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Volumn 91, Issue 1, 2015, Pages

Optimizing the calculation of energy landscape parameters from single-molecule protein unfolding experiments

Author keywords

[No Author keywords available]

Indexed keywords

ATOMIC FORCE MICROSCOPY; BELLS; INTELLIGENT SYSTEMS; MOLECULES; PROBABILITY; PROBABILITY DISTRIBUTIONS; PROTEINS;

EID: 84921849612     PISSN: 15393755     EISSN: 15502376     Source Type: Journal    
DOI: 10.1103/PhysRevE.91.012710     Document Type: Article
Times cited : (13)

References (64)
  • 1
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • SCIEAS 0036-8075
    • M. Rief, M. Gautel, F. Oesterhelt, J. Fernandez, and H. Gaub, Reversible unfolding of individual titin immunoglobulin domains by AFM, Science 276, 1109 (1997). SCIEAS 0036-8075 10.1126/science.276.5315.1109
    • (1997) Science , vol.276 , pp. 1109
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.4    Gaub, H.5
  • 2
    • 50649092124 scopus 로고    scopus 로고
    • Single-molecule studies of protein folding
    • ARBOAW 0066-4154
    • A. Borgia, P. M. Williams, and J. Clarke, Single-molecule studies of protein folding, Annu. Rev. Biochem. 77, 101 (2008). ARBOAW 0066-4154 10.1146/annurev.biochem.77.060706.093102
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 101
    • Borgia, A.1    Williams, P.M.2    Clarke, J.3
  • 3
    • 77957269559 scopus 로고    scopus 로고
    • Single-molecule derivation of salt dependent base-pair free energies in DNA
    • PNASA6 0027-8424
    • J. Huguet, C. Bizarro, N. R. Forns, S. Smith, C. Bustamante, and F. Ritort, Single-molecule derivation of salt dependent base-pair free energies in DNA, Proc. Natl. Acad. Sci. USA 107, 15431 (2010). PNASA6 0027-8424 10.1073/pnas.1001454107
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 15431
    • Huguet, J.1    Bizarro, C.2    Forns, N.R.3    Smith, S.4    Bustamante, C.5    Ritort, F.6
  • 4
    • 84862839278 scopus 로고    scopus 로고
    • Single molecule force spectroscopy using polyproteins
    • 0306-0012
    • T. Hoffmann and L. Dougan, Single molecule force spectroscopy using polyproteins, Chem. Soc. Rev. 41, 4781 (2012). 0306-0012 10.1039/c2cs35033e
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 4781
    • Hoffmann, T.1    Dougan, L.2
  • 5
    • 84865514087 scopus 로고    scopus 로고
    • Single molecule force spectroscopy reveals critical roles of hydrophobic core packing in determining the mechanical stability of protein GB1
    • LANGD5 0743-7463
    • T. Bu, H.-C. E. Wang, and H. Li, Single molecule force spectroscopy reveals critical roles of hydrophobic core packing in determining the mechanical stability of protein GB1, Langmuir 28, 12319 (2012). LANGD5 0743-7463 10.1021/la301940g
    • (2012) Langmuir , vol.28 , pp. 12319
    • Bu, T.1    Wang, H.-C.E.2    Li, H.3
  • 6
    • 84878119770 scopus 로고    scopus 로고
    • Single-molecule studies on polysumo proteins reveal their mechanical flexibility
    • BIOJAU 0006-3495
    • H. C. Kotamarthi, R. Sharma, and S. R. K. Ainavarapu, Single-molecule studies on polysumo proteins reveal their mechanical flexibility, Biophys. J. 104, 2273 (2013). BIOJAU 0006-3495 10.1016/j.bpj.2013.04.008
    • (2013) Biophys. J. , vol.104 , pp. 2273
    • Kotamarthi, H.C.1    Sharma, R.2    Ainavarapu, S.R.K.3
  • 7
    • 84873525793 scopus 로고    scopus 로고
    • Force as a single molecule probe of multidimensional protein energy landscapes
    • COSBEF 0959-440X
