메뉴 건너뛰기




Volumn 40, Issue 1, 2011, Pages 187-203

Molecular origin of the hierarchical elasticity of titin: Simulation, experiment, and theory

Author keywords

elastic protein; mechanical protein; molecular dynamics; steered molecular dynamics

Indexed keywords

CONNECTIN; FIBRONECTIN; FIBRONECTIN III; GLUTAMIC ACID; IMMUNOGLOBULIN G; LYSINE; PROLINE; UNCLASSIFIED DRUG; VALINE;

EID: 79951831503     PISSN: 1936122X     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev-biophys-072110-125325     Document Type: Article
Times cited : (50)

References (94)
  • 2
    • 77955560782 scopus 로고    scopus 로고
    • The structure of the FnIII tandem A77-A78 points to a periodically conserved architecture in the myosin-binding region of titin
    • Bucher RM, Svergun DI, Muhle-Goll C, Mayans O. 2010. The structure of the FnIII tandem A77-A78 points to a periodically conserved architecture in the myosin-binding region of titin. J. Mol. Biol. 401:843-53
    • (2010) J. Mol. Biol. , vol.401 , pp. 843-853
    • Bucher, R.M.1    Svergun, D.I.2    Muhle-Goll, C.3    Mayans, O.4
  • 5
    • 0038412705 scopus 로고    scopus 로고
    • Calculating free energies using a scaled-force molecular dynamics algorithm
    • DOI 10.1080/08927020211975, PII BXP6WB3MKDLRE39H
    • DarveE,Wilson MA, PohorilleA. 2002. Calculating free energies using a scaled-force molecular dynamics algorithm. Mol. Sim. 28:113-44 (Pubitemid 44121114)
    • (2002) Molecular Simulation , vol.28 , Issue.1-2 , pp. 113-144
    • Darve, E.1    Wilson, M.A.2    Pohorille, A.3
  • 6
    • 0028028999 scopus 로고
    • Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin
    • Erickson HP. 1994. Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin. Proc. Natl. Acad. Sci. USA 91:10114-18
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10114-10118
    • Erickson, H.P.1
  • 7
    • 0034979287 scopus 로고    scopus 로고
    • Probing the relation between force - Lifetime - And chemistry in single molecular bonds
    • DOI 10.1146/annurev.biophys.30.1.105
    • Evans E. 2001. Probing the relation between force-lifetime-and chemistry in single molecular bonds. Annu. Rev. Biophys. Biomol. Struct. 30:105-28 (Pubitemid 32566158)
    • (2001) Annual Review of Biophysics and Biomolecular Structure , vol.30 , pp. 105-128
    • Evans, E.1
  • 8
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans E, Ritchie K. 1997. Dynamic strength of molecular adhesion bonds. Biophys. J. 72(4):1541-55 (Pubitemid 27133095)
    • (1997) Biophysical Journal , vol.72 , Issue.4 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 9
    • 28444487209 scopus 로고    scopus 로고
    • Fingerprinting single molecules in vivo
    • DOI 10.1529/biophysj.105.072223
    • Fernandez JM. 2005. Fingerprinting single molecules in vivo. Biophys. J. 89:3676-77 (Pubitemid 41725591)
    • (2005) Biophysical Journal , vol.89 , Issue.6 , pp. 3676-3677
    • Fernandez, J.M.1
  • 12
    • 0036389817 scopus 로고    scopus 로고
    • Mechanical unfolding of a titin Ig domain: Structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering
    • Fowler SB, Best RB, Herrera JLT, Rutherford TJ, Steward A, et al. 2002. Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering. J. Mol. Biol. 322(4):841-49
    • (2002) J. Mol. Biol. , vol.322 , Issue.4 , pp. 841-849
    • Fowler, S.B.1    Best, R.B.2    Jlt, H.3    Rutherford, T.J.4    Steward, A.5
  • 13
    • 0034805058 scopus 로고    scopus 로고
    • Simulated refolding of stretched titin immunoglobulin domains
    • Gao M, Lu H, Schulten K. 2001. Simulated refolding of stretched titin immunoglobulin domains. Biophys. J. 81:2268-77 (Pubitemid 32917175)
