메뉴 건너뛰기




Volumn 20, Issue 4, 2010, Pages 508-517

Unravelling the design principles for single protein mechanical strength

Author keywords

[No Author keywords available]

Indexed keywords

BIOMATERIAL; POLYPROTEIN; PROTEIN DERIVATIVE; SCAFFOLD PROTEIN; STRUCTURAL PROTEIN;

EID: 77955983405     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2010.05.005     Document Type: Review
Times cited : (55)

References (89)
  • 2
    • 76049107424 scopus 로고    scopus 로고
    • Lethal factor unfolding is the most force-dependent step of anthrax toxin translocation
    • Thoren K.L., Worden E.J., Yassif J.M., Krantz B.A. Lethal factor unfolding is the most force-dependent step of anthrax toxin translocation. Proc Natl Acad Sci U S A 2009, 106:21555-21560.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 21555-21560
    • Thoren, K.L.1    Worden, E.J.2    Yassif, J.M.3    Krantz, B.A.4
  • 3
    • 33751228400 scopus 로고    scopus 로고
    • ATP-dependent proteases of bacteria: recognition logic and operating principles
    • Baker T.A., Sauer R.T. ATP-dependent proteases of bacteria: recognition logic and operating principles. Trends Biochem Sci 2006, 31:647-653.
    • (2006) Trends Biochem Sci , vol.31 , pp. 647-653
    • Baker, T.A.1    Sauer, R.T.2
  • 4
    • 66749099068 scopus 로고    scopus 로고
    • Mechanoenzymatic cleavage of the ultralarge vascular protein von Willebrand factor
    • Zhang X.H., Halvorsen K., Zhang C.Z., Wong W.P., Springer T.A. Mechanoenzymatic cleavage of the ultralarge vascular protein von Willebrand factor. Science 2009, 324:1330-1334.
    • (2009) Science , vol.324 , pp. 1330-1334
    • Zhang, X.H.1    Halvorsen, K.2    Zhang, C.Z.3    Wong, W.P.4    Springer, T.A.5
  • 5
    • 60949107887 scopus 로고    scopus 로고
    • Deformation and failure of protein materials in physiologically extreme conditions and disease
    • Buehler M.J., Yung Y.C. Deformation and failure of protein materials in physiologically extreme conditions and disease. Nat Mater 2009, 8:175-188.
    • (2009) Nat Mater , vol.8 , pp. 175-188
    • Buehler, M.J.1    Yung, Y.C.2
  • 6
    • 67650391229 scopus 로고    scopus 로고
    • Mechanical characterization of protein L in the low-force regime by electromagnetic tweezers/evanescent nanometry
    • Liu R.C., Garcia-Manyes S., Sarkar A., Badilla C.L., Fernandez J.M. Mechanical characterization of protein L in the low-force regime by electromagnetic tweezers/evanescent nanometry. Biophys J 2009, 96:3810-3821.
    • (2009) Biophys J , vol.96 , pp. 3810-3821
    • Liu, R.C.1    Garcia-Manyes, S.2    Sarkar, A.3    Badilla, C.L.4    Fernandez, J.M.5
  • 7
    • 76649093956 scopus 로고    scopus 로고
    • Full distance-resolved folding energy landscape of one single protein molecule
    • Gebhardt J.C.M., Bornschlogl T., Rief M. Full distance-resolved folding energy landscape of one single protein molecule. Proc Natl Acad Sci U S A 2010, 107:2013-2018.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 2013-2018
    • Gebhardt, J.C.M.1    Bornschlogl, T.2    Rief, M.3
  • 8
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief M., Gautel M., Oesterhelt F., Fernandez J.M., Gaub H.E. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 1997, 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
  • 10
    • 2442448427 scopus 로고    scopus 로고
    • The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques
    • Schlierf M., Li H.B., Fernandez J.M. The unfolding kinetics of ubiquitin captured with single-molecule force-clamp techniques. Proc Natl Acad Sci U S A 2004, 101:7299-7304.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 7299-7304
    • Schlierf, M.1    Li, H.B.2    Fernandez, J.M.3
  • 11
    • 76649112096 scopus 로고    scopus 로고
    • Computational and single-molecule force studies of a macro domain protein reveal a key molecular determinant for mechanical stability
    • Guzman D.L., Randall A., Baldi P., Guan Z.B. Computational and single-molecule force studies of a macro domain protein reveal a key molecular determinant for mechanical stability. Proc Natl Acad Sci U S A 2010, 107:1989-1994.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 1989-1994
    • Guzman, D.L.1    Randall, A.2    Baldi, P.3    Guan, Z.B.4
  • 12
    • 33846428813 scopus 로고    scopus 로고
    • Spectrin domains lose cooperativity in forced unfolding
    • Randles L.G., Rounsevell R.W.S., Clarke J. Spectrin domains lose cooperativity in forced unfolding. Biophys J 2007, 92:571-577.