    • G. Zoldak and M. Rief, Force as a single molecule probe of multidimensional protein energy landscapes, Curr. Opin. Struct. Biol. 23, 48 (2013). COSBEF 0959-440X 10.1016/j.sbi.2012.11.007
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 48
    • Zoldak, G.1    Rief, M.2
  • 8
    • 84859769391 scopus 로고    scopus 로고
    • Stretching single polysaccharides and proteins using atomic force microscopy
    • 0306-0012
    • P. E. Marszalek and Y. F. Dufrêne, Stretching single polysaccharides and proteins using atomic force microscopy, Chem. Soc. Rev. 41, 3523 (2012). 0306-0012 10.1039/c2cs15329g
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 3523
    • Marszalek, P.E.1    Dufrêne, Y.F.2
  • 9
    • 84873914964 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy identifies a small cold shock protein as being mechanically robust
    • JPCBFK 1520-6106
    • T. Hoffmann, K. Tych, D. Brockwell, and L. Dougan, Single-molecule force spectroscopy identifies a small cold shock protein as being mechanically robust, J. Phys. Chem. B 117, 1819 (2013). JPCBFK 1520-6106 10.1021/jp310442s
    • (2013) J. Phys. Chem. B , vol.117 , pp. 1819
    • Hoffmann, T.1    Tych, K.2    Brockwell, D.3    Dougan, L.4
  • 10
    • 84883435959 scopus 로고    scopus 로고
    • Single molecule force spectroscopy reveals the temperature-dependent robustness and malleability of a hyperthermophilic protein
    • 1744-683X 10.1039/c3sm51439k
    • K. Tych, T. Hoffmann, D. Brockwell, and L. Dougan, Single molecule force spectroscopy reveals the temperature-dependent robustness and malleability of a hyperthermophilic protein, Soft Matter 9, 9016 (2013). 1744-683X 10.1039/c3sm51439k
    • (2013) Soft Matter , vol.9 , pp. 9016
    • Tych, K.1    Hoffmann, T.2    Brockwell, D.3    Dougan, L.4
  • 12
    • 0042335817 scopus 로고    scopus 로고
    • Specific binding of the regulatory protein expg to promoter regions of the galactoglucan biosynthesis gene cluster of sinorhizobium meliloti-A combined molecular biology and force spectroscopy investigation
    • JSBIEM 1047-8477
    • F. Bartels, B. Baumgarth, D. Anselmetti, R. Ros, and A. Becker, Specific binding of the regulatory protein expg to promoter regions of the galactoglucan biosynthesis gene cluster of sinorhizobium meliloti-a combined molecular biology and force spectroscopy investigation, J. Struct. Biol. 143, 145 (2003). JSBIEM 1047-8477 10.1016/S1047-8477(03)00127-8
    • (2003) J. Struct. Biol. , vol.143 , pp. 145
    • Bartels, F.1    Baumgarth, B.2    Anselmetti, D.3    Ros, R.4    Becker, A.5
  • 13
    • 38349086420 scopus 로고    scopus 로고
    • Energy landscape roughness of the streptavidin-biotin interaction
    • 0952-3499
    • F. Rico and V. Moy, Energy landscape roughness of the streptavidin-biotin interaction, J. Mol. Recog. 20, 495 (2007). 0952-3499 10.1002/jmr.841
    • (2007) J. Mol. Recog. , vol.20 , pp. 495
    • Rico, F.1    Moy, V.2
  • 14
    • 84907808419 scopus 로고    scopus 로고
    • Force spectroscopy studies on protein-ligand interactions: A single protein mechanics perspective
    • X. Hu and H. Li, Force spectroscopy studies on protein-ligand interactions: A single protein mechanics perspective, FEBS Lett. 588, 3613 (2014). 10.1016/j.febslet.2014.04.009
    • (2014) FEBS Lett. , vol.588 , pp. 3613
    • Hu, X.1    Li, H.2
  • 15
    • 84885124147 scopus 로고    scopus 로고
    • Multiple unfolding pathways of leucine binding protein (LBP) probed by single-molecule force spectroscopy (SMFS)