    • (2001) Biophysical Journal , vol.81 , Issue.4 , pp. 2268-2277
    • Gao, M.1    Lu, H.2    Schulten, K.3
  • 14
    • 0037569632 scopus 로고    scopus 로고
    • Unfolding of titin domains studied by molecular dynamics simulations
    • DOI 10.1023/A:1023466608163
    • Gao M, Lu H, Schulten K. 2002. Unfolding of titin domains studied by molecular dynamics simulations. J. Muscle Res. Cell Motil. 23:513-21 (Pubitemid 36583668)
    • (2002) Journal of Muscle Research and Cell Motility , vol.23 , Issue.5-6 , pp. 513-521
    • Gao, M.1    Lu, H.2    Schulten, K.3
  • 16
    • 0036924186 scopus 로고    scopus 로고
    • Steered molecular dynamics studies of titin I1 domain unfolding
    • Gao M, Wilmanns M, Schulten K. 2002. Steered molecular dynamics studies of titin I1 domain unfolding. Biophys. J. 83:3435-45 (Pubitemid 36041960)
    • (2002) Biophysical Journal , vol.83 , Issue.6 , pp. 3435-3445
    • Gao, M.1    Wilmanns, M.2    Schulten, K.3
  • 17
    • 66149128872 scopus 로고    scopus 로고
    • Mechanical stability and differentially conserved physical-chemical properties of titin Ig-domains
    • Garcia TI, Oberhauser AF, Braun W. 2009. Mechanical stability and differentially conserved physical-chemical properties of titin Ig-domains. Proteins Struct. Func. Bioinform. 75:706-18
    • (2009) Proteins Struct. Func. Bioinform. , vol.75 , pp. 706-718
    • Garcia, T.I.1    Oberhauser, A.F.2    Braun, W.3
  • 18
    • 34848909232 scopus 로고    scopus 로고
    • Force-clamp spectroscopy of single-protein monomers reveals the individual unfolding and folding pathways of i27 and ubiquitin
    • DOI 10.1529/biophysj.107.104422
    • Garcia-Manyes S, Brujic J, Badilla CL, Fernandez JM. 2007. Force-clamp spectroscopy of single-protein monomers reveals the individual unfolding and folding pathways of I27 and ubiquitin. Biophys. J. 93:2436-46 (Pubitemid 47511144)
    • (2007) Biophysical Journal , vol.93 , Issue.7 , pp. 2436-2446
    • Garcia-Manyes, S.1    Brujic, J.2    Badilla, C.L.3    Fernandez, J.M.4
  • 19
    • 0035707910 scopus 로고    scopus 로고
    • The muscular dystrophy with myositis (mdm) mouse mutation disrupts a skeletal muscle-specific domain of titin
    • DOI 10.1006/geno.2002.6685
    • Garvey SM, Rajan C, Lerner AP, Frankel WN, Cox GA. 2002. The muscular dystrophy with myositis (mdm) mouse mutation disrupts a skeletal muscle-specific domain of titin. Genomics 79:146-49 (Pubitemid 34124016)
    • (2001) Genomics , vol.79 , Issue.2 , pp. 146-149
    • Garvey, S.M.1    Rajan, C.2    Lerner, A.P.3    Frankel, W.N.4    Cox, G.A.5
  • 20
    • 0029882110 scopus 로고    scopus 로고
    • A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series
    • DOI 10.1016/0014-5793(96)00338-9
    • Gautel M, Goulding D. 1996. A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series. FEBS Lett. 385:11-14 (Pubitemid 26153462)
    • (1996) FEBS Letters , vol.385 , Issue.1-2 , pp. 11-14
    • Gautel, M.1    Goulding, D.2
  • 21
    • 1242342244 scopus 로고    scopus 로고
    • The giant protein titin: A major player in myocardial mechanics, signaling, and disease
    • DOI 10.1161/01.RES.0000117769.88862.F8
    • Granzier HL, Labeit S. 2004. The giant protein titin: a major player in myocardial mechanics, signaling, and disease. Circ. Res. 94:284-95 (Pubitemid 38240719)
    • (2004) Circulation Research , vol.94 , Issue.3 , pp. 284-295
    • Granzier, H.L.1    Labeit, S.2
  • 22
    • 26844443092 scopus 로고    scopus 로고
    • Titin and its associated proteins: The third myofilament system of the sarcomere
    • DOI 10.1016/S0065-3233(04)71003-7, PII S0065323304710037