    • (2007) Biophys J , vol.92 , pp. 571-577
    • Randles, L.G.1    Rounsevell, R.W.S.2    Clarke, J.3
  • 15
    • 0032988663 scopus 로고    scopus 로고
    • Strength of a weak bond connecting flexible polymer chains
    • Evans E., Ritchie K. Strength of a weak bond connecting flexible polymer chains. Biophys J 1999, 76:2439-2447.
    • (1999) Biophys J , vol.76 , pp. 2439-2447
    • Evans, E.1    Ritchie, K.2
  • 16
    • 33645004171 scopus 로고    scopus 로고
    • Intrinsic rates and activation free energies from single-molecule pulling experiments
    • Dudko O.K., Hummer G., Szabo A. Intrinsic rates and activation free energies from single-molecule pulling experiments. Phys Rev Lett 2006, 96:108101-108104.
    • (2006) Phys Rev Lett , vol.96 , pp. 108101-108104
    • Dudko, O.K.1    Hummer, G.2    Szabo, A.3
  • 17
    • 57349124448 scopus 로고    scopus 로고
    • Theory, analysis, and interpretation of single-molecule force spectroscopy experiments
    • Dudko O.K., Hummer G., Szabo A. Theory, analysis, and interpretation of single-molecule force spectroscopy experiments. Proc Natl Acad Sci U S A 2008, 105:15755-15760.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 15755-15760
    • Dudko, O.K.1    Hummer, G.2    Szabo, A.3
  • 18
    • 67049117733 scopus 로고    scopus 로고
    • Characterizing the resistance generated by a molecular bond as it is forcibly separated
    • Freund L.B. Characterizing the resistance generated by a molecular bond as it is forcibly separated. Proc Natl Acad Sci U S A 2009, 106:8818-8823.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 8818-8823
    • Freund, L.B.1
  • 19
    • 0038650860 scopus 로고    scopus 로고
    • Kinetics from nonequilibrium single-molecule pulling experiments
    • Hummer G., Szabo A. Kinetics from nonequilibrium single-molecule pulling experiments. Biophys J 2003, 85:5-15.
    • (2003) Biophys J , vol.85 , pp. 5-15
    • Hummer, G.1    Szabo, A.2
  • 20
    • 72249117439 scopus 로고    scopus 로고
    • Direct and model free calculation of force-dependent dissociation rates from force spectroscopic data
    • Oberbarnscheidt L., Janissen R., Oesterhelt F. Direct and model free calculation of force-dependent dissociation rates from force spectroscopic data. Biophys J 2009, 97:L19-L21.
    • (2009) Biophys J , vol.97
    • Oberbarnscheidt, L.1    Janissen, R.2    Oesterhelt, F.3
  • 21
    • 33645767959 scopus 로고    scopus 로고
    • Single-molecule unfolding force distributions reveal a funnel-shaped energy landscape
    • Schlierf M., Rief M. Single-molecule unfolding force distributions reveal a funnel-shaped energy landscape. Biophys J 2006, 90:L33-L35.
