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Volumn 105, Issue 6, 2008, Pages 1885-1890

Atomic force microscopy reveals parallel mechanical unfolding pathways of T4 lysozyme: Evidence for a kinetic partitioning mechanism

Author keywords

Energy landscape; Force spectroscopy; Multiple pathways; Single molecule studies; Unfolding intermediate

Indexed keywords

LYSOZYME;

EID: 41149180083     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0706775105     Document Type: Article
Times cited : (94)

References (50)
  • 3
    • 0029010695 scopus 로고
    • Kinetics of protein-folding: Nucleation mechanism, time scales, and pathways
    • Guo ZY, Thirumalai D (1995) Kinetics of protein-folding: Nucleation mechanism, time scales, and pathways. Biopolymers 36:83-102.
    • (1995) Biopolymers , vol.36 , pp. 83-102
    • Guo, Z.Y.1    Thirumalai, D.2
  • 4
    • 0031285905 scopus 로고    scopus 로고
    • Kinetic partitioning mechanism as a unifying theme in the folding of biomolecules
    • Thirumalai D, Klimov DK, Woodson SA (1997) Kinetic partitioning mechanism as a unifying theme in the folding of biomolecules. Theor Chem Acc 96:14-22.
    • (1997) Theor Chem Acc , vol.96 , pp. 14-22
    • Thirumalai, D.1    Klimov, D.K.2    Woodson, S.A.3
  • 5
    • 0029025915 scopus 로고
    • Kinetic traps in lysozyme folding
    • Kiefhaber T (1995) Kinetic traps in lysozyme folding. Proc Natl Acad Sci USA 92:9029-9033.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9029-9033
    • Kiefhaber, T.1
  • 7
    • 0030787174 scopus 로고    scopus 로고
    • Multiple intermediates and transition states during protein unfolding
    • Zaidi FN, Nath U, Udgaonkar JB (1997) Multiple intermediates and transition states during protein unfolding. Nat Struct Biol 4:1016-1024.
    • (1997) Nat Struct Biol , vol.4 , pp. 1016-1024
    • Zaidi, F.N.1    Nath, U.2    Udgaonkar, J.B.3
  • 8
    • 0037418635 scopus 로고    scopus 로고
    • Hammond behavior versus ground state effects in protein folding: Evidence for narrow free energy barriers and residual structure in unfolded states
    • Sanchez IE, Kiefhaber T (2003) Hammond behavior versus ground state effects in protein folding: Evidence for narrow free energy barriers and residual structure in unfolded states. J Mol Biol 327:867-884.
    • (2003) J Mol Biol , vol.327 , pp. 867-884
    • Sanchez, I.E.1    Kiefhaber, T.2
  • 9
    • 0029746061 scopus 로고    scopus 로고
    • Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH
    • Chamberlain AK, Handel TM, 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
  • 10
    • 17644425688 scopus 로고    scopus 로고
    • Local and long-range stability in tandemly arrayed tetratricopeptide repeats
    • Main ER, Stott K, Jackson SE, Regan L (2005) Local and long-range stability in tandemly arrayed tetratricopeptide repeats. Proc Natl Acad Sci USA 102:5721-5726.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5721-5726
    • Main, E.R.1    Stott, K.2    Jackson, S.E.3    Regan, L.4
  • 11
    • 0032876680 scopus 로고    scopus 로고
    • Protein conformational stabilities can be determined from hydrogen exchange rates
    • Huyghues-Despointes BM, Scholtz JM, Pace CN (1999) Protein conformational stabilities can be determined from hydrogen exchange rates. Nat Struct Biol 6:910-912.
    • (1999) Nat Struct Biol , vol.6 , pp. 910-912
    • Huyghues-Despointes, B.M.1    Scholtz, J.M.2    Pace, C.N.3
  • 12
    • 0023104358 scopus 로고
    • Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution
    • Weaver LH, Matthews BW (1987) Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution. J Mol Biol 193:189-199.
    • (1987) J Mol Biol , vol.193 , pp. 189-199
    • Weaver, L.H.1    Matthews, B.W.2
  • 13
    • 0030045089 scopus 로고    scopus 로고
    • Structural and genetic analysis of the folding and function of T4 lysozyme
    • Matthews BW (1996) Structural and genetic analysis of the folding and function of T4 lysozyme. FASEB J 10:35-41.
    • (1996) FASEB J , vol.10 , pp. 35-41
    • Matthews, B.W.1