    • JACSAT 0002-7863
    • H. C. Kotamarthi, R. Sharma, S. Narayan, S. Ray, and S. R. K. Ainavarapu, Multiple unfolding pathways of leucine binding protein (LBP) probed by single-molecule force spectroscopy (SMFS), J. Am. Chem. Soc. 135, 14768 (2013). JACSAT 0002-7863 10.1021/ja406238q
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 14768
    • Kotamarthi, H.C.1    Sharma, R.2    Narayan, S.3    Ray, S.4    Ainavarapu, S.R.K.5
  • 16
    • 84869051278 scopus 로고    scopus 로고
    • Variation in the mechanical unfolding pathway of p53DBD induced by interaction with p53 N-terminal region or DNA
    • 1932-6203
    • 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, e49003 (2012). 1932-6203 10.1371/journal.pone.0049003
    • (2012) PLoS ONE , vol.7 , pp. e49003
    • Taniguchi, Y.1    Kawakami, M.2
  • 17
    • 59149096062 scopus 로고    scopus 로고
    • Ligand-dependent equilibrium fluctuations of single calmodulin molecules
    • SCIEAS 0036-8075
    • J. P. Junker, F. Ziegler, and M. Rief, Ligand-dependent equilibrium fluctuations of single calmodulin molecules, Science 323, 633 (2009). SCIEAS 0036-8075 10.1126/science.1166191
    • (2009) Science , vol.323 , pp. 633
    • Junker, J.P.1    Ziegler, F.2    Rief, M.3
  • 18
    • 35648958777 scopus 로고    scopus 로고
    • A functional single-molecule binding assay via force spectroscopy
    • PNASA6 0027-8424
    • Y. Cao, M. M. Balamurali, D. Sharma, and H. Li, A functional single-molecule binding assay via force spectroscopy, Proc. Natl. Acad. Sci. USA 104, 15677 (2007). PNASA6 0027-8424 10.1073/pnas.0705367104
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 15677
    • Cao, Y.1    Balamurali, M.M.2    Sharma, D.3    Li, H.4
  • 19
    • 70349885458 scopus 로고    scopus 로고
    • Force and function: Probing proteins with afm-based force spectroscopy
    • COSBEF 0959-440X
    • E. M. Puchner and H. E. Gaub, Force and function: probing proteins with afm-based force spectroscopy, Curr. Opin. Struct. Biol. 19, 605 (2009). COSBEF 0959-440X 10.1016/j.sbi.2009.09.005
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 605
    • Puchner, E.M.1    Gaub, H.E.2
  • 20
    • 0034069612 scopus 로고    scopus 로고
    • Single-molecule studies of dna mechanics
    • COSBEF 0959-440X
    • C. Bustamante, S. Smith, J. Liphardt, and D. Smith, Single-molecule studies of dna mechanics, Curr. Opin. Struct. Biol. 10, 279 (2000). COSBEF 0959-440X 10.1016/S0959-440X(00)00085-3
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 279
    • Bustamante, C.1    Smith, S.2    Liphardt, J.3    Smith, D.4
  • 21
    • 0036111913 scopus 로고    scopus 로고
    • Magnetic tweezers: Micromanipulation and force measurement at the molecular level
    • BIOJAU 0006-3495
    • C. Gosse and V. Croquette, Magnetic tweezers: Micromanipulation and force measurement at the molecular level, Biophys. J. 82, 3314 (2002). BIOJAU 0006-3495 10.1016/S0006-3495(02)75672-5
    • (2002) Biophys. J. , vol.82 , pp. 3314
    • Gosse, C.1    Croquette, V.2
  • 22
    • 44449087047 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy: Optical tweezers, magnetic tweezers and atomic force microscopy
    • 1548-7091
    • K. Neuman and A. Nagy, Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy, Nat. Meth. 5, 491 (2008). 1548-7091 10.1038/nmeth.1218
    • (2008) Nat. Meth. , vol.5 , pp. 491
    • Neuman, K.1    Nagy, A.2
  • 23
    • 0029062769 scopus 로고
    • Sensitive force technique to probe molecular adhesion and structural linkages at biological interfaces