    • (2006) Biophys J , vol.90
    • Schlierf, M.1    Rief, M.2
  • 22
    • 64349116014 scopus 로고    scopus 로고
    • A simple and practical spreadsheet-based method to extract single-molecule dissociation kinetics from variable loading-rate force spectroscopy data
    • Serpe M.J., Kersey F.R., Whitehead J.R., Wilson S.M., Clark R.L., Craig S.L. A simple and practical spreadsheet-based method to extract single-molecule dissociation kinetics from variable loading-rate force spectroscopy data. J Phys Chem C 2008, 112:19163-19167.
    • (2008) J Phys Chem C , vol.112 , pp. 19163-19167
    • Serpe, M.J.1    Kersey, F.R.2    Whitehead, J.R.3    Wilson, S.M.4    Clark, R.L.5    Craig, S.L.6
  • 23
    • 57949090593 scopus 로고    scopus 로고
    • New dynamical window onto the landscape for forced protein unfolding
    • Yew Z.T., McLeish T., Paci E. New dynamical window onto the landscape for forced protein unfolding. Phys Rev Lett 2008, 101:1248104.
    • (2008) Phys Rev Lett , vol.101 , pp. 1248104
    • Yew, Z.T.1    McLeish, T.2    Paci, E.3
  • 25
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco K.W., Simons K.T., Baker D. Contact order, transition state placement and the refolding rates of single domain proteins. J Mol Biol 1998, 277:985-994.
    • (1998) J Mol Biol , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 26
    • 67650764018 scopus 로고    scopus 로고
    • Mechanical stability of proteins
    • Gabovich A.M., Li M.S. Mechanical stability of proteins. J Chem Phys 2009, 131:024121.
    • (2009) J Chem Phys , vol.131 , pp. 024121
    • Gabovich, A.M.1    Li, M.S.2
  • 29
    • 54249156909 scopus 로고    scopus 로고
    • Navigating the folding energy landscape of Green Fluorescent Protein
    • Bertz M., Kunfermann A., Rief M. Navigating the folding energy landscape of Green Fluorescent Protein. Angew Chem Int Ed Engl 2008, 47:8192-8195.
    • (2008) Angew Chem Int Ed Engl , vol.47 , pp. 8192-8195
    • Bertz, M.1    Kunfermann, A.2    Rief, M.3
  • 31
    • 1642493664 scopus 로고    scopus 로고
    • Tuning the mechanical stability of fibronectin type III modules through sequence variations
    • Craig D., Gao M., Schulten K., Vogel V. Tuning the mechanical stability of fibronectin type III modules through sequence variations. Structure 2004, 12:21-30.
    • (2004) Structure , vol.12 , pp. 21-30
    • Craig, D.1    Gao, M.2    Schulten, K.3    Vogel, V.4
  • 32
    • 71049121056 scopus 로고    scopus 로고
    • Non-native interactions are critical for mechanical strength in PKD domains
    • Forman J.R., Yew Z.T., Qamar S., Sandford R.N., Paci E., Clarke J. Non-native interactions are critical for mechanical strength in PKD domains. Structure 2009, 17:1582-1590.
    • (2009) Structure , vol.17 , pp. 1582-1590
    • Forman, J.R.1    Yew, Z.T.2    Qamar, S.3    Sandford, R.N.4    Paci, E.5    Clarke, J.6
  • 33
    • 49449106310 scopus 로고    scopus 로고
    • Engineered elastomeric proteins with dual elasticity can be controlled by a molecular regulator
    • Cao Y., Li H.B. Engineered elastomeric proteins with dual elasticity can be controlled by a molecular regulator. Nat Nanotechnol 2008, 3:512-516.
    • (2008) Nat Nanotechnol , vol.3 , pp. 512-516
    • Cao, Y.1    Li, H.B.2
  • 34
    • 42649120688 scopus 로고    scopus 로고
    • Protein-protein interaction regulates proteins' mechanical stability
    • Cao Y., Yoo T., Zhuang S.L., Li H.B. Protein-protein interaction regulates proteins' mechanical stability. J Mol Biol 2008, 378:1132-1141.