  • 14
    • 0024977347 scopus 로고
    • Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations
    • Chen BL, Baase WA, Schellman JA (1989) Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations. Biochemistry 28:691-699.
    • (1989) Biochemistry , vol.28 , pp. 691-699
    • Chen, B.L.1    Baase, W.A.2    Schellman, J.A.3
  • 16
    • 0032707706 scopus 로고    scopus 로고
    • The energetics of T4 lysozyme reveal a hierarchy of conformations
    • Llinas M, Gillespie B, Dahlquist FW, Marqusee S (1999) The energetics of T4 lysozyme reveal a hierarchy of conformations. Nat Struct Biol 6:1072-1078.
    • (1999) Nat Struct Biol , vol.6 , pp. 1072-1078
    • Llinas, M.1    Gillespie, B.2    Dahlquist, F.W.3    Marqusee, S.4
  • 17
    • 0031891493 scopus 로고    scopus 로고
    • Subdomain interactions as a determinant in the folding and stability of T4 lysozyme
    • Llinas M, Marqusee S (1998) Subdomain interactions as a determinant in the folding and stability of T4 lysozyme. Protein Sci 7:96-104.
    • (1998) Protein Sci , vol.7 , pp. 96-104
    • Llinas, M.1    Marqusee, S.2
  • 18
    • 34247593368 scopus 로고    scopus 로고
    • Exploring subdomain cooperativity in T4 lysozyme I: Structural and energetic studies of a circular permutant and protein fragment
    • Cellitti J, et al. (2007) Exploring subdomain cooperativity in T4 lysozyme I: Structural and energetic studies of a circular permutant and protein fragment. Protein Sci 16:842-851.
    • (2007) Protein Sci , vol.16 , pp. 842-851
    • Cellitti, J.1
  • 20
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief M, Gautel M, Oesterhelt F, Fernandez JM, Gaub HE (1997) Reversible unfolding of individual titin immunoglobulin domains by AFM Science 276:1109-1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 22
    • 33748046806 scopus 로고    scopus 로고
    • Anisotropic deformation response of single protein molecules
    • Dietz H, Berkemeier F, Bertz M, Rief M (2006) Anisotropic deformation response of single protein molecules. Proc Natl Acad Sci USA 103:12724-12728.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 12724-12728
    • Dietz, H.1    Berkemeier, F.2    Bertz, M.3    Rief, M.4
  • 23
    • 33847273015 scopus 로고    scopus 로고
    • Force denaturation of proteins: An unfolding story
    • Brockwell DJ (2007) Force denaturation of proteins: An unfolding story. Curr Nanosci 3:3-15.
    • (2007) Curr Nanosci , vol.3 , pp. 3-15
    • Brockwell, D.J.1
  • 25
    • 1542513548 scopus 로고    scopus 로고
    • Force-clamp spectroscopy monitors the folding trajectory of a single protein
    • Fernandez JM, Li H (2004) Force-clamp spectroscopy monitors the folding trajectory of a single protein. Science 303:1674-1678.
    • (2004) Science , vol.303 , pp. 1674-1678
    • Fernandez, J.M.1    Li, H.2
  • 26
    • 31044449315 scopus 로고    scopus 로고
    • Nonmechanical protein can have significant mechanical stability
    • Cao Y, Lam C, Wang M, Li H (2006) Nonmechanical protein can have significant mechanical stability. Angew Chem Int Ed Engl 45:642-645.
    • (2006) Angew Chem Int Ed Engl , vol.45 , pp. 642-645
    • Cao, Y.1    Lam, C.2    Wang, M.3    Li, H.4
  • 27
    • 34547151186 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy reveals a mechanically stable protein fold and the rational tuning of its mechanical stability
    • Sharma D, et al. (2007) Single-molecule force spectroscopy reveals a mechanically stable protein fold and the rational tuning of its mechanical stability. Proc Natl Acad Sci USA 104:9278-9283.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 9278-9283
    • Sharma, D.1
  • 28
    • 0033523904 scopus 로고    scopus 로고
    • Mechanical unfolding intermediates in titin modules
    • Marszalek PE, et al. (1999) Mechanical unfolding intermediates in titin modules. Nature 402:100-103.
    • (1999) Nature , vol.402 , pp. 100-103
    • Marszalek, P.E.1
  • 29
    • 10044247452 scopus 로고    scopus 로고
