메뉴 건너뛰기




Volumn 371, Issue 4, 2007, Pages 851-854

Experiments Suggest that Simulations May Overestimate Electrostatic Contributions to the Mechanical Stability of a Fibronectin Type III Domain

Author keywords

AFM; extracellular matrix; forced unfolding; MD simulations; titin

Indexed keywords

FIBRONECTIN; SCLEROPROTEIN; TENASCIN;

EID: 34547116898     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.06.015     Document Type: Article
Times cited : (10)

References (21)
  • 1
    • 0042562089 scopus 로고    scopus 로고
    • Biomimetic materials for tissue engineering
    • Shin H., Jo S., and Mikos A.G. Biomimetic materials for tissue engineering. Biomaterials 24 (2003) 4353-4364
    • (2003) Biomaterials , vol.24 , pp. 4353-4364
    • Shin, H.1    Jo, S.2    Mikos, A.G.3
  • 2
    • 0036127725 scopus 로고    scopus 로고
    • Function of linear and cyclic RGD-containing peptides in osteoprogenitor cells adhesion process
    • Verrier S., Pallu S., Bareille R., Jonczyk A., Meyer J., Dard M., and Amedee J. Function of linear and cyclic RGD-containing peptides in osteoprogenitor cells adhesion process. Biomaterials 23 (2002) 585-596
    • (2002) Biomaterials , vol.23 , pp. 585-596
    • Verrier, S.1    Pallu, S.2    Bareille, R.3    Jonczyk, A.4    Meyer, J.5    Dard, M.6    Amedee, J.7
  • 3
    • 33645780908 scopus 로고    scopus 로고
    • Mechanotransduction involving multimodular proteins: converting force into biochemical signals
    • Vogel V. Mechanotransduction involving multimodular proteins: converting force into biochemical signals. Annu. Rev. Biophys. Biomol. Struct. 35 (2006) 459-488
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 459-488
    • Vogel, V.1
  • 5
    • 10044247452 scopus 로고    scopus 로고
    • Mechanical unfolding intermediates observed by single-molecule force spectroscopy in a fibronectin type III module
    • Li L., Huang H.H., Badilla C.L., and Fernandez J.M. Mechanical unfolding intermediates observed by single-molecule force spectroscopy in a fibronectin type III module. J. Mol. Biol. 345 (2005) 817-826
    • (2005) J. Mol. Biol. , vol.345 , pp. 817-826
    • Li, L.1    Huang, H.H.2    Badilla, C.L.3    Fernandez, J.M.4
  • 6
    • 1642493664 scopus 로고    scopus 로고
    • Tuning the mechanical stability of fibronectin type III modules through sequence variations
    • Craig D., Gao M., Schulten K., and Vogel V. Tuning the mechanical stability of fibronectin type III modules through sequence variations. Structure 12 (2004) 21-30
    • (2004) Structure , vol.12 , pp. 21-30
    • Craig, D.1    Gao, M.2    Schulten, K.3    Vogel, V.4
  • 7
    • 0033531973 scopus 로고    scopus 로고
    • Forced unfolding of fibronectin type 3 modules: an analysis by biased molecular dynamics simulations
    • Paci E., and Karplus M. Forced unfolding of fibronectin type 3 modules: an analysis by biased molecular dynamics simulations. J. Mol. Biol. 288 (1999) 441-459
    • (1999) J. Mol. Biol. , vol.288 , pp. 441-459
    • Paci, E.1    Karplus, M.2
  • 8
    • 0034691149 scopus 로고    scopus 로고
    • Native topology determines force induced unfolding pathways in globular proteins
    • Klimov D.K., and Thirumalai D. Native topology determines force induced unfolding pathways in globular proteins. Proc. Natl Acad. Sci. USA 97 (2000) 7254-7259
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 7254-7259
    • Klimov, D.K.1    Thirumalai, D.2
  • 9
    • 0033957144 scopus 로고    scopus 로고
    • Folding of beta-sandwich proteins: three-state transition of a fibronectin type III module