    • Granzier HL, Labeit S. 2005. Titin and its associated proteins: the third myofilament system of the sarcomere. Adv. Protein Chem. 71:89-119 (Pubitemid 41446927)
    • (2005) Advances in Protein Chemistry , vol.71 , pp. 89-119
    • Granzier, H.L.1    Labeit, S.2
  • 25
    • 4344660645 scopus 로고    scopus 로고
    • Overcoming free energy barriers using unconstrained molecular dynamics simulations
    • Hénin J, Chipot C. 2004. Overcoming free energy barriers using unconstrained molecular dynamics simulations. J. Chem. Phys. 121(7):2904-14
    • (2004) J. Chem. Phys. , vol.121 , Issue.7 , pp. 2904-2914
    • Hénin, J.1    Chipot, C.2
  • 26
    • 20444499328 scopus 로고    scopus 로고
    • Insights into the recognition and association of transmembrane α-helices. The free energy of α-helix dimerization in glycophorin A
    • DOI 10.1021/ja050581y
    • Hénin J, Pohorille A, Chipot C. 2005. Insights into the recognition and association of transmembrane alpha-helices. The free energy of alpha-helix dimerization in glycophorin A. J. Am. Chem. Soc. 127:8478-84 (Pubitemid 40828164)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.23 , pp. 8478-8484
    • Henin, J.1    Pohorille, A.2    Chipot, C.3
  • 27
    • 0027488781 scopus 로고
    • Characterization of β-connectin (titin 2) from striated muscle by dynamic light scattering
    • Higuchi H, Nakauchi Y, Maruyama K, Fujime S. 1993. Characterization of beta-connectin (titin 2) from striated muscle by dynamic light scattering. Biophys. J. 65:1906-15 (Pubitemid 23334858)
    • (1993) Biophysical Journal , vol.65 , Issue.5 , pp. 1906-1915
    • Higuchi, H.1    Nakauchi, Y.2    Maruyama, K.3    Fujime, S.4
  • 28
    • 79951821839 scopus 로고    scopus 로고
    • Amplification of tertiary structure elasticity in a tandem titin Ig chain
    • Hsin J, Schulten K. 2011. Amplification of tertiary structure elasticity in a tandem titin Ig chain. Biophys. J. 100:L22-24
    • (2011) Biophys. J. , vol.100
    • Hsin, J.1    Schulten, K.2
  • 29
    • 0038650860 scopus 로고    scopus 로고
    • Kinetics from nonequilibrium single-molecule pulling experiments
    • Hummer G, Szabo A. 2003. Kinetics from nonequilibrium single-molecule pulling experiments. Biophys. J. 85(1):5-15 (Pubitemid 36753612)
    • (2003) Biophysical Journal , vol.85 , Issue.1 , pp. 5-15
    • Hummer, G.1    Szabo, A.2
  • 31
    • 0030584660 scopus 로고    scopus 로고
    • Immunoglobulin-like modules from titin I-band: Extensible components of muscle elasticity
    • Improta S, Politou AS, Pastore A. 1996. Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity. Structure 4:323-37
    • (1996) Structure , vol.4 , pp. 323-337
    • Improta, S.1    Politou, A.S.2    Pastore, A.3
  • 32
    • 0035312645 scopus 로고    scopus 로고
    • Steered molecular dynamics and mechanical functions of proteins
    • DOI 10.1016/S0959-440X(00)00194-9
    • Isralewitz B, Gao M, Schulten K. 2001. Steered molecular dynamics and mechanical functions of proteins. Curr. Opin. Struct. Biol. 11:224-30 (Pubitemid 32289426)
    • (2001) Current Opinion in Structural Biology , vol.11 , Issue.2 , pp. 224-230
    • Isralewitz, B.1    Gao, M.2    Schulten, K.3
  • 33
    • 0002174423 scopus 로고    scopus 로고
    • Steered molecular dynamics
    • Lect. Notes Comput. Sci. Eng., ed. P Deuflhard, J Hermans, B Leimkuhler, AE Mark, S Reich, RD Skeel Berlin: Springer- Verlag
    • Izrailev S, Stepaniants S, Isralewitz B, Kosztin D, Lu H, et al. 1998. Steered molecular dynamics. In Computational Molecular Dynamics: Challenges, Methods, Ideas. Vol. 4: Lect. Notes Comput. Sci. Eng., ed. P Deuflhard, J Hermans, B Leimkuhler, AE Mark, S Reich, RD Skeel, pp. 39-65. Berlin: Springer-Verlag
