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Volumn 588, Issue 19, 2014, Pages 3613-3620

Force spectroscopy studies on protein-ligand interactions: A single protein mechanics perspective

Author keywords

Binding assay; Force spectroscopy; Mechanical stability; Protein unfolding; Protein ligand interaction

Indexed keywords

CHAPERONIN 60; EARLY PREGNANCY FACTOR; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; LIGAND; PROTEIN;

EID: 84907808419     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2014.04.009     Document Type: Review
Times cited : (44)

References (51)
  • 2
    • 33847273015 scopus 로고    scopus 로고
    • Force denaturation of proteins - An unfolding story
    • D.J. Brockwell Force denaturation of proteins - an unfolding story Curr. Nanosci. 3 2007 3 15
    • (2007) Curr. Nanosci. , vol.3 , pp. 3-15
    • Brockwell, D.J.1
  • 3
    • 49449106310 scopus 로고    scopus 로고
    • Engineered elastomeric proteins with dual elasticity can be controlled by a molecular regulator
    • Y. Cao, and H.B. Li Engineered elastomeric proteins with dual elasticity can be controlled by a molecular regulator Nat. Nanotechnol. 3 2008 512 516
    • (2008) Nat. Nanotechnol. , vol.3 , pp. 512-516
    • Cao, Y.1    Li, H.B.2
  • 4
    • 84873525793 scopus 로고    scopus 로고
    • Force as a single molecule probe of multidimensional protein energy landscapes
    • G. Zoldak, and M. Rief Force as a single molecule probe of multidimensional protein energy landscapes Curr. Opin. Struct. Biol. 23 2013 48 57
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 48-57
    • Zoldak, G.1    Rief, M.2
  • 5
    • 84859769391 scopus 로고    scopus 로고
    • Stretching single polysaccharides and proteins using atomic force microscopy
    • P.E. Marszalek, and Y.F. Dufrene Stretching single polysaccharides and proteins using atomic force microscopy Chem. Soc. Rev. 41 2012 3523 3534
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 3523-3534
    • Marszalek, P.E.1    Dufrene, Y.F.2
  • 6
    • 70349885458 scopus 로고    scopus 로고
    • Force and function: Probing proteins with AFM-based force spectroscopy
    • E.M. Puchner, and H.E. Gaub Force and function: probing proteins with AFM-based force spectroscopy Curr. Opin. Struct. Biol. 19 2009 605 614
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 605-614
    • Puchner, E.M.1    Gaub, H.E.2
  • 8
    • 84862839278 scopus 로고    scopus 로고
    • Single molecule force spectroscopy using polyproteins
    • T. Hoffmann, and L. Dougan Single molecule force spectroscopy using polyproteins Chem. Soc. Rev. 41 2012 4781 4796
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 4781-4796
    • Hoffmann, T.1    Dougan, L.2
  • 10
    • 85042774432 scopus 로고    scopus 로고
    • Protein Nanomechanics
    • D. Andrews, G. Scholes, G. Wiederrecht, Academic Press
    • H. Li Protein Nanomechanics D. Andrews, G. Scholes, G. Wiederrecht, Comprehensive Nanoscience and Technology 2011 Academic Press 227 261
    • (2011) Comprehensive Nanoscience and Technology , pp. 227-261
    • Li, H.1
  • 11
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • M.R. Arkin, and J.A. Wells Small-molecule inhibitors of protein-protein interactions: progressing towards the dream Nat. Rev. Drug Discovery 3 2004 301 317