    • (2008) J Mol Biol , vol.378 , pp. 1132-1141
    • Cao, Y.1    Yoo, T.2    Zhuang, S.L.3    Li, H.B.4
  • 35
  • 36
    • 42149186359 scopus 로고    scopus 로고
    • Solvent molecules bridge the mechanical unfolding transition state of a protein
    • Dougan L., Feng G., Lu H., Fernandez J.M. Solvent molecules bridge the mechanical unfolding transition state of a protein. Proc Natl Acad Sci U S A 2008, 105:3185-3190.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3185-3190
    • Dougan, L.1    Feng, G.2    Lu, H.3    Fernandez, J.M.4
  • 40
    • 33645091911 scopus 로고    scopus 로고
    • Single molecule unzipping of coiled coils: sequence resolved stability profiles
    • Bornschlogl T., Rief M. Single molecule unzipping of coiled coils: sequence resolved stability profiles. Phys Rev Lett 2006, 96:118102.
    • (2006) Phys Rev Lett , vol.96 , pp. 118102
    • Bornschlogl, T.1    Rief, M.2
  • 41
    • 40449108888 scopus 로고    scopus 로고
    • Single-molecule dynamics of mechanical coiled-coil unzipping
    • Bornschlog T., Rief M. Single-molecule dynamics of mechanical coiled-coil unzipping. Langmuir 2008, 24:1338-1342.
    • (2008) Langmuir , vol.24 , pp. 1338-1342
    • Bornschlog, T.1    Rief, M.2
  • 42
    • 70350747497 scopus 로고    scopus 로고
    • Designing the folding mechanics of coiled coils
    • Bornschlogl T., Gebhardt J.C.M., Rief M. Designing the folding mechanics of coiled coils. ChemPhysChem 2009, 10:2800-2804.
    • (2009) ChemPhysChem , vol.10 , pp. 2800-2804
    • Bornschlogl, T.1    Gebhardt, J.C.M.2    Rief, M.3
  • 45
    • 49649083370 scopus 로고    scopus 로고
    • Single molecule force spectroscopy reveals engineered metal chelation is a general approach to enhance mechanical stability of proteins
    • Cao Y., Yoo T., Li H.B. Single molecule force spectroscopy reveals engineered metal chelation is a general approach to enhance mechanical stability of proteins. Proc Natl Acad Sci U S A 2008, 105:11152-11157.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 11152-11157
    • Cao, Y.1    Yoo, T.2    Li, H.B.3
  • 46
    • 41249102384 scopus 로고    scopus 로고
    • Mechanical unfoldons as building blocks of maltose-binding protein
    • Bertz M., Rief M. Mechanical unfoldons as building blocks of maltose-binding protein. J Mol Biol 2008, 378:447-458.
    • (2008) J Mol Biol , vol.378 , pp. 447-458
    • Bertz, M.1    Rief, M.2
  • 47
    • 56049108131 scopus 로고    scopus 로고
    • Stabilization provided by neighboring strands is critical for the mechanical stability of proteins
    • Sharma D., Feng G., Khor D., Genchev G.Z., Lu H., Li H.B. Stabilization provided by neighboring strands is critical for the mechanical stability of proteins. Biophys J 2008, 95:3935-3942.
    • (2008) Biophys J , vol.95 , pp. 3935-3942
    • Sharma, D.1    Feng, G.2    Khor, D.3    Genchev, G.Z.4    Lu, H.5    Li, H.B.6
  • 49
    • 73549110486 scopus 로고    scopus 로고
    • Mechanical strength of 17 134 model proteins and cysteine slipknots
    • Sikora M., Sulkowska J.I., Cieplak M. Mechanical strength of 17 134 model proteins and cysteine slipknots. PLoS Comput Biol 2009, 5:e1000547.
    • (2009) PLoS Comput Biol , vol.5
    • Sikora, M.1    Sulkowska, J.I.2    Cieplak, M.3
  • 50
    • 66149128872 scopus 로고    scopus 로고
    • Mechanical stability and differentially conserved physical-chemical properties of titin Ig-domains
    • Garcia T.I., Oberhauser A.F., Braun W. Mechanical stability and differentially conserved physical-chemical properties of titin Ig-domains. Proteins 2009, 75:706-718.