    • (1998) Computational Molecular Dynamics: Challenges, Methods, Ideas. , vol.4 , pp. 39-65
    • Izrailev, S.1    Stepaniants, S.2    Isralewitz, B.3    Kosztin, D.4    Lu, H.5
  • 34
    • 0031234623 scopus 로고    scopus 로고
    • A combined wormlike-chain and bead model for dynamic simulations of long linear DNA
    • DOI 10.1006/jcph.1997.5765, PII S002199919795765X
    • Jian H, Vologodskii AV, Schlick T. 1997. A combined wormlike-chain and bead model for dynamics simulations of long linear DNA. J. Comp. Phys. 136:168-79 (Pubitemid 127170097)
    • (1997) Journal of Computational Physics , vol.136 , Issue.1 , pp. 168-179
    • Jian, H.1    Vologodskii, A.V.2    Schlick, T.3
  • 36
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • DOI 10.1126/science.276.5315.1112
    • Kellermayer MSZ, Smith SB, Granzier HL, Bustamante C. 1997. Folding-unfolding transition in single titin modules characterized with laser tweezers. Science 276:1112-16 (Pubitemid 27218119)
    • (1997) Science , vol.276 , Issue.5315 , pp. 1112-1116
    • Kellermayer, M.S.Z.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 37
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit S, Kolmerer B. 1995. Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science 270:293-96
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 38
    • 30444458378 scopus 로고    scopus 로고
    • From A to Z and back? Multicompartment proteins in the sarcomere
    • DOI 10.1016/j.tcb.2005.11.007, PII S0962892405003028
    • Lange S, Ehler E, Gautel M. 2006. From A to Z and back? Multicompartment proteins in the sarcomere. Trends Cell. Biol. 16:11-18 (Pubitemid 43077090)
    • (2006) Trends in Cell Biology , vol.16 , Issue.1 , pp. 11-18
    • Lange, S.1    Ehler, E.2    Gautel, M.3
  • 40
    • 4143147307 scopus 로고    scopus 로고
    • The elasticity of single titin molecules using a two-bead optical tweezers assay
    • DOI 10.1529/biophysj.103.033571
    • Leake MC, Wilson D, Gautel M, Simmons RM. 2004. The elasticity of single titin molecules using a two-bead optical tweezers assay. Biophys. J. 87:1112-35 (Pubitemid 39095089)
    • (2004) Biophysical Journal , vol.87 , Issue.2 , pp. 1112-1135
    • Leake, M.C.1    Wilson, D.2    Gautel, M.3    Simmons, R.M.4
  • 41
    • 34548645722 scopus 로고    scopus 로고
    • Secondary and tertiary structure elasticity of titin Z1Z2 and a titin chain model
    • DOI 10.1529/biophysj.107.105528
    • Lee EH, Hsin J, Mayans O, Schulten K. 2007. Secondary and tertiary structure elasticity of titin Z1Z2 and a titin chain model. Biophys. J. 93:1719-35 (Pubitemid 47403312)
    • (2007) Biophysical Journal , vol.93 , Issue.5 , pp. 1719-1735
    • Lee, E.H.1    Hsin, J.2    Mayans, O.3    Schulten, K.4
  • 44
    • 33644849450 scopus 로고    scopus 로고
    • Nanospring behaviour of ankyrin repeats
    • DOI 10.1038/nature04437, PII N04437
    • Lee G, Abdi K, Jiang Y, Michaely P, Bennett V, Marszalek PE. 2006. Nanospring behaviour of ankyrin repeats. Nature 440:246-49 (Pubitemid 43372106)
    • (2006) Nature , vol.440 , Issue.7081 , pp. 246-249
    • Lee, G.1    Abdi, K.2    Jiang, Y.3    Michaely, P.4    Bennett, V.5    Marszalek, P.E.6
  • 45
    • 0142195769 scopus 로고    scopus 로고
    • Mechanical design of the first proximal Ig domain of human cardiac titin revealed by single molecule force spectroscopy
    • DOI 10.1016/j.jmb.2003.09.036
    • Li H, Fernandez JM. 2003. Mechanical design of the first proximal Ig domain of human cardiac titin revealed by single molecule force spectroscopy. J. Mol. Biol. 334(1):75-86 (Pubitemid 37330101)