    • (2004) Nat. Rev. Drug Discovery , vol.3 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 12
    • 20344370764 scopus 로고    scopus 로고
    • Allosteric mechanisms of signal transduction
    • J.P. Changeux, and S.J. Edelstein Allosteric mechanisms of signal transduction Science 308 2005 1424 1428
    • (2005) Science , vol.308 , pp. 1424-1428
    • Changeux, J.P.1    Edelstein, S.J.2
  • 13
  • 14
    • 0021100265 scopus 로고
    • Thermodynamics of the binding of l-arabinose and of d-galactose to the l-arabinose-binding protein of Escherichia coli
    • H. Fukada, J.M. Sturtevant, and F.A. Quiocho Thermodynamics of the binding of l-arabinose and of d-galactose to the l-arabinose-binding protein of Escherichia coli J. Biol. Chem. 258 1983 13193 13198
    • (1983) J. Biol. Chem. , vol.258 , pp. 13193-13198
    • Fukada, H.1    Sturtevant, J.M.2    Quiocho, F.A.3
  • 15
    • 33846622066 scopus 로고    scopus 로고
    • Ligand effects on protein thermodynamic stability
    • J.M. Sanchez-Ruiz Ligand effects on protein thermodynamic stability Biophys. Chem. 126 2007 43 49
    • (2007) Biophys. Chem. , vol.126 , pp. 43-49
    • Sanchez-Ruiz, J.M.1
  • 16
    • 33646839120 scopus 로고    scopus 로고
    • Characterization of protein-ligand interaction sites using experimental and computational methods
    • S. Vajda, and F. Guarnieri Characterization of protein-ligand interaction sites using experimental and computational methods Curr. Opin. Drug Discovery Dev. 9 2006 354 362
    • (2006) Curr. Opin. Drug Discovery Dev. , vol.9 , pp. 354-362
    • Vajda, S.1    Guarnieri, F.2
  • 17
    • 1542787841 scopus 로고    scopus 로고
    • Label-free screening of bio-molecular interactions
    • M.A. Cooper Label-free screening of bio-molecular interactions Anal. Bioanal. Chem. 377 2003 834 842
    • (2003) Anal. Bioanal. Chem. , vol.377 , pp. 834-842
    • Cooper, M.A.1
  • 18
    • 13844277017 scopus 로고    scopus 로고
    • New methodologies for measuring protein interactions in vivo and in vitro
    • J. Piehler New methodologies for measuring protein interactions in vivo and in vitro Curr. Opin. Struct. Biol. 15 2005 4 14
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 4-14
    • Piehler, J.1
  • 20
    • 59149096062 scopus 로고    scopus 로고
    • Ligand-dependent equilibrium fluctuations of single calmodulin molecules
    • J.P. Junker, F. Ziegler, and M. Rief Ligand-dependent equilibrium fluctuations of single calmodulin molecules Science 323 2009 633 637
    • (2009) Science , vol.323 , pp. 633-637
    • Junker, J.P.1    Ziegler, F.2    Rief, M.3
  • 21
    • 0034979287 scopus 로고    scopus 로고
    • Probing the relation between force-lifetime-and chemistry in single molecular bonds
    • E. Evans Probing the relation between force-lifetime-and chemistry in single molecular bonds Annu. Rev. Biophys. Biomol. Struct. 30 2001 105 128
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 105-128
    • Evans, E.1
  • 23
    • 27744581873 scopus 로고    scopus 로고
    • Ligand binding modulates the mechanical stability of dihydrofolate reductase
    • R.K. Ainavarapu, L.Y. Li, C.L. Badilla, and J.M. Fernandez Ligand binding modulates the mechanical stability of dihydrofolate reductase Biophys. J. 89 2005 3337 3344
    • (2005) Biophys. J. , vol.89 , pp. 3337-3344
    • Ainavarapu, R.K.1    Li, L.Y.2    Badilla, C.L.3    Fernandez, J.M.4