    • (2009) Proteins , vol.75 , pp. 706-718
    • Garcia, T.I.1    Oberhauser, A.F.2    Braun, W.3
  • 51
    • 61549120107 scopus 로고    scopus 로고
    • The C2 domains of human synaptotagmin 1 have distinct mechanical properties
    • Fuson K.L., Ma L., Sutton R.B., Oberhauser A.F. The C2 domains of human synaptotagmin 1 have distinct mechanical properties. Biophys J 2009, 96:1083-1090.
    • (2009) Biophys J , vol.96 , pp. 1083-1090
    • Fuson, K.L.1    Ma, L.2    Sutton, R.B.3    Oberhauser, A.F.4
  • 52
    • 40849142370 scopus 로고    scopus 로고
    • Elastic bond network model for protein unfolding mechanics
    • Dietz H., Rief M. Elastic bond network model for protein unfolding mechanics. Phys Rev Lett 2008, 100:098101.
    • (2008) Phys Rev Lett , vol.100 , pp. 098101
    • Dietz, H.1    Rief, M.2
  • 53
    • 40549141130 scopus 로고    scopus 로고
    • Predicting the order in which contacts are broken during single molecule protein stretching experiments
    • Sulkowska J.I., Kloczkowski A., Sen T.Z., Cieplak M., Jernigan R.L. Predicting the order in which contacts are broken during single molecule protein stretching experiments. Proteins 2008, 71:45-60.
    • (2008) Proteins , vol.71 , pp. 45-60
    • Sulkowska, J.I.1    Kloczkowski, A.2    Sen, T.Z.3    Cieplak, M.4    Jernigan, R.L.5
  • 54
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless S.W., Ranganathan R. Evolutionarily conserved pathways of energetic connectivity in protein families. Science 1999, 286:295-299.
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 55
    • 63549143744 scopus 로고    scopus 로고
    • Mechanical network in titin immunoglobulin from force distribution analysis
    • Stacklies W., Vega M.C., Wilmanns M., Grater F. Mechanical network in titin immunoglobulin from force distribution analysis. PLoS Comput Biol 2009, 5:e1000306.
    • (2009) PLoS Comput Biol , vol.5
    • Stacklies, W.1    Vega, M.C.2    Wilmanns, M.3    Grater, F.4
  • 56
    • 0042744701 scopus 로고    scopus 로고
    • Mechanical unfolding of a titin Ig domain: structure of transition state revealed by combining atomic force microscopy, protein engineering and molecular dynamics simulations
    • Best R.B., Fowler S.B., Herrera J.L.T., Steward A., Paci E., Clarke J. Mechanical unfolding of a titin Ig domain: structure of transition state revealed by combining atomic force microscopy, protein engineering and molecular dynamics simulations. J Mol Biol 2003, 330:867-877.
    • (2003) J Mol Biol , vol.330 , pp. 867-877
    • Best, R.B.1    Fowler, S.B.2    Herrera, J.L.T.3    Steward, A.4    Paci, E.5    Clarke, J.6
  • 57
    • 52449107719 scopus 로고    scopus 로고
    • An effective strategy for the design of proteins with enhanced mechanical stability
    • Borgia A., Steward A., Clarke J. An effective strategy for the design of proteins with enhanced mechanical stability. Angew Chem Int Ed Engl 2008, 47:6900-6903.
    • (2008) Angew Chem Int Ed Engl , vol.47 , pp. 6900-6903
    • Borgia, A.1    Steward, A.2    Clarke, J.3
  • 58
    • 52949145661 scopus 로고    scopus 로고
    • Recombination of protein fragments: a promising approach toward engineering proteins with novel nanomechanical properties
    • Balamurali M.M., Sharma D., Chang A., Khor D., Chu R., Li H.B. Recombination of protein fragments: a promising approach toward engineering proteins with novel nanomechanical properties. Protein Sci 2008, 17:1815-1826.