    • BIOJAU 0006-3495
    • E. Evans, K. Ritchie, and R. Merkel, Sensitive force technique to probe molecular adhesion and structural linkages at biological interfaces, Biophys. J. 68, 2580 (1995). BIOJAU 0006-3495 10.1016/S0006-3495(95)80441-8
    • (1995) Biophys. J. , vol.68 , pp. 2580
    • Evans, E.1    Ritchie, K.2    Merkel, R.3
  • 26
    • 31944436148 scopus 로고    scopus 로고
    • Protein structure by mechanical triangulation
    • PNASA6 0027-8424
    • H. Dietz and M. Rief, Protein structure by mechanical triangulation, Proc. Natl. Acad. Sci. USA 103, 1244 (2006). PNASA6 0027-8424 10.1073/pnas.0509217103
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 1244
    • Dietz, H.1    Rief, M.2
  • 27
    • 79958179287 scopus 로고    scopus 로고
    • Facile method of constructing polyproteins for single-molecule force spectroscopy studies
    • LANGD5 0743-7463
    • P. Zheng, Y. Cao, and H. Li, Facile method of constructing polyproteins for single-molecule force spectroscopy studies, Langmuir 27, 5713 (2011). LANGD5 0743-7463 10.1021/la200915d
    • (2011) Langmuir , vol.27 , pp. 5713
    • Zheng, P.1    Cao, Y.2    Li, H.3
  • 29
    • 0346668262 scopus 로고    scopus 로고
    • Force mode atomic force microscopy as a tool for protein folding studies
    • ACACAM 0003-2670
    • R. Best, D. Brockwell, J. L. Toca-Herrera, A. Blake, D. Smith, S. Radford, and J. Clarke, Force mode atomic force microscopy as a tool for protein folding studies, Anal. Chim. Acta 479, 87 (2003). ACACAM 0003-2670 10.1016/S0003-2670(02)01572-6
    • (2003) Anal. Chim. Acta , vol.479 , pp. 87
    • Best, R.1    Brockwell, D.2    Toca-Herrera, J.L.3    Blake, A.4    Smith, D.5    Radford, S.6    Clarke, J.7
  • 30
    • 34848909232 scopus 로고    scopus 로고
    • Force-clamp spectroscopy of single-protein monomers reveals the individual unfolding and folding pathways of i27 and ubiquitin
    • BIOJAU 0006-3495
    • S. Garcia-Manyes, J. Brujic, C. Badilla, and J. Fernandez, Force-clamp spectroscopy of single-protein monomers reveals the individual unfolding and folding pathways of i27 and ubiquitin, Biophys. J. 93, 2436 (2007). BIOJAU 0006-3495 10.1529/biophysj.107.104422
    • (2007) Biophys. J. , vol.93 , pp. 2436
    • Garcia-Manyes, S.1    Brujic, J.2    Badilla, C.3    Fernandez, J.4
  • 31
    • 34147138772 scopus 로고    scopus 로고
    • Dwell-time distribution analysis of polyprotein unfolding using force-clamp spectroscopy
    • BIOJAU 0006-3495
    • J. Brujić, R. Hermans, S. Garcia-Manyes, K. Walther, and J. Fernandez, Dwell-time distribution analysis of polyprotein unfolding using force-clamp spectroscopy, Biophys. J. 92, 2896 (2007). BIOJAU 0006-3495 10.1529/biophysj.106.099481
    • (2007) Biophys. J. , vol.92 , pp. 2896
    • Brujić, J.1    Hermans, R.2    Garcia-Manyes, S.3    Walther, K.4    Fernandez, J.5
  • 32
    • 70349233748 scopus 로고    scopus 로고
    • Identification of a mechanical rheostat in the hydrophobic core of protein l
    • JMOBAK 0022-2836
    • D. Sadler, E. Petrik, Y. Taniguchi, J. Pullen, M. Kawakami, S. Radford, and D. Brockwell, Identification of a mechanical rheostat in the hydrophobic core of protein l, J. Mol. Biol. 393, 237 (2009). JMOBAK 0022-2836 10.1016/j.jmb.2009.08.015
    • (2009) J. Mol. Biol. , vol.393 , pp. 237
    • Sadler, D.1    Petrik, E.2    Taniguchi, Y.3    Pullen, J.4    Kawakami, M.5    Radford, S.6    Brockwell, D.7
  • 33
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • SCIEAS 0036-8075