    • (2003) Journal of Molecular Biology , vol.334 , Issue.1 , pp. 75-86
    • Li, H.1    Fernandez, J.M.2
  • 49
    • 0033928461 scopus 로고    scopus 로고
    • Stretching molecular springs: Elasticity of titin filaments in vertebrate striated muscle
    • Linke WA. 2000. Stretching molecular springs: elasticity of titin filaments in vertebrate striated muscle. Histol. Histopathol. 15:799-811 (Pubitemid 30488563)
    • (2000) Histology and Histopathology , vol.15 , Issue.3 , pp. 799-811
    • Linke, W.A.1
  • 50
    • 43149084573 scopus 로고    scopus 로고
    • Pulling single molecules of titin by AFM-recent advances and physiological implications
    • Linke WA, Grützner A. 2008. Pulling single molecules of titin by AFM-recent advances and physiological implications. Pflug. Arch. Eur. J. Physiol. 456(1):101-15
    • (2008) Pflug. Arch. Eur. J. Physiol. , vol.456 , Issue.1 , pp. 101-115
    • Linke, W.A.1    Grützner, A.2
  • 54
    • 4444302854 scopus 로고    scopus 로고
    • Multiple sources of passive stress relaxation in muscle fibres
    • DOI 10.1088/0031-9155/49/16/009, PII S0031915504713792
    • Linke WA, Leake MC. 2004. Multiple sources of passive stress relaxation in muscle fibres. Phys. Med. Biol. 49:3613-27 (Pubitemid 39206444)
    • (2004) Physics in Medicine and Biology , vol.49 , Issue.16 , pp. 3613-3627
    • Linke, W.A.1    Leake, M.C.2
  • 56
    • 0031848099 scopus 로고    scopus 로고
    • Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation
    • Lu H, Isralewitz B, Krammer A, Vogel V, Schulten K. 1998. Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation. Biophys. J. 75:662-71 (Pubitemid 28357508)
    • (1998) Biophysical Journal , vol.75 , Issue.2 , pp. 662-671
    • Lu, H.1    Isralewitz, B.2    Krammer, A.3    Vogel, V.4    Schulten, K.5
  • 57
    • 0033445338 scopus 로고    scopus 로고
    • Steered molecular dynamics simulation of conformational changes of im-munoglobulin domain I27 interpret atomic force microscopy observations
    • Lu H, Schulten K. 1999. Steered molecular dynamics simulation of conformational changes of im-munoglobulin domain I27 interpret atomic force microscopy observations. Chem. Phys. 247:141-53
    • (1999) Chem. Phys. , vol.247 , pp. 141-153
    • Lu, H.1    Schulten, K.2
  • 58
    • 0033917135 scopus 로고    scopus 로고
    • The key event in force-induced unfolding of titin's immunoglobulin domains
    • Lu H, Schulten K. 2000. The key event in force-induced unfolding of titin's immunoglobulin domains. Biophys. J. 79:51-65 (Pubitemid 30436727)
    • (2000) Biophysical Journal , vol.79 , Issue.1 , pp. 51-65
    • Lu, H.1    Schulten, K.2
  • 59
    • 77950370873 scopus 로고    scopus 로고
    • Unraveling evolutionary constraints: A heterogeneous conservation in dynamics of the titin Ig domains
    • Lukman S, Grant GH, Bui JM. 2010. Unraveling evolutionary constraints: a heterogeneous conservation in dynamics of the titin Ig domains. FEBS Lett. 584:1235-39
    • (2010) FEBS Lett. , vol.584 , pp. 1235-1239
    • Lukman, S.1    Grant, G.H.2    Bui, J.M.3
  • 60
    • 33748331350 scopus 로고    scopus 로고
    • The Ig doublet Z1Z2: A model system for the hybrid analysis of conformational dynamics in Ig tandems from titin
    • DOI 10.1016/j.str.2006.07.009, PII S0969212606003327
    • Marino M, Zou P, Svergun D, Garcia P, Edlich C, et al. 2006. The Ig doublet Z1Z2: a model system for the hybrid analysis of conformational dynamics in Ig tandems from titin. Structure 14:1437-47 (Pubitemid 44331621)
    • (2006) Structure , vol.14 , Issue.9 , pp. 1437-1447
    • Marino, M.1    Zou, P.2    Svergun, D.3    Garcia, P.4    Edlich, C.5    Simon, B.6    Wilmanns, M.7    Muhle-Goll, C.8    Mayans, O.9