  • 24
    • 27744453306 scopus 로고    scopus 로고
    • Influence of substrate binding on the mechanical stability of mouse dihydrofolate reductase
    • J.P. Junker, K. Hell, M. Schlierf, W. Neupert, and M. Rief Influence of substrate binding on the mechanical stability of mouse dihydrofolate reductase Biophys. J. 89 2005 L46 L48
    • (2005) Biophys. J. , vol.89 , pp. 46-L48
    • Junker, J.P.1    Hell, K.2    Schlierf, M.3    Neupert, W.4    Rief, M.5
  • 25
    • 35648958777 scopus 로고    scopus 로고
    • A functional single-molecule binding assay via force spectroscopy
    • Y. Cao, M.M. Balamurali, D. Sharma, and H. Li A functional single-molecule binding assay via force spectroscopy Proc. Natl. Acad. Sci. U.S.A. 104 2007 15677 15681
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 15677-15681
    • Cao, Y.1    Balamurali, M.M.2    Sharma, D.3    Li, H.4
  • 26
    • 42649120688 scopus 로고    scopus 로고
    • Protein-protein interaction regulates proteins' mechanical stability
    • Y. Cao, T. Yoo, S. Zhuang, and H. Li Protein-protein interaction regulates proteins' mechanical stability J. Mol. Biol. 378 2008 1132 1141
    • (2008) J. Mol. Biol. , vol.378 , pp. 1132-1141
    • Cao, Y.1    Yoo, T.2    Zhuang, S.3    Li, H.4
  • 27
    • 0022384947 scopus 로고
    • Protein G: A powerful tool for binding and detection of monoclonal and polyclonal antibodies
    • B. Akerstrom, T. Brodin, K. Reis, and L. Bjorck Protein G: a powerful tool for binding and detection of monoclonal and polyclonal antibodies J. Immunol. 135 1985 2589 2592
    • (1985) J. Immunol. , vol.135 , pp. 2589-2592
    • Akerstrom, B.1    Brodin, T.2    Reis, K.3    Bjorck, L.4
  • 28
    • 0022535330 scopus 로고
    • Detection and purification of rat and goat immunoglobulin G antibodies using protein G-based solid-phase radioimmunoassays
    • B. Nilson, L. Bjorck, and B. Akerstrom Detection and purification of rat and goat immunoglobulin G antibodies using protein G-based solid-phase radioimmunoassays J. Immunol. Methods 91 1986 275 281
    • (1986) J. Immunol. Methods , vol.91 , pp. 275-281
    • Nilson, B.1    Bjorck, L.2    Akerstrom, B.3
  • 30
    • 70350034005 scopus 로고    scopus 로고
    • Ligand binding mechanics of maltose binding protein
    • M. Bertz, and M. Rief Ligand binding mechanics of maltose binding protein J. Mol. Biol. 393 2009 1097 1105
    • (2009) J. Mol. Biol. , vol.393 , pp. 1097-1105
    • Bertz, M.1    Rief, M.2
  • 31
    • 69449083856 scopus 로고    scopus 로고
    • The titin-telethonin complex is a directed, superstable molecular bond in the muscle Z-disk
    • M. Bertz, M. Wilmanns, and M. Rief The titin-telethonin complex is a directed, superstable molecular bond in the muscle Z-disk Proc. Natl. Acad. Sci. U.S.A. 106 2009 13307 133310
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 13307-133310
    • Bertz, M.1    Wilmanns, M.2    Rief, M.3
  • 32
    • 49649083370 scopus 로고    scopus 로고
    • Single molecule force spectroscopy reveals engineered metal chelation is a general approach to enhance mechanical stability of proteins
    • Y. Cao, T. Yoo, and H. Li 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. 105 2008 11152 11157
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 11152-11157
    • Cao, Y.1    Yoo, T.2    Li, H.3
  • 33