    • G. Bell, Models for the specific adhesion of cells to cells, Science 200, 618 (1978). SCIEAS 0036-8075 10.1126/science.347575
    • (1978) Science , vol.200 , pp. 618
    • Bell, G.1
  • 34
    • 4243754128 scopus 로고    scopus 로고
    • Nonequilibrium equality for free energy differences
    • PRLTAO 0031-9007
    • C. Jarzynski, Nonequilibrium equality for free energy differences, Phys. Rev. Lett. 78, 2690 (1997). PRLTAO 0031-9007 10.1103/PhysRevLett.78.2690
    • (1997) Phys. Rev. Lett. , vol.78 , pp. 2690
    • Jarzynski, C.1
  • 35
    • 0000186593 scopus 로고    scopus 로고
    • Path-ensemble averages in systems driven far from equilibrium
    • 1063-651X 10.1103/PhysRevE.61.2361
    • G. E. Crooks, Path-ensemble averages in systems driven far from equilibrium, Phys. Rev. E 61, 2361 (2000). 1063-651X 10.1103/PhysRevE.61.2361
    • (2000) Phys. Rev. e , vol.61 , pp. 2361
    • Crooks, G.E.1
  • 36
    • 0035957434 scopus 로고    scopus 로고
    • Free energy reconstruction from nonequilibrium single-molecule pulling experiments
    • PNASA6 0027-8424
    • G. Hummer and A. Szabo, Free energy reconstruction from nonequilibrium single-molecule pulling experiments, Proc. Natl. Acad. Sci. USA 98, 3658 (2001). PNASA6 0027-8424 10.1073/pnas.071034098
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3658
    • Hummer, G.1    Szabo, A.2
  • 37
    • 44949091394 scopus 로고    scopus 로고
    • Pulling direction as a reaction coordinate for the mechanical unfolding of single molecules
    • JPCBFK 1520-6106
    • R. B. Best, E. Paci, G. Hummer, and O. K. Dudko, Pulling direction as a reaction coordinate for the mechanical unfolding of single molecules, J. Phys. Chem. B 112, 5968 (2008). JPCBFK 1520-6106 10.1021/jp075955j
    • (2008) J. Phys. Chem. B , vol.112 , pp. 5968
    • Best, R.B.1    Paci, E.2    Hummer, G.3    Dudko, O.K.4
  • 38
    • 81055126961 scopus 로고    scopus 로고
    • Locating the barrier for folding of single molecules under an external force
    • PRLTAO 0031-9007
    • O. K. Dudko, T. G. W. Graham, and R. B. Best, Locating the barrier for folding of single molecules under an external force, Phys. Rev. Lett. 107, 208301 (2011). PRLTAO 0031-9007 10.1103/PhysRevLett.107.208301
    • (2011) Phys. Rev. Lett. , vol.107 , pp. 208301
    • Dudko, O.K.1    Graham, T.G.W.2    Best, R.B.3
  • 39
    • 57349124448 scopus 로고    scopus 로고
    • Theory, analysis, and interpretation of single-molecule force spectroscopy experiments
    • PNASA6 0027-8424
    • O. K. Dudko, G. Hummer, and A. Szabo, Theory, analysis, and interpretation of single-molecule force spectroscopy experiments, Proc. Natl. Acad. Sci. USA 105, 15755 (2008). PNASA6 0027-8424 10.1073/pnas.0806085105
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15755
    • Dudko, O.K.1    Hummer, G.2    Szabo, A.3
  • 40
    • 33751579133 scopus 로고    scopus 로고
    • Free energy for protein folding from nonequilibrium simulations using the jarzynski equality
    • JCPSA6 0021-9606
    • D. K. West, P. D. Olmsted, and E. Paci, Free energy for protein folding from nonequilibrium simulations using the jarzynski equality, J. Chem. Phys. 125, 204910 (2006). JCPSA6 0021-9606 10.1063/1.2393232
    • (2006) J. Chem. Phys. , vol.125 , pp. 204910
    • West, D.K.1    Olmsted, P.D.2    Paci, E.3
  • 41
    • 0041335634 scopus 로고    scopus 로고
    • Can energy landscape roughness of proteins and rna be measured by using mechanical unfolding experiments?