    • (2008) Protein Sci , vol.17 , pp. 1815-1826
    • Balamurali, M.M.1    Sharma, D.2    Chang, A.3    Khor, D.4    Chu, R.5    Li, H.B.6
  • 59
    • 58849130229 scopus 로고    scopus 로고
    • Changing the mechanical unfolding pathway of FnIII(10) by tuning the pulling strength
    • Mitternacht S., Luccioli S., Torcini A., Imparato A., Irback A. Changing the mechanical unfolding pathway of FnIII(10) by tuning the pulling strength. Biophys J 2009, 96:429-441.
    • (2009) Biophys J , vol.96 , pp. 429-441
    • Mitternacht, S.1    Luccioli, S.2    Torcini, A.3    Imparato, A.4    Irback, A.5
  • 60
    • 56749155582 scopus 로고    scopus 로고
    • The effects of macromolecular crowding on the mechanical stability of protein molecules
    • Yuan J.M., Chyan C.L., Zhou H.X., Chung T.Y., Peng H.B., Ping G.H., Yang G.L. The effects of macromolecular crowding on the mechanical stability of protein molecules. Protein Sci 2008, 17:2156-2166.
    • (2008) Protein Sci , vol.17 , pp. 2156-2166
    • Yuan, J.M.1    Chyan, C.L.2    Zhou, H.X.3    Chung, T.Y.4    Peng, H.B.5    Ping, G.H.6    Yang, G.L.7
  • 61
    • 61749097701 scopus 로고    scopus 로고
    • Crowding effects on the mechanical stability and unfolding pathways of ubiquitin
    • Pincus D.L., Thirumalai D. Crowding effects on the mechanical stability and unfolding pathways of ubiquitin. J Phys Chem B 2009, 113:359-368.
    • (2009) J Phys Chem B , vol.113 , pp. 359-368
    • Pincus, D.L.1    Thirumalai, D.2
  • 62
    • 44149110851 scopus 로고    scopus 로고
    • Configurational entropy modulates the mechanical stability of protein GB1
    • Li H.B., Wang H.C., Cao Y., Sharma D., Wang M. Configurational entropy modulates the mechanical stability of protein GB1. J Mol Biol 2008, 379:871-880.
    • (2008) J Mol Biol , vol.379 , pp. 871-880
    • Li, H.B.1    Wang, H.C.2    Cao, Y.3    Sharma, D.4    Wang, M.5
  • 63
    • 36348998132 scopus 로고    scopus 로고
    • How do chemical denaturants affect the mechanical folding and unfolding of proteins?
    • Cao Y., Li H. How do chemical denaturants affect the mechanical folding and unfolding of proteins?. J Mol Biol 2008, 375:316-324.
    • (2008) J Mol Biol , vol.375 , pp. 316-324
    • Cao, Y.1    Li, H.2
  • 64
    • 58149356274 scopus 로고    scopus 로고
    • The effect of temperature on mechanical resistance of the native and intermediate states of I27
    • Taniguchi Y., Brockwell D.J., Kawakami M. The effect of temperature on mechanical resistance of the native and intermediate states of I27. Biophys J 2008, 95:5296-5305.
    • (2008) Biophys J , vol.95 , pp. 5296-5305
    • Taniguchi, Y.1    Brockwell, D.J.2    Kawakami, M.3
  • 65
    • 70349624828 scopus 로고    scopus 로고
    • Domain insertion effectively regulates the mechanical unfolding hierarchy of elastomeric proteins: toward engineering multifunctional elastomeric proteins
    • Peng Q., Li H.B. Domain insertion effectively regulates the mechanical unfolding hierarchy of elastomeric proteins: toward engineering multifunctional elastomeric proteins. J Am Chem Soc 2009, 131:14050-14056.
    • (2009) J Am Chem Soc , vol.131 , pp. 14050-14056
    • Peng, Q.1    Li, H.B.2
  • 66
    • 70349386569 scopus 로고    scopus 로고
    • Direct observation of tug-of-war during the folding of a mutually exclusive protein
    • Peng Q., Li H.B. Direct observation of tug-of-war during the folding of a mutually exclusive protein. J Am Chem Soc 2009, 131:13347-13354.
