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Volumn 82, Issue 5, 2014, Pages 717-726

Theoretical tests of the mechanical protection strategy in protein nanomechanics

Author keywords

Coarse grained models; Cystine slipknots; PFS vectors; Single molecule force spectroscopy; Stretching of proteins

Indexed keywords

COHESIN; CYSTINE; PROTEIN; NANOMATERIAL;

EID: 84898049775     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24436     Document Type: Article
Times cited : (13)

References (39)
  • 1
    • 33746675190 scopus 로고    scopus 로고
    • Single-molecule experiments in biological physics: methods and applications
    • Ritort F. Single-molecule experiments in biological physics: methods and applications. J Phys Cond Matter 2006;18:R531-R583.
    • (2006) J Phys Cond Matter , vol.18
    • Ritort, F.1
  • 2
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding in single titin molecules characterized with laser tweezers
    • Kellermayer MSZ, Smith SB, Granzier HL, Bustamante C. Folding-unfolding in single titin molecules characterized with laser tweezers. Science 1997;276:11126.
    • (1997) Science , vol.276 , pp. 11126
    • Kellermayer, M.S.Z.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 6
    • 77955983405 scopus 로고    scopus 로고
    • Unravelling the design principles for single protein mechanical strength
    • Crampton N, Brockwell DJ. Unravelling the design principles for single protein mechanical strength. Curr Opin Struct Biol 2010;20:508-517.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 508-517
    • Crampton, N.1    Brockwell, D.J.2
  • 8
    • 3042806394 scopus 로고    scopus 로고
    • Thermal effects in stretching of Go-like models of titin and secondary structures
    • Cieplak M, Hoang TX, Robbins MO. Thermal effects in stretching of Go-like models of titin and secondary structures. Proteins Struct Funct Bio 2004;56:285-297.
    • (2004) Proteins Struct Funct Bio , vol.56 , pp. 285-297
    • Cieplak, M.1    Hoang, T.X.2    Robbins, M.O.3
  • 9
    • 22944478656 scopus 로고    scopus 로고
    • Mechanical properties of the domains of titin in a Go-like model
    • Cieplak M, Pastore A, Hoang TX. Mechanical properties of the domains of titin in a Go-like model. J Chem Phys 2005;122:054906.
    • (2005) J Chem Phys , vol.122 , pp. 054906
    • Cieplak, M.1    Pastore, A.2    Hoang, T.X.3
  • 10
    • 84856743116 scopus 로고    scopus 로고
    • Unequivocal single-molecule force spectroscopy of proteins by AFM using pFS vectors
    • Oroz J, Hervas R, Carrion-Vazquez M. Unequivocal single-molecule force spectroscopy of proteins by AFM using pFS vectors. Biophys J 2012;102:682-690.
    • (2012) Biophys J , vol.102 , pp. 682-690
    • Oroz, J.1    Hervas, R.2    Carrion-Vazquez, M.3
  • 14
    • 0037216990 scopus 로고    scopus 로고
    • Universality classes in folding times of proteins
    • Cieplak M, Hoang TX. Universality classes in folding times of proteins Biophys J 2003;84:475-488.
    • (2003) Biophys J , vol.84 , pp. 475-488
    • Cieplak, M.1    Hoang, T.X.2
  • 15
    • 34547673274 scopus 로고    scopus 로고
    • Mechanical stretching of proteins-a theoretical survey of the Protein Data Bank
    • Sulkowska JI, Cieplak M. Mechanical stretching of proteins-a theoretical survey of the Protein Data Bank. J Phys Cond Mat 2007;19:283201.
    • (2007) J Phys Cond Mat , vol.19 , pp. 283201
    • Sulkowska, J.I.1    Cieplak, M.2
  • 16
    • 55949109149 scopus 로고    scopus 로고
    • Selection of optimal variants of Go-like models of proteins through studies of stretching
    • Sulkowska JI, Cieplak M. Selection of optimal variants of Go-like models of proteins through studies of stretching. Biophys J 2008;95:3174-3191.
    • (2008) Biophys J , vol.95 , pp. 3174-3191
    • Sulkowska, J.I.1    Cieplak, M.2
  • 17
    • 84898030391 scopus 로고    scopus 로고
    • The PyMol Molecular Graphics System, Version 1.5.0.4 Schrodinger, LLC
    • The PyMol Molecular Graphics System, Version 1.5.0.4 Schrodinger, LLC; http://www.pymol.org
  • 18
    • 0042885340 scopus 로고    scopus 로고
    • Free energy calculation from steered molecular dynamics simulations using Jarzynski's equality
    • Park S, Khalili-Araghi F, Tajkhorshid E, Schulten K. Free energy calculation from steered molecular dynamics simulations using Jarzynski's equality. J Chem Phys 2003;119:3559-3566.
    • (2003) J Chem Phys , vol.119 , pp. 3559-3566
    • Park, S.1    Khalili-Araghi, F.2    Tajkhorshid, E.3    Schulten, K.4
  • 20
    • 0035956901 scopus 로고    scopus 로고
    • Solvent effects on the energy landscapes and folding kinetics
    • Levy Y, Jortner J, Becker OM. Solvent effects on the energy landscapes and folding kinetics. Proc Natl Acad Sci USA 2001;98:2188-2193.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2188-2193
    • Levy, Y.1    Jortner, J.2    Becker, O.M.3
  • 21
    • 0033516705 scopus 로고    scopus 로고
    • The packing density in proteins: standard radii and volumes