    • PNASA6 0027-8424
    • C. Hyeon and D. Thirumalai, Can energy landscape roughness of proteins and rna be measured by using mechanical unfolding experiments? Proc. Natl. Acad. Sci. USA 100, 10249 (2003). PNASA6 0027-8424 10.1073/pnas.1833310100
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10249
    • Hyeon, C.1    Thirumalai, D.2
  • 42
    • 33847753469 scopus 로고    scopus 로고
    • Measuring the energy landscape roughness and the transition state location of biomolecules using single molecule mechanical unfolding experiments
    • JCOMEL 0953-8984
    • C. Hyeon and D. Thirumalai, Measuring the energy landscape roughness and the transition state location of biomolecules using single molecule mechanical unfolding experiments, J. Phys.: Condens. Matter 19, 113101 (2007). JCOMEL 0953-8984 10.1088/0953-8984/19/11/113101
    • (2007) J. Phys.: Condens. Matter , vol.19 , pp. 113101
    • Hyeon, C.1    Thirumalai, D.2
  • 43
    • 84884139880 scopus 로고    scopus 로고
    • Towards design principles for determining the mechanical stability of proteins
    • PPCPFQ 1463-9076
    • T. Hoffmann, K. M. Tych, M. L. Hughes, D. J. Brockwell, and L. Dougan, Towards design principles for determining the mechanical stability of proteins, Phys. Chem. Chem. Phys. 15, 15767 (2013). PPCPFQ 1463-9076 10.1039/c3cp52142g
    • (2013) Phys. Chem. Chem. Phys. , vol.15 , pp. 15767
    • Hoffmann, T.1    Tych, K.M.2    Hughes, M.L.3    Brockwell, D.J.4    Dougan, L.5
  • 44
    • 84901737158 scopus 로고    scopus 로고
    • Viscoelasticity of tau proteins leads to strain rate-dependent breaking of microtubules during axonal stretch injury: Predictions from a mathematical model
    • BIOJAU 0006-3495
    • H. Ahmadzadeh, D. H. Smith, and V. B. Shenoy, Viscoelasticity of tau proteins leads to strain rate-dependent breaking of microtubules during axonal stretch injury: Predictions from a mathematical model, Biophys. J. 106, 1123 (2014). BIOJAU 0006-3495 10.1016/j.bpj.2014.01.024
    • (2014) Biophys. J. , vol.106 , pp. 1123
    • Ahmadzadeh, H.1    Smith, D.H.2    Shenoy, V.B.3
  • 45
    • 84921842138 scopus 로고    scopus 로고
    • Direct correlation of single-molecule properties with bulk mechanical performance for the biomimetic design of polymers
    • J. Chung, A. M. Kushner, A. C. Weisman, and Z. Guan, Direct correlation of single-molecule properties with bulk mechanical performance for the biomimetic design of polymers, Nat. Mater. 1, 1 (2014).
    • (2014) Nat. Mater. , vol.1 , pp. 1
    • Chung, J.1    Kushner, A.M.2    Weisman, A.C.3    Guan, Z.4
  • 46
    • 84907001202 scopus 로고    scopus 로고
    • Direct single-molecule observation of calcium-dependent misfolding in human neuronal calcium sensor-1
    • PNASA6 0027-8424
    • P. O. Heidarsson, M. M. Naqvi, M. R. Otazo, A. Mossa, B. B. Kragelund, and C. Cecconi, Direct single-molecule observation of calcium-dependent misfolding in human neuronal calcium sensor-1, Proc. Natl. Acad. Sci. USA 111, 13069 (2014). PNASA6 0027-8424 10.1073/pnas.1401065111
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 13069
    • Heidarsson, P.O.1    Naqvi, M.M.2    Otazo, M.R.3    Mossa, A.4    Kragelund, B.B.5    Cecconi, C.6
  • 47
    • 84874929344 scopus 로고    scopus 로고
    • Kinetic, energetic, and mechanical differences between dark-state rhodopsin and opsin, structure
    • STRUE6 0969-2126
    • S. Kawamura, M. Gerstung, A. T. Colozo, J. Helenius, A. Maeda, N. Beerenwinkel, P. S. H. Park, and D. J. Muller, Kinetic, energetic, and mechanical differences between dark-state rhodopsin and opsin, structure, Structure 21, 426 (2014). STRUE6 0969-2126 10.1016/j.str.2013.01.011
    • (2014) Structure , vol.21 , pp. 426
    • Kawamura, S.1    Gerstung, M.2    Colozo, A.T.3    Helenius, J.4    Maeda, A.5    Beerenwinkel, N.6    Park, P.S.H.7    Muller, D.J.8
  • 48
    • 84899636482 scopus 로고    scopus 로고