    • (2009) J Am Chem Soc , vol.131 , pp. 13347-13354
    • Peng, Q.1    Li, H.B.2
  • 67
    • 67650331321 scopus 로고    scopus 로고
    • Controlling proteins through molecular springs
    • Zocchi G. Controlling proteins through molecular springs. Annu Rev Biophys 2009, 38:75-88.
    • (2009) Annu Rev Biophys , vol.38 , pp. 75-88
    • Zocchi, G.1
  • 69
    • 77249156811 scopus 로고    scopus 로고
    • PR65, the HEAT-repeat scaffold of phosphatase PP2A, is an elastic connector that links force and catalysis
    • Grinthal A., Adamovic I., Weiner B., Karplus M., Kleckner N. PR65, the HEAT-repeat scaffold of phosphatase PP2A, is an elastic connector that links force and catalysis. Proc Natl Acad Sci U S A 2010, 107:2467-2472.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 2467-2472
    • Grinthal, A.1    Adamovic, I.2    Weiner, B.3    Karplus, M.4    Kleckner, N.5
  • 70
    • 44449085063 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy reveals a stepwise unfolding of Caenorhabditis elegans giant protein kinase domains
    • Greene D.N., Garcia T., Sutton R.B., Gernert K.M., Benian G.M., Oberhauser A.F. Single-molecule force spectroscopy reveals a stepwise unfolding of Caenorhabditis elegans giant protein kinase domains. Biophys J 2008, 95:1360-1370.
    • (2008) Biophys J , vol.95 , pp. 1360-1370
    • Greene, D.N.1    Garcia, T.2    Sutton, R.B.3    Gernert, K.M.4    Benian, G.M.5    Oberhauser, A.F.6
  • 73
    • 27744453306 scopus 로고    scopus 로고
    • Influence of substrate binding on the mechanical stability of mouse dihydrofolate reductase
    • Junker J.P., Hell K., Schlierf M., Neupert W., Rief M. Influence of substrate binding on the mechanical stability of mouse dihydrofolate reductase. Biophys J 2005, 89:L46-L48.
    • (2005) Biophys J , vol.89
    • Junker, J.P.1    Hell, K.2    Schlierf, M.3    Neupert, W.4    Rief, M.5
  • 74
    • 62649138263 scopus 로고    scopus 로고
    • Tightening the knot in phytochrome by single-molecule atomic force microscopy
    • Bornschlogl T., Anstrom D.M., Mey E., Dzubiella J., Rief M., Forest K.T. Tightening the knot in phytochrome by single-molecule atomic force microscopy. Biophys J 2009, 96:1508-1514.
    • (2009) Biophys J , vol.96 , pp. 1508-1514
    • Bornschlogl, T.1    Anstrom, D.M.2    Mey, E.3    Dzubiella, J.4    Rief, M.5    Forest, K.T.6
  • 75
    • 27744581873 scopus 로고    scopus 로고
    • Ligand binding modulates the mechanical stability of dihydrofolate reductase
    • Ainavarapu S.R.K., Li L.Y., Badilla C.L., Fernandez J.M. Ligand binding modulates the mechanical stability of dihydrofolate reductase. Biophys J 2005, 89:3337-3344.
    • (2005) Biophys J , vol.89 , pp. 3337-3344
    • Ainavarapu, S.R.K.1    Li, L.Y.2    Badilla, C.L.3    Fernandez, J.M.4
  • 76
    • 70350034005 scopus 로고    scopus 로고
    • Ligand binding mechanics of maltose binding protein
    • Bertz M., Rief M. Ligand binding mechanics of maltose binding protein. J Mol Biol 2009, 393:1097-1105.
    • (2009) J Mol Biol , vol.393 , pp. 1097-1105
    • Bertz, M.1    Rief, M.2
  • 78
    • 3042660150 scopus 로고    scopus 로고
    • Structure, dynamics, and catalytic function of dihydrofolate reductase
    • Schnell J.R., Dyson H.J., Wright P.E. Structure, dynamics, and catalytic function of dihydrofolate reductase. Annu Rev Biophys Biomol Struct 2004, 33:119-140.