    • 70149120516 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy distinguishes target binding modes of calmodulin
    • J.P. Junker, and M. Rief Single-molecule force spectroscopy distinguishes target binding modes of calmodulin Proc. Natl. Acad. Sci. U.S.A. 106 2009 14361 14366
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 14361-14366
    • Junker, J.P.1    Rief, M.2
  • 34
    • 79953183005 scopus 로고    scopus 로고
    • Nanomechanics of the cadherin ectodomain: "canalization" by Ca2+ binding results in a new mechanical element
    • J. Oroz, A. Valbuena, A.M. Vera, J. Mendieta, P. Gomez-Puertas, and M. Carrion-Vazquez Nanomechanics of the cadherin ectodomain: "canalization" by Ca2+ binding results in a new mechanical element J. Biol. Chem. 286 2011 9405 9418
    • (2011) J. Biol. Chem. , vol.286 , pp. 9405-9418
    • Oroz, J.1    Valbuena, A.2    Vera, A.M.3    Mendieta, J.4    Gomez-Puertas, P.5    Carrion-Vazquez, M.6
  • 35
    • 84873492994 scopus 로고    scopus 로고
    • Effects of ligand binding on the mechanical properties of ankyrin repeat protein gankyrin
    • G. Settanni, D. Serquera, P.E. Marszalek, E. Paci, and L.S. Itzhaki Effects of ligand binding on the mechanical properties of ankyrin repeat protein gankyrin PLoS Comput. Biol. 9 2013 e1002864
    • (2013) PLoS Comput. Biol. , vol.9 , pp. 1002864
    • Settanni, G.1    Serquera, D.2    Marszalek, P.E.3    Paci, E.4    Itzhaki, L.S.5
  • 36
    • 79951828755 scopus 로고    scopus 로고
    • Inhibitor binding increases the mechanical stability of staphylococcal nuclease
    • C.C. Wang, T.Y. Tsong, Y.H. Hsu, and P.E. Marszalek Inhibitor binding increases the mechanical stability of staphylococcal nuclease Biophys. J. 100 2011 1094 1099
    • (2011) Biophys. J. , vol.100 , pp. 1094-1099
    • Wang, C.C.1    Tsong, T.Y.2    Hsu, Y.H.3    Marszalek, P.E.4
  • 37
    • 84879411505 scopus 로고    scopus 로고
    • Altered mechanical properties of titin immunoglobulin domain 27 in the presence of calcium
    • M.M. DuVall, J.L. Gifford, M. Amrein, and W. Herzog Altered mechanical properties of titin immunoglobulin domain 27 in the presence of calcium Eur. Biophys. J. 42 2013 301 307
    • (2013) Eur. Biophys. J. , vol.42 , pp. 301-307
    • Duvall, M.M.1    Gifford, J.L.2    Amrein, M.3    Herzog, W.4
  • 39
    • 84870896671 scopus 로고    scopus 로고
    • Cholesterol increases kinetic, energetic, and mechanical stability of the human beta2-adrenergic receptor
    • M. Zocher, C. Zhang, S.G. Rasmussen, B.K. Kobilka, and D.J. Muller Cholesterol increases kinetic, energetic, and mechanical stability of the human beta2-adrenergic receptor Proc. Natl. Acad. Sci. U.S.A. 109 2012 E3463 E3472
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 3463-E3472
    • Zocher, M.1    Zhang, C.2    Rasmussen, S.G.3    Kobilka, B.K.4    Muller, D.J.5
  • 40
    • 67649378405 scopus 로고    scopus 로고
    • Modulating the mechanical stability of extracellular matrix protein tenascin-C in a controlled and reversible fashion
    • S. Zhuang, Q. Peng, Y. Cao, and H. Li Modulating the mechanical stability of extracellular matrix protein tenascin-C in a controlled and reversible fashion J. Mol. Biol. 390 2009 820 829
    • (2009) J. Mol. Biol. , vol.390 , pp. 820-829
    • Zhuang, S.1    Peng, Q.2    Cao, Y.3    Li, H.4
  • 41
    • 41249102384 scopus 로고    scopus 로고