    • (Equation presented) binding enhanced mechanical stability of an archaeal crystallin
    • 1932-6203
    • V. Ramanujam, H. C. Kotamarthi, and S. R. K. Ainavarapu, (Equation presented) binding enhanced mechanical stability of an archaeal crystallin, PLoS ONE 9, e94513 (2014). 1932-6203 10.1371/journal.pone.0094513
    • (2014) PLoS ONE , vol.9 , pp. e94513
    • Ramanujam, V.1    Kotamarthi, H.C.2    Ainavarapu, S.R.K.3
  • 49
    • 84887313611 scopus 로고    scopus 로고
    • High-speed force spectroscopy unfolds titin at the velocity of molecular dynamics simulations
    • SCIEAS 0036-8075
    • F. Rico, L. Gonzalez, I. Casuso, M. Puig-Vidal, and S. Scheuring, High-speed force spectroscopy unfolds titin at the velocity of molecular dynamics simulations, Science 342, 741 (2013). SCIEAS 0036-8075 10.1126/science.1239764
    • (2013) Science , vol.342 , pp. 741
    • Rico, F.1    Gonzalez, L.2    Casuso, I.3    Puig-Vidal, M.4    Scheuring, S.5
  • 50
    • 84898821754 scopus 로고    scopus 로고
    • Force-dependent isomerization kinetics of a highly conserved proline switch modulates the mechanosensing region of filamin
    • PNASA6 0027-8424
    • L. Rognoni, T. Most, G. Zoldak, and M. Rief, Force-dependent isomerization kinetics of a highly conserved proline switch modulates the mechanosensing region of filamin, Proc. Natl. Acad. Sci. USA 111, 5568 (2014). PNASA6 0027-8424 10.1073/pnas.1319448111
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 5568
    • Rognoni, L.1    Most, T.2    Zoldak, G.3    Rief, M.4
  • 51
    • 84897037576 scopus 로고    scopus 로고
    • Interaction of mutant p53 with p73: A surface plasmon resonance and atomic force spectroscopy study
    • 0304-4165
    • S. Santini, S. Di Agostino, E. Coppari, A. R. Bizzarri, G. Blandino, and S. Cannistraro, Interaction of mutant p53 with p73: A surface plasmon resonance and atomic force spectroscopy study, Biochem. Biophys. Acta 1840, 1958 (2014). 0304-4165 10.1016/j.bbagen.2014.02.014
    • (2014) Biochem. Biophys. Acta , vol.1840 , pp. 1958
    • Santini, S.1    Di Agostino, S.2    Coppari, E.3    Bizzarri, A.R.4    Blandino, G.5    Cannistraro, S.6
  • 52
    • 84910016436 scopus 로고    scopus 로고
    • Single lipid extraction: The anchoring strength of cholesterol in liquid-ordered and liquid-disordered phases
    • BIOJAU 0006-3495
    • F. W. S. Stetter, L. Cwiklik, P. Jungwirth, and T. Hugel, Single lipid extraction: The anchoring strength of cholesterol in liquid-ordered and liquid-disordered phases, Biophys. J. 107, 1167 (2014). BIOJAU 0006-3495 10.1016/j.bpj.2014.07.018
    • (2014) Biophys. J. , vol.107 , pp. 1167
    • Stetter, F.W.S.1    Cwiklik, L.2    Jungwirth, P.3    Hugel, T.4
  • 53
    • 84888351252 scopus 로고    scopus 로고
    • Atomic force microscopy: A multifaceted tool to study membrane proteins and their interactions with ligands
    • 0005-2736
    • A. M. Whited and P. S. H. Park, Atomic force microscopy: A multifaceted tool to study membrane proteins and their interactions with ligands, Biochem. Biophys. Acta 1838, 56 (2014). 0005-2736 10.1016/j.bbamem.2013.04.011
    • (2014) Biochem. Biophys. Acta , vol.1838 , pp. 56
    • Whited, A.M.1    Park, P.S.H.2
  • 54
    • 84900808778 scopus 로고    scopus 로고
    • Different roles of cadherins in the assembly and structural integrity of the desmosome complex
    • JNCSAI 0021-9533
    • M. Lowndes, S. Rakshit, O. Shafraz, N. Borghi, R. M. Harmon, K. J. Green, S. Sivasankar, and W. J. Nelson, Different roles of cadherins in the assembly and structural integrity of the desmosome complex, J. Cell Sci. 127, 2339 (2014). JNCSAI 0021-9533 10.1242/jcs.146316
    • (2014) J. Cell Sci. , vol.127 , pp. 2339
    • Lowndes, M.1    Rakshit, S.2    Shafraz, O.3    Borghi, N.4    Harmon, R.M.5    Green, K.J.6    Sivasankar, S.7    Nelson, W.J.8
  • 55
    • 84905055105 scopus 로고    scopus 로고