    • Cota E., and Clarke J. Folding of beta-sandwich proteins: three-state transition of a fibronectin type III module. Protein Sci. 9 (2000) 112-120
    • (2000) Protein Sci. , vol.9 , pp. 112-120
    • Cota, E.1    Clarke, J.2
  • 10
    • 0035964254 scopus 로고    scopus 로고
    • Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface
    • Koide A., Jordan M.R., Horner S.R., Batori V., and Koide S. Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface. Biochemistry 40 (2001) 10326-10333
    • (2001) Biochemistry , vol.40 , pp. 10326-10333
    • Koide, A.1    Jordan, M.R.2    Horner, S.R.3    Batori, V.4    Koide, S.5
  • 11
    • 0034804341 scopus 로고    scopus 로고
    • Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation
    • Best R.B., Li B., Steward A., Daggett V., and Clarke J. Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation. Biophys. J. 81 (2001) 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
  • 13
    • 20544465799 scopus 로고    scopus 로고
    • Mechanical unfolding of TNfn3: the unfolding pathway of a fnIII domain probed by protein engineering. AFM and MD simulation
    • Ng S.P., Rounsevell R.W., Steward A., Geierhaas C. D., Williams P.M., Paci E., and Clarke J. Mechanical unfolding of TNfn3: the unfolding pathway of a fnIII domain probed by protein engineering. AFM and MD simulation. J. Mol. Biol. 350 (2005) 776-789
    • (2005) J. Mol. Biol. , vol.350 , pp. 776-789
    • Ng, S.P.1    Rounsevell, R.W.2    Steward, A.3    Geierhaas, C. D.4    Williams, P.M.5    Paci, E.6    Clarke, J.7
  • 14
    • 0034703474 scopus 로고    scopus 로고
    • Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability
    • Cota E., Hamill S.J., Fowler S.B., and Clarke J. Two proteins with the same structure respond very differently to mutation: the role of plasticity in protein stability. J. Mol. Biol. 302 (2000) 713-725
    • (2000) J. Mol. Biol. , vol.302 , pp. 713-725
    • Cota, E.1    Hamill, S.J.2    Fowler, S.B.3    Clarke, J.4
  • 16
    • 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., Steward A., Paci E., and 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. 330 (2003) 867-877
    • (2003) J. Mol. Biol. , vol.330 , pp. 867-877
    • Best, R.B.1    Fowler, S.B.2    Herrera, J.L.3    Steward, A.4    Paci, E.5    Clarke, J.6
  • 18
    • 33846193288 scopus 로고    scopus 로고
    • Pathways and kinetic barriers in mechanical unfolding and folding of RNA and proteins
    • Hyeon C., Dima R.I., and Thirumalai D. Pathways and kinetic barriers in mechanical unfolding and folding of RNA and proteins. Structure 14 (2006) 1645-1663
    • (2006) Structure , vol.14 , pp. 1645-1663
    • Hyeon, C.1    Dima, R.I.2    Thirumalai, D.3
  • 20
    • 0036707999 scopus 로고    scopus 로고
    • Versatile cloning system for construction of multimeric proteins for use in atomic force microscopy
    • Steward A., Toca-Herrera J.L., and Clarke J. Versatile cloning system for construction of multimeric proteins for use in atomic force microscopy. Protein Sci. 11 (2002) 2179-2183
    • (2002) Protein Sci. , vol.11 , pp. 2179-2183
    • Steward, A.1    Toca-Herrera, J.L.2    Clarke, J.3
  • 21
    • 20544435808 scopus 로고    scopus 로고
    • Biophysical investigations of engineered polyproteins:implications for force data
    • Rounsevell R.W.S., Steward A., and Clarke J. Biophysical investigations of engineered polyproteins:implications for force data. Biophys. J. 88 (2005) 2022-2029
    • (2005) Biophys. J. , vol.88 , pp. 2022-2029
    • Rounsevell, R.W.S.1    Steward, A.2    Clarke, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.