    • Mechanical unfolding intermediates observed by single-molecule force spectroscopy in a fibronectin type III module
    • Li L, Huang HH, Badilla CL, Fernandez JM (2005) Mechanical unfolding intermediates observed by single-molecule force spectroscopy in a fibronectin type III module. J Mol Biol 345:817-826.
    • (2005) J Mol Biol , vol.345 , pp. 817-826
    • Li, L.1    Huang, H.H.2    Badilla, C.L.3    Fernandez, J.M.4
  • 31
    • 2442448427 scopus 로고    scopus 로고
    • The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques
    • Schlierf M, Li H, Fernandez JM (2004) The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques. Proc Natl Acad Sci USA 101:7299-7304.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7299-7304
    • Schlierf, M.1    Li, H.2    Fernandez, J.M.3
  • 32
    • 9244234443 scopus 로고    scopus 로고
    • Exploring the energy landscape of GFP by single-molecule mechanical experiments
    • Dietz H, Rief M (2004) Exploring the energy landscape of GFP by single-molecule mechanical experiments. Proc Natl Acad Sci USA 101:16192-16197.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16192-16197
    • Dietz, H.1    Rief, M.2
  • 33
    • 33845980623 scopus 로고    scopus 로고
    • Mechanical unfolding pathways of the enhanced yellow fluorescent protein revealed by single molecule force spectroscopy
    • Perez-Jimenez R, Garcia-Manyes S, Ainavarapu SR, Fernandez JM (2006) Mechanical unfolding pathways of the enhanced yellow fluorescent protein revealed by single molecule force spectroscopy. J Biol Chem 281:40010-40014.
    • (2006) J Biol Chem , vol.281 , pp. 40010-40014
    • Perez-Jimenez, R.1    Garcia-Manyes, S.2    Ainavarapu, S.R.3    Fernandez, J.M.4
  • 34
    • 0034602693 scopus 로고    scopus 로고
    • Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme
    • Yang G, et al. (2000) Solid-state synthesis and mechanical unfolding of polymers of T4 lysozyme. Proc Natl Acad Sci USA 97:139-144.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 139-144
    • Yang, G.1
  • 35
    • 0842347938 scopus 로고    scopus 로고
    • Relocation or duplication of the helix A sequence of T4 lysozyme causes only modest changes in structure but can increase or decrease the rate of folding
    • Sagermann M, Baase WA, Mooers BH, Gay L, Matthews BW (2004) Relocation or duplication of the helix A sequence of T4 lysozyme causes only modest changes in structure but can increase or decrease the rate of folding. Biochemistry 43:1296-1301.
    • (2004) Biochemistry , vol.43 , pp. 1296-1301
    • Sagermann, M.1    Baase, W.A.2    Mooers, B.H.3    Gay, L.4    Matthews, B.W.5
  • 37
    • 0034691149 scopus 로고    scopus 로고
    • Native topology determines force-induced unfolding pathways in globular proteins
    • Klimov DK, Thirumalai D (2000) Native topology determines force-induced unfolding pathways in globular proteins. Proc Natl Acad Sci USA 97:7254-7259.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7254-7259
    • Klimov, D.K.1    Thirumalai, D.2
  • 38
    • 0033616713 scopus 로고    scopus 로고
    • Mechanical and chemical unfolding of a single protein: A comparison
    • Carrion-Vazquez M, et al. (1999) Mechanical and chemical unfolding of a single protein: a comparison. Proc Natl Acad Sci USA 96:3694-3699.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3694-3699
    • Carrion-Vazquez, M.1
  • 39
    • 0242417558 scopus 로고    scopus 로고
    • Identifying kinetic barriers to mechanical unfolding of the T. thermophila ribozyme
    • Onoa B, et al. (2003) Identifying kinetic barriers to mechanical unfolding of the T. thermophila ribozyme. Science 299:1892-1895.
    • (2003) Science , vol.299 , pp. 1892-1895
    • Onoa, B.1
  • 40
    • 0033517740 scopus 로고    scopus 로고
    • Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding
    • Gassner NC, et al. (1999) Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding. Biochemistry 38:14451-14460.
    • (1999) Biochemistry , vol.38 , pp. 14451-14460
    • Gassner, N.C.1
  • 41
    • 0021753949 scopus 로고