    • Probability of observing a number of unfolding events while stretching polyproteins
    • LANGD5 0743-7463
    • R. Hermans, Probability of observing a number of unfolding events while stretching polyproteins, Langmuir 30, 8650 (2014). LANGD5 0743-7463 10.1021/la501161p
    • (2014) Langmuir , vol.30 , pp. 8650
    • Hermans, R.1
  • 56
    • 34347209835 scopus 로고
    • Calculation of thermal noise in atomic force microscopy
    • NNOTER 0957-4484
    • H. Butt and M. Jaschke, Calculation of thermal noise in atomic force microscopy, Nanotechnology 6, 1 (1995). NNOTER 0957-4484 10.1088/0957-4484/6/1/001
    • (1995) Nanotechnology , vol.6 , pp. 1
    • Butt, H.1    Jaschke, M.2
  • 57
    • 0028834673 scopus 로고
    • Sensing specific molecular interactions with the atomic force microscope
    • BBIOE4 0956-5663
    • E. Florin, M. Rief, H. Lehmann, M. Ludwig, C. Dornmair, V. Moy, and H. Gaub, Sensing specific molecular interactions with the atomic force microscope, Biosens. Bioelectron. 10, 895 (1995). BBIOE4 0956-5663 10.1016/0956-5663(95)99227-C
    • (1995) Biosens. Bioelectron. , vol.10 , pp. 895
    • Florin, E.1    Rief, M.2    Lehmann, H.3    Ludwig, M.4    Dornmair, C.5    Moy, V.6    Gaub, H.7
  • 59
    • 0347123330 scopus 로고    scopus 로고
    • Thermal denaturation and folding rates of single domain proteins: Size matters
    • M. S. Li, D. K. Klimov, and D. Thirumalai, Thermal denaturation and folding rates of single domain proteins: Size matters, Polymer 45, 573 (2004). 10.1016/j.polymer.2003.10.066
    • (2004) Polymer , vol.45 , pp. 573
    • Li, M.S.1    Klimov, D.K.2    Thirumalai, D.3
  • 60
    • 15544363835 scopus 로고
    • Stretching dna
    • MAMOBX 0024-9297
    • J. Marko and E. Siggia, Stretching dna, Macromolecules 28, 8759 (1995). MAMOBX 0024-9297 10.1021/ma00130a008
    • (1995) Macromolecules , vol.28 , pp. 8759
    • Marko, J.1    Siggia, E.2
  • 61
    • 84883277333 scopus 로고    scopus 로고
    • Improving single molecule force spectroscopy through automated real-time data collection and quantification of experimental conditions
    • ULTRD6 0304-3991
    • Z. Scholl and P. Marszalek, Improving single molecule force spectroscopy through automated real-time data collection and quantification of experimental conditions, Ultramicroscopy 136, 7 (2014). ULTRD6 0304-3991 10.1016/j.ultramic.2013.07.020
    • (2014) Ultramicroscopy , vol.136 , pp. 7
    • Scholl, Z.1    Marszalek, P.2
  • 62
    • 33645765218 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin
    • 1745-2473
    • J. Brujic, R. I. Hermans, K. A. Walther, and J. M. Fernandez, Single-molecule force spectroscopy reveals signatures of glassy dynamics in the energy landscape of ubiquitin, Nat. Phys. 2, 282 (2006). 1745-2473 10.1038/nphys269
    • (2006) Nat. Phys. , vol.2 , pp. 282
    • Brujic, J.1    Hermans, R.I.2    Walther, K.A.3    Fernandez, J.M.4
  • 63
    • 0036891724 scopus 로고    scopus 로고
    • Mechanically unfolding proteins: The effect of unfolding history and the supramolecular scaffold
    • PRCIEI 0961-8368
    • R. Zinober, D. Brockwell, G. Beddard, A. Blake, P. Olmsted, S. Radford, and D. Smith, Mechanically unfolding proteins: The effect of unfolding history and the supramolecular scaffold, Protein Sci. 11, 2759 (2002). PRCIEI 0961-8368 10.1110/ps.0224602
    • (2002) Protein Sci. , vol.11 , pp. 2759
    • Zinober, R.1    Brockwell, D.2    Beddard, G.3    Blake, A.4    Olmsted, P.5    Radford, S.6    Smith, D.7
  • 64
    • 0035366858 scopus 로고    scopus 로고
    • Kinetic Monte Carlo simulation of titin unfolding
    • JCPSA6 0021-9606
    • D. Makarov, P. Hansma, and H. Metiu, Kinetic Monte Carlo simulation of titin unfolding, J. Chem. Phys. 114, 9663 (2001). JCPSA6 0021-9606 10.1063/1.1369622
    • (2001) J. Chem. Phys. , vol.114 , pp. 9663
    • Makarov, D.1    Hansma, P.2    Metiu, H.3


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