    • Tsai J, Taylor R, Chothia C, Gerstein M. The packing density in proteins: standard radii and volumes. J Mol Biol 1999;290:253-266.
    • (1999) J Mol Biol , vol.290 , pp. 253-266
    • Tsai, J.1    Taylor, R.2    Chothia, C.3    Gerstein, M.4
  • 22
    • 73549110486 scopus 로고    scopus 로고
    • Mechanical strength of 17 132 model proteins and cysteine slipknots
    • Sikora M, Sulkowska JI, Cieplak M. Mechanical strength of 17 132 model proteins and cysteine slipknots. PloS Comp Biol 2008;5:e1000547.
    • (2008) PloS Comp Biol , vol.5
    • Sikora, M.1    Sulkowska, J.I.2    Cieplak, M.3
  • 23
    • 5544254964 scopus 로고
    • Molecular dynamics simulation for polymers in the presence of a heat bath
    • Grest GS, Kremer K. Molecular dynamics simulation for polymers in the presence of a heat bath. Phys Rev A 1986;33:3628-3631.
    • (1986) Phys Rev A , vol.33 , pp. 3628-3631
    • Grest, G.S.1    Kremer, K.2
  • 26
    • 0026044754 scopus 로고
    • Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy
    • Bycroft M, Ludvigsen S, Fersht AR, Poulsen FM. Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy. Biochemistry 1991;30:8697-8701.
    • (1991) Biochemistry , vol.30 , pp. 8697-8701
    • Bycroft, M.1    Ludvigsen, S.2    Fersht, A.R.3    Poulsen, F.M.4
  • 28
    • 0030584660 scopus 로고    scopus 로고
    • Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity
    • Improta S, Politou AS, Pastore A. Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity. Structure 1996;4:323-337.
    • (1996) Structure , vol.4 , pp. 323-337
    • Improta, S.1    Politou, A.S.2    Pastore, A.3
  • 29
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 Å resolution
    • Vijay-Kumar S, Bugg CE, Cook WJ. Structure of ubiquitin refined at 1.8 Å resolution. J Mol Biol 1987;194:531-544.
    • (1987) J Mol Biol , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 30
    • 0034711422 scopus 로고    scopus 로고
    • Crystal structure of a cohesin module from Clostridium cellulolyticum: implications for dockerin recognition
    • Spinelli S, Fierobe HP, Belaich A, Belaich JP, Henrissat B, Cambillau C. Crystal structure of a cohesin module from Clostridium cellulolyticum: implications for dockerin recognition. J Mol Biol 2000;304:189-200.
    • (2000) J Mol Biol , vol.304 , pp. 189-200
    • Spinelli, S.1    Fierobe, H.P.2    Belaich, A.3    Belaich, J.P.4    Henrissat, B.5    Cambillau, C.6
  • 31
    • 0032879635 scopus 로고    scopus 로고
    • Crystal structure of streptokinase beta-domain
    • Wang X, Tang J, Hunter B, Zhang XC. Crystal structure of streptokinase beta-domain. FEBS Lett 1999;459:85-89.
    • (1999) FEBS Lett , vol.459 , pp. 85-89
    • Wang, X.1    Tang, J.2    Hunter, B.3    Zhang, X.C.4
  • 32
    • 0034804341 scopus 로고    scopus 로고
    • Can non-mechanical proteins withstand force?Stretching barnase by atomic force microscopy and molecular dynamics simulation
    • Best RB, Li B, Steward A, Daggett V, Clarke J. Can non-mechanical proteins withstand force?Stretching barnase by atomic force microscopy and molecular dynamics simulation. Biophys J 2001;81:2344-2356.
    • (2001) Biophys J , vol.81 , pp. 2344-2356
    • Best, R.B.1    Li, B.2    Steward, A.3    Daggett, V.4    Clarke, J.5
  • 33
    • 33846666463 scopus 로고    scopus 로고
    • Polyprotein of GB1 is an ideal articial elastomeric protein
    • Cao Y, Li H. Polyprotein of GB1 is an ideal articial elastomeric protein. Nat Mater 2007;6:109114.
    • (2007) Nat Mater , vol.6 , pp. 109114
    • Cao, Y.1    Li, H.2
  • 34
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief M, Gautel M, Oesterhelt F, Fernandez JM, Gaub HE. 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
  • 36
    • 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. 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.2
  • 37
    • 79952096460 scopus 로고    scopus 로고
    • Molecular jamming-the cysteine slipknot mechanical clamp in all-atom simulations
    • Peplowski L, Sikora M, Nowak W, Cieplak M. Molecular jamming-the cysteine slipknot mechanical clamp in all-atom simulations. J Chem Phys 2011;134:085102.
    • (2011) J Chem Phys , vol.134 , pp. 085102
    • Peplowski, L.1    Sikora, M.2    Nowak, W.3    Cieplak, M.4
  • 38
    • 84874786719 scopus 로고    scopus 로고
    • Formation of cystine slipknots in dimeric proteins
    • Sikora M, Cieplak M. Formation of cystine slipknots in dimeric proteins. PLoS One 2013;8:e57443.
    • (2013) PLoS One , vol.8
    • Sikora, M.1    Cieplak, M.2
  • 39
    • 84869065519 scopus 로고    scopus 로고
    • Cystine plug and other novel mechanisms of large mechanical stability in dimeric proteins
    • Sikora M, Cieplak M. Cystine plug and other novel mechanisms of large mechanical stability in dimeric proteins. Phys Rev Lett 2012;109:208101.
    • (2012) Phys Rev Lett , vol.109 , pp. 208101
    • Sikora, M.1    Cieplak, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.