    • (2004) Annu Rev Biophys Biomol Struct , vol.33 , pp. 119-140
    • Schnell, J.R.1    Dyson, H.J.2    Wright, P.E.3
  • 79
    • 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., Perisic O., Peng Q., Cao Y., Lam C., Lu H., Li H.B. Single-molecule force spectroscopy reveals a mechanically stable protein fold and the rational tuning of its mechanical stability. Proc Natl Acad Sci U S A 2007, 104:9278-9283.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 9278-9283
    • Sharma, D.1    Perisic, O.2    Peng, Q.3    Cao, Y.4    Lam, C.5    Lu, H.6    Li, H.B.7
  • 80
    • 67649378405 scopus 로고    scopus 로고
    • Modulating the mechanical stability of extracellular matrix protein Tenascin-C in a controlled and reversible fashion
    • Zhuang S.L., Peng Q., Cao Y., Li H.B. Modulating the mechanical stability of extracellular matrix protein Tenascin-C in a controlled and reversible fashion. J Mol Biol 2009, 390:820-829.
    • (2009) J Mol Biol , vol.390 , pp. 820-829
    • Zhuang, S.L.1    Peng, Q.2    Cao, Y.3    Li, H.B.4
  • 83
    • 0033531109 scopus 로고    scopus 로고
    • Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy
    • Merkel R., Nassoy P., Leung A., Ritchie K., Evans E. Energy landscapes of receptor-ligand bonds explored with dynamic force spectroscopy. Nature 1999, 397:50-53.
    • (1999) Nature , vol.397 , pp. 50-53
    • Merkel, R.1    Nassoy, P.2    Leung, A.3    Ritchie, K.4    Evans, E.5
  • 84
    • 1842477478 scopus 로고    scopus 로고
    • Collective and single-molecule interactions of alpha(5)beta(1) integrins
    • Kokkoli E., Ochsenhirt S.E., Tirrell M. Collective and single-molecule interactions of alpha(5)beta(1) integrins. Langmuir 2004, 20:2397-2404.
    • (2004) Langmuir , vol.20 , pp. 2397-2404
    • Kokkoli, E.1    Ochsenhirt, S.E.2    Tirrell, M.3
  • 86
    • 74249119695 scopus 로고    scopus 로고
    • Reduction of the damping on an AFM cantilever in fluid by the use of micropillars
    • Kawakami M., Taniguchi Y., Hiratsuka Y., Shimoike M., Smith D.A. Reduction of the damping on an AFM cantilever in fluid by the use of micropillars. Langmuir 2010, 26:1002-1007.
    • (2010) Langmuir , vol.26 , pp. 1002-1007
    • Kawakami, M.1    Taniguchi, Y.2    Hiratsuka, Y.3    Shimoike, M.4    Smith, D.A.5
  • 87
    • 59149096062 scopus 로고    scopus 로고
    • Ligand-dependent equilibrium fluctuations of single calmodulin molecules
    • Junker J.P., Ziegler F., Rief M. Ligand-dependent equilibrium fluctuations of single calmodulin molecules. Science 2009, 323:633-637.
    • (2009) Science , vol.323 , pp. 633-637
    • Junker, J.P.1    Ziegler, F.2    Rief, M.3
  • 88
    • 36849080807 scopus 로고    scopus 로고
    • Direct observation of active protein folding using lock-in force spectroscopy
    • Schlierf M., Berkemeier F., Rief M. Direct observation of active protein folding using lock-in force spectroscopy. Biophys J 2007, 93:3989-3998.
    • (2007) Biophys J , vol.93 , pp. 3989-3998
    • Schlierf, M.1    Berkemeier, F.2    Rief, M.3
  • 89
    • 25444512161 scopus 로고    scopus 로고
    • Direct observation of the three-state folding of a single protein molecule
    • Cecconi C., Shank E.A., Bustamante C., Marqusee S. Direct observation of the three-state folding of a single protein molecule. Science 2005, 309:2057-2060.
    • (2005) Science , vol.309 , pp. 2057-2060
    • Cecconi, C.1    Shank, E.A.2    Bustamante, C.3    Marqusee, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.