  • 63
    • 0034886351 scopus 로고    scopus 로고
    • Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin
    • DOI 10.1016/S0969-2126(01)00591-3, PII S0969212601005913
    • Mayans O, Wuerges J, Canela S, Gautel M, Wilmanns M. 2001. Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin. Structure 9:331-40 (Pubitemid 32772578)
    • (2001) Structure , vol.9 , Issue.4 , pp. 331-340
    • Mayans, O.1    Wuerges, J.2    Canela, S.3    Gautel, M.4    Wilmanns, M.5
  • 65
    • 34247624040 scopus 로고    scopus 로고
    • Molecular determinants for the recruitment of the ubiquitin-ligase MuRF-1 onto M-line titin
    • DOI 10.1096/fj.06-7644com
    • Mrosek M, Labeit D, Witt S, Heerklotz H, von Castelmur E, et al. 2007. Molecular determinants for the recruitment of the ubiquitin-ligase MuRF-1 onto M-line titin. FASEB J. 21:1383-92 (Pubitemid 46684841)
    • (2007) FASEB Journal , vol.21 , Issue.7 , pp. 1383-1392
    • Mrosek, M.1    Labeit, D.2    Witt, S.3    Heerklotz, H.4    Von Castelmur, E.5    Labeit, S.6    Mayans, O.7
  • 66
    • 34447270294 scopus 로고    scopus 로고
    • Rigid Conformation of an Immunoglobulin Domain Tandem Repeat in the A-band of the Elastic Muscle Protein Titin
    • DOI 10.1016/j.jmb.2007.05.055, PII S0022283607007024
    • Müller S, Lange S, Gautel M, Wilmanns M. 2007. Rigid conformation of an immunoglobulin domain tandem repeat in the A-band of the elastic muscle protein titin. J. Mol. Biol. 371:469-80 (Pubitemid 47048277)
    • (2007) Journal of Molecular Biology , vol.371 , Issue.2 , pp. 469-480
    • Muller, S.1    Lange, S.2    Gautel, M.3    Wilmanns, M.4
  • 68
    • 43749107950 scopus 로고    scopus 로고
    • Mechanical biochemistry of protein one molecule at a time
    • Oberhauser AF, Carrion-Vazquez M. 2008. Mechanical biochemistry of protein one molecule at a time. J. Biol. Chem. 283:6617-21
    • (2008) J. Biol. Chem. , vol.283 , pp. 6617-6621
    • Oberhauser, A.F.1    Carrion-Vazquez, M.2
  • 70
    • 0001832838 scopus 로고    scopus 로고
    • Single molecule force spectroscopy by AFM indicates helical structure of poly(ethylene-glycol) in water
    • Oesterhelt F, Rief M, Gaub HE. 1999. Single molecule force spectroscopy by AFM indicates helical structure of poly(ethylene-glycol) in water. New J. Phys. 1:6.1-6.11
    • (1999) New J. Phys. , vol.1 , pp. 61-611
    • Oesterhelt, F.1    Rief, M.2    Gaub, H.E.3
  • 73
    • 70349885458 scopus 로고    scopus 로고
    • Force and function: Probing proteins with AFM-based force spectroscopy
    • Puchner EM, Gaub HE. 2009. Force and function: probing proteins with AFM-based force spectroscopy. Curr. Opin. Struct. Biol. 19:605-14
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 605-614
    • Puchner, E.M.1    Gaub, H.E.2
  • 74
    • 11544281834 scopus 로고    scopus 로고
    • Elastically coupled two-level systems as a model for biopolymer extensibility
    • Rief M, Fernandez JM, Gaub HE. 1998. Elastically coupled two-level systems as a model for biopolymer extensibility. Phys. Rev. Lett. 81:4764-67 (Pubitemid 128626983)
    • (1998) Physical Review Letters , vol.81 , Issue.21 , pp. 4764-4767
    • Rief, M.1    Fernandez, J.M.2    Gaub, H.E.3
  • 75
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • DOI 10.1126/science.276.5315.1109
    • Rief M, Gautel M, Oesterhelt F, Fernandez JM, Gaub HE. 1997. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276:1109-12 (Pubitemid 27218118)
    • (1997) Science , vol.276 , Issue.5315 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 76
    • 0031767965 scopus 로고    scopus 로고
    • The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy
    • Rief M, Gautel M, Schemmel A, Gaub HE. 1998. The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by AFM. Biophys. J. 75:3008-14 (Pubitemid 28548968)
    • (1998) Biophysical Journal , vol.75 , Issue.6 , pp. 3008-3014
    • Rief, M.1    Gautel, M.2    Schemmel, A.3    Gaub, H.E.4
  • 77
    • 0037066262 scopus 로고    scopus 로고
    • Force spectroscopy of single biomolecules
    • Rief M, Grubmüller H. 2002. Force spectroscopy of single biomolecules. Chemphyschem 3:255-61
    • (2002) Chemphyschem , vol.3 , pp. 255-261
    • Rief, M.1    Grubmüller, H.2
  • 78
    • 1642617408 scopus 로고    scopus 로고
    • Assessing the efficiency of free energy calculation methods
    • Rodriguez-Gomez D, Darve E, Pohorille A. 2004. Assessing the efficiency of free energy calculation methods. J. Chem. Phys. 120:3563-78
    • (2004) J. Chem. Phys. , vol.120 , pp. 3563-3578
    • Rodriguez-Gomez, D.1    Darve, E.2    Pohorille, A.3
  • 79
    • 14844297706 scopus 로고    scopus 로고
    • The elasticity of individual titin PEVK exons measured by single molecule atomic force microscopy
    • DOI 10.1074/jbc.C400573200
    • Sarkar A, Caamano S, Fernandez JM. 2005. The elasticity of individual titin PEVK exons measured by single molecule atomic force microscopy. J. Biol. Chem. 280:6261-64 (Pubitemid 40341171)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.8 , pp. 6261-6264
    • Sarkar, A.1    Caamano, S.2    Fernandez, J.M.3
  • 82
    • 17044401714 scopus 로고    scopus 로고
    • In search of the hair-cell gating spring: Elastic properties of ankyrin and cadherin repeats
    • Sotomayor M, Corey DP, Schulten K. 2005. In search of the hair-cell gating spring: elastic properties of ankyrin and cadherin repeats. Structure 13:669-82
    • (2005) Structure , vol.13 , pp. 669-682
    • Sotomayor, M.1    Corey, D.P.2    Schulten, K.3
  • 83
    • 34249930159 scopus 로고    scopus 로고
    • Single-molecule experiments in vitro and in silico
    • DOI 10.1126/science.1137591
    • Sotomayor M, Schulten K. 2007. Single-molecule experiments in vitro and in silico. Science 316:1144-48 (Pubitemid 46877468)
    • (2007) Science , vol.316 , Issue.5828 , pp. 1144-1148
    • Sotomayor, M.1    Schulten, K.2
  • 84
    • 45849137475 scopus 로고    scopus 로고
    • ++ switch in adhesion and elasticity of C-cadherin
    • ++ switch in adhesion and elasticity of C-cadherin. Biophys. J. 94:4621-33
    • (2008) Biophys. J. , vol.94 , pp. 4621-4633
    • Sotomayor, M.1    Schulten, K.2
  • 85
    • 0032559640 scopus 로고    scopus 로고
    • Titin extensibility in situ: Entropic elasticity of permanently folded and permanently unfolded molecular segments
    • DOI 10.1083/jcb.140.4.853
    • Trombitas K, Greaser M, Labeit S, Jin JP, Kellermayer M, et al. 1998. Titin extensibility in situ: entropic elasticity of permanently folded and permanently unfolded molecular segments. J. Cell Biol. 140:853-59 (Pubitemid 28141223)
    • (1998) Journal of Cell Biology , vol.140 , Issue.4 , pp. 853-859
    • Trombitas, K.1    Greaser, M.2    Labeit, S.3    Jin, J.-P.4    Kellermayer, M.5    Helmes, M.6    Granzier, H.7
  • 87
    • 0031006659 scopus 로고    scopus 로고
    • Elasticity and unfolding of single molecules of the giant muscle protein titin
    • DOI 10.1038/387308a0
    • Tskhovrebova L, Trinick J, Sleep JA, Simmons RM. 1997. Elasticity and unfolding of single molecules of the giant muscle protein titin. Nature 387:308-12 (Pubitemid 27220769)
    • (1997) Nature , vol.387 , Issue.6630 , pp. 308-312
    • Tskhovrebova, L.1    Trinick, J.2    Sleep, J.A.3    Simmons, R.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.