    • Evidence for intermediates during unfolding and refolding of a two-domain protein, phage T4 lysozyme: Equilibrium and kinetic studies
    • Desmadril M, Yon JM (1984) Evidence for intermediates during unfolding and refolding of a two-domain protein, phage T4 lysozyme: Equilibrium and kinetic studies. Biochemistry 23:11-19.
    • (1984) Biochemistry , vol.23 , pp. 11-19
    • Desmadril, M.1    Yon, J.M.2
  • 42
    • 0026742164 scopus 로고
    • Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR
    • Lu J, Dahlquist FW (1992) Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR Biochemistry 31:4749-4756.
    • (1992) Biochemistry , vol.31 , pp. 4749-4756
    • Lu, J.1    Dahlquist, F.W.2
  • 43
    • 33845622937 scopus 로고    scopus 로고
    • The Folding pathway of T4 lysozyme: The high-resolution structure and folding of a hidden intermediate
    • Kato H, Feng H, Bai Y (2007) The Folding pathway of T4 lysozyme: The high-resolution structure and folding of a hidden intermediate. J Mol Biol 365:870-880.
    • (2007) J Mol Biol , vol.365 , pp. 870-880
    • Kato, H.1    Feng, H.2    Bai, Y.3
  • 44
    • 33845796109 scopus 로고    scopus 로고
    • The folding pathway of T4 lysozyme: An on-pathway hidden folding intermediate
    • Kato H, Vu ND, Feng H, Zhou Z, Bai Y (2007) The folding pathway of T4 lysozyme: An on-pathway hidden folding intermediate. J Mol Biol 365:881-891.
    • (2007) J Mol Biol , vol.365 , pp. 881-891
    • Kato, H.1    Vu, N.D.2    Feng, H.3    Zhou, Z.4    Bai, Y.5
  • 45
    • 34247639886 scopus 로고    scopus 로고
    • Exploring subdomain cooperativity in T4 lysozyme II: Uncovering the C-terminal subdomain as a hidden intermediate in the kinetic folding pathway
    • Cellitti J, Bernstein R, Marqusee S (2007) Exploring subdomain cooperativity in T4 lysozyme II: Uncovering the C-terminal subdomain as a hidden intermediate in the kinetic folding pathway. Protein Sci 16:852-862.
    • (2007) Protein Sci , vol.16 , pp. 852-862
    • Cellitti, J.1    Bernstein, R.2    Marqusee, S.3
  • 46
    • 0009586942 scopus 로고    scopus 로고
    • Understanding protein folding via free-energy surfaces from theory and experiment
    • Dinner AR, Sali A, Smith LJ, Dobson CM, Karplus M (2000) Understanding protein folding via free-energy surfaces from theory and experiment. Trends Biochem Sci 25:331-339.
    • (2000) Trends Biochem Sci , vol.25 , pp. 331-339
    • Dinner, A.R.1    Sali, A.2    Smith, L.J.3    Dobson, C.M.4    Karplus, M.5
  • 47
    • 0025047629 scopus 로고
    • A mutant T4 lysozyme displays five different crystal conformations
    • Faber HR, Matthews BW (1990) A mutant T4 lysozyme displays five different crystal conformations. Nature 348:263-266.
    • (1990) Nature , vol.348 , pp. 263-266
    • Faber, H.R.1    Matthews, B.W.2
  • 48
    • 34249855274 scopus 로고    scopus 로고
    • Real-time control of the energy landscape by force directs the folding of RNA molecules
    • Li PT, Bustamante C, Tinoco I, Jr (2007) Real-time control of the energy landscape by force directs the folding of RNA molecules. Proc Natl Acad Sci USA 104:7039-7044.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 7039-7044
    • Li, P.T.1    Bustamante, C.2    Tinoco Jr, I.3
  • 49
    • 16344371778 scopus 로고    scopus 로고
    • RNA and protein folding: Common themes and variations
    • Thirumalai D, Hyeon C (2005) RNA and protein folding: common themes and variations. Biochemistry 44:4957-4970.
    • (2005) Biochemistry , vol.44 , pp. 4957-4970
    • Thirumalai, D.1    Hyeon, C.2
  • 50
    • 33746256462 scopus 로고    scopus 로고
    • Details of the partial unfolding of T4 lysozyme on quartz using site-directed spin labeling
    • Jacobsen K, Hubbell WL, Ernst OP, Risse T (2006) Details of the partial unfolding of T4 lysozyme on quartz using site-directed spin labeling. Angew Chem Int Ed Engl 45:3874-3877.
    • (2006) Angew Chem Int Ed Engl , vol.45 , pp. 3874-3877
    • Jacobsen, K.1    Hubbell, W.L.2    Ernst, O.P.3    Risse, T.4


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