adv. Protein Chem , vol.24 , pp. 1-95
    • Tanford, C.1
  • 58
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling
    • Uversky, V.N., Oldfield, C.J., and Dunker, A.K. 2005. Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling. J. Mol. Recognit. 18: 343-384.
    • (2005) J. Mol. Recognit , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 59
    • 0037058950 scopus 로고    scopus 로고
    • Sequential vs. parallel protein-folding mechanisms: Experimental tests for complex folding reactions
    • Wallace, L.A. and Matthews, C.R. 2002. Sequential vs. parallel protein-folding mechanisms: Experimental tests for complex folding reactions. Biophys. Chem. 101-102: 113-131.
    • (2002) Biophys. Chem , vol.101-102 , pp. 113-131
    • Wallace, L.A.1    Matthews, C.R.2
  • 60
    • 0038497542 scopus 로고
    • Molecular structure of nucleic acids. A structure for deoxyribose nucleic acid
    • Watson, J.D. and Crick, F.H.C. 1953. Molecular structure of nucleic acids. A structure for deoxyribose nucleic acid. Nature 171: 737-738.
    • (1953) Nature , vol.171 , pp. 737-738
    • Watson, J.D.1    Crick, F.H.C.2
  • 61
    • 24644481440 scopus 로고    scopus 로고
    • A funneled energy landscape for cytochrome c directly predicts the sequential folding route inferred from hydrogen exchange experiments
    • Weinkam, P., Zong, C., and Wolynes, P.G. 2005. A funneled energy landscape for cytochrome c directly predicts the sequential folding route inferred from hydrogen exchange experiments. Proc. Natl. Acad. Sci. 102: 12401-12406.
    • (2005) Proc. Natl. Acad. Sci , vol.102 , pp. 12401-12406
    • Weinkam, P.1    Zong, C.2    Wolynes, P.G.3
  • 62
    • 0030796986 scopus 로고    scopus 로고
    • Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate
    • Wildegger, G. and Kiefhaber, T. 1997. Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate. J. Mol. Biol. 270: 294-304.
    • (1997) J. Mol. Biol , vol.270 , pp. 294-304
    • Wildegger, G.1    Kiefhaber, T.2
  • 64
    • 0031662891 scopus 로고    scopus 로고
    • Evidence for an unfolding and refolding pathway in cytochrome c
    • Xu, Y., Mayne, L., and Englander, S.W. 1998. Evidence for an unfolding and refolding pathway in cytochrome c. Nat. Struct. Biol. 5: 774-778.
    • (1998) Nat. Struct. Biol , vol.5 , pp. 774-778
    • Xu, Y.1    Mayne, L.2    Englander, S.W.3
  • 65
    • 0036408312 scopus 로고    scopus 로고
    • Thermodynamic and kinetic exploration of the energy landscape of Borrelia budgdorferi OspA by native-state hydrogen exchange
    • Yan, S., Kennedy, S.D., and Koide, S. 2002. Thermodynamic and kinetic exploration of the energy landscape of Borrelia budgdorferi OspA by native-state hydrogen exchange. J. Mol. Biol. 323: 363-375.
    • (2002) J. Mol. Biol , vol.323 , pp. 363-375
    • Yan, S.1    Kennedy, S.D.2    Koide, S.3
  • 66
    • 1942457259 scopus 로고    scopus 로고
    • Conformational heterogeneity of an equilibrium folding intermediate quantified and mapped by scanning mutagenesis
    • Yan, S., Gawlak, G., Smith, J., Silver, L., Koide, A., and Koide, S. 2004. Conformational heterogeneity of an equilibrium folding intermediate quantified and mapped by scanning mutagenesis. J. Mol. Biol. 338: 811-825.
    • (2004) J. Mol. Biol , vol.338 , pp. 811-825
    • Yan, S.1    Gawlak, G.2    Smith, J.3    Silver, L.4    Koide, A.5    Koide, S.6
  • 67
    • 29144447995 scopus 로고    scopus 로고
    • Serendipity strikes twice: The discovery and rediscovery of defective ribosomal products (DRiPS)
    • Yewdell, J.W. 2005. Serendipity strikes twice: The discovery and rediscovery of defective ribosomal products (DRiPS). Cell. Mol. Biol. 51: 635-641.
    • (2005) Cell. Mol. Biol , vol.51 , pp. 635-641
    • Yewdell, J.W.1
  • 68
    • 0000668407 scopus 로고
    • Theory of the phase transition between helix and random coil in polypeptide chains
    • Zimm, G.H. and Bragg, J.K. 1959. Theory of the phase transition between helix and random coil in polypeptide chains. J. Chem. Phys. 31: 526-535.
    • (1959) J. Chem. Phys , vol.31 , pp. 526-535
    • Zimm, G.H.1    Bragg, J.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.