    • Mechanical unfoldons as building blocks of maltose-binding protein
    • M. Bertz, and M. Rief Mechanical unfoldons as building blocks of maltose-binding protein J. Mol. Biol. 378 2008 447 458
    • (2008) J. Mol. Biol. , vol.378 , pp. 447-458
    • Bertz, M.1    Rief, M.2
  • 43
    • 84869051278 scopus 로고    scopus 로고
    • Variation in the mechanical unfolding pathway of p53DBD induced by interaction with p53 N-terminal region or DNA
    • Y. Taniguchi, and M. Kawakami Variation in the mechanical unfolding pathway of p53DBD induced by interaction with p53 N-terminal region or DNA PLoS One 7 2012 e49003
    • (2012) PLoS One , vol.7 , pp. 49003
    • Taniguchi, Y.1    Kawakami, M.2
  • 44
    • 84885124147 scopus 로고    scopus 로고
    • Multiple unfolding pathways of leucine binding protein (LBP) probed by single-molecule force spectroscopy (SMFS)
    • H.C. Kotamarthi, R. Sharma, S. Narayan, S. Ray, and S.R. Ainavarapu Multiple unfolding pathways of leucine binding protein (LBP) probed by single-molecule force spectroscopy (SMFS) J. Am. Chem. Soc. 135 2013 14768 14774
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 14768-14774
    • Kotamarthi, H.C.1    Sharma, R.2    Narayan, S.3    Ray, S.4    Ainavarapu, S.R.5
  • 46
    • 0036005637 scopus 로고    scopus 로고
    • Role of cofactors in protein folding
    • P. Wittung-Stafshede Role of cofactors in protein folding Acc. Chem. Res. 35 2002 201 208
    • (2002) Acc. Chem. Res. , vol.35 , pp. 201-208
    • Wittung-Stafshede, P.1
  • 47
    • 80054679425 scopus 로고    scopus 로고
    • Dynamics of protein folding and cofactor binding monitored by single-molecule force spectroscopy
    • Y. Cao, and H. Li Dynamics of protein folding and cofactor binding monitored by single-molecule force spectroscopy Biophys. J. 101 2011 2009 2017
    • (2011) Biophys. J. , vol.101 , pp. 2009-2017
    • Cao, Y.1    Li, H.2
  • 48
    • 67650069571 scopus 로고    scopus 로고
    • A force-spectroscopy-based single-molecule metal-binding assay
    • Y. Cao, K.S. Er, R. Parhar, and H. Li A force-spectroscopy-based single-molecule metal-binding assay Chemphyschem 10 2009 1450 1454
    • (2009) Chemphyschem , vol.10 , pp. 1450-1454
    • Cao, Y.1    Er, K.S.2    Parhar, R.3    Li, H.4
  • 49
    • 79959673671 scopus 로고    scopus 로고
    • Enhancing the mechanical stability of proteins through a cocktail approach
    • Y. Cao, Y.D. Li, and H. Li Enhancing the mechanical stability of proteins through a cocktail approach Biophys. J. 100 2011 1794 1799
    • (2011) Biophys. J. , vol.100 , pp. 1794-1799
    • Cao, Y.1    Li, Y.D.2    Li, H.3
  • 50
    • 0025730892 scopus 로고
    • Engineered metal-binding proteins: Purification to protein folding
    • F.H. Arnold, and B.L. Haymore Engineered metal-binding proteins: purification to protein folding Science 252 1991 1796 1797
    • (1991) Science , vol.252 , pp. 1796-1797
    • Arnold, F.H.1    Haymore, B.L.2
  • 51
    • 14744283294 scopus 로고
    • Protein stabilization by engineered metal chelation
    • J.T. Kellis Jr., R.J. Todd, and F.H. Arnold Protein stabilization by engineered metal chelation Biotechnology (N Y) 9 1991 994 995
    • (1991) Biotechnology (N Y) , vol.9 , pp. 994-995
    • Kellis, J.T.1    Todd, R.J.2    Arnold, F.H.3


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