메뉴 건너뛰기




Volumn 1, Issue 6, 2015, Pages 363-371

Dimerization of Terminal Domains in Spiders Silk Proteins Is Controlled by Electrostatic Anisotropy and Modulated by Hydrophobic Patches

Author keywords

dimer formation; electrostatic anisotropy; hydrophobic patchiness; Monte Carlo simulation; silk assembly; silk termini domains

Indexed keywords

DIMER; MONOMER; MUTANT PROTEIN; PROTEIN; SILK; SILK PROTEIN; SODIUM CHLORIDE; UNCLASSIFIED DRUG; WATER;

EID: 84969188108     PISSN: None     EISSN: 23739878     Source Type: Journal    
DOI: 10.1021/ab500039q     Document Type: Article
Times cited : (23)

References (43)
  • 1
    • 0034978997 scopus 로고    scopus 로고
    • Changes in element composition along the spinning duct in a Nephila spider
    • Knight, D.; Vollrath, F. Changes in element composition along the spinning duct in a Nephila spider Naturwissenschaften 2001, 88, 179-182 10.1007/s001140100220
    • (2001) Naturwissenschaften , vol.88 , pp. 179-182
    • Knight, D.1    Vollrath, F.2
  • 3
    • 84874905314 scopus 로고    scopus 로고
    • Spider silk: Super material or thin fibre?
    • Porter, D.; Guan, J.; Vollrath, F. Spider silk: super material or thin fibre? Adv. Mater. (Weinheim, Ger.) 2013, 25, 1275-9 10.1002/adma.201204158
    • (2013) Adv. Mater. (Weinheim, Ger.) , vol.25 , pp. 1275-1279
    • Porter, D.1    Guan, J.2    Vollrath, F.3
  • 5
    • 37749031729 scopus 로고    scopus 로고
    • The Role of Behavior in the Evolution of Spiders, Silks, and Webs
    • Vollrath, F.; Selden, P. The Role of Behavior in the Evolution of Spiders, Silks, and Webs Annu. Rev. Ecol. Evol. Syst. 2007, 38, 819-846 10.1146/annurev.ecolsys.37.091305.110221
    • (2007) Annu. Rev. Ecol. Evol. Syst. , vol.38 , pp. 819-846
    • Vollrath, F.1    Selden, P.2
  • 6
  • 7
    • 0034252384 scopus 로고    scopus 로고
    • Strength and structure of spiders' silks
    • Vollrath, F. Strength and structure of spiders' silks Rev. Mol. Biotechnol. 2000, 74, 67-83 10.1016/S1389-0352(00)00006-4
    • (2000) Rev. Mol. Biotechnol. , vol.74 , pp. 67-83
    • Vollrath, F.1
  • 8
    • 33745685415 scopus 로고    scopus 로고
    • Spider silk as archetypal protein elastomer
    • Vollrath, F.; Porter, D. Spider silk as archetypal protein elastomer Soft Matter 2006, 2, 377 10.1039/b600098n
    • (2006) Soft Matter , vol.2 , pp. 377
    • Vollrath, F.1    Porter, D.2
  • 9
    • 80053580903 scopus 로고    scopus 로고
    • There are many more lessons still to be learned from spider silks
    • Vollrath, F.; Porter, D.; Holland, C. There are many more lessons still to be learned from spider silks Soft Matter 2011, 7, 9595 10.1039/c1sm05812f
    • (2011) Soft Matter , vol.7 , pp. 9595
    • Vollrath, F.1    Porter, D.2    Holland, C.3
  • 10
    • 0034575301 scopus 로고    scopus 로고
    • X-ray diffraction on spider silk during controlled extrusion under a synchrotron radiation X-ray beam
    • Riekel, C.; Madsen, B.; Knight, D.; Vollrath, F. X-ray diffraction on spider silk during controlled extrusion under a synchrotron radiation X-ray beam Biomacromolecules 2000, 1, 622-6 10.1021/bm000047c
    • (2000) Biomacromolecules , vol.1 , pp. 622-626
    • Riekel, C.1    Madsen, B.2    Knight, D.3    Vollrath, F.4
  • 11
    • 0036678028 scopus 로고    scopus 로고
    • The molecular structure of spider dragline silk: Folding and orientation of the protein backbone
    • van Beek, J. D.; Hess, S.; Vollrath, F.; Meier, B. H. The molecular structure of spider dragline silk: folding and orientation of the protein backbone Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 10266-71 10.1073/pnas.152162299
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 10266-10271
    • Van Beek, J.D.1    Hess, S.2    Vollrath, F.3    Meier, B.H.4
  • 12
    • 0025008260 scopus 로고
    • Structure of a protein superfiber: Spider dragline silk
    • Xu, M.; Lewis, R. V. Structure of a protein superfiber: spider dragline silk Proc. Natl. Acad. Sci. U. S. A. 1990, 87, 7120-4 10.1073/pnas.87.18.7120
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 7120-7124
    • Xu, M.1    Lewis, R.V.2
  • 13
    • 0029925013 scopus 로고    scopus 로고
    • Silk properties determined by gland-specific expression of a spider fibroin gene family
    • Guerette, P. A.; Ginzinger, D. G.; Weber, B. H.; Gosline, J. M. Silk properties determined by gland-specific expression of a spider fibroin gene family Science (Washington, DC, U. S.) 1996, 272, 112-115 10.1126/science.272.5258.112
    • (1996) Science (Washington, DC, U. S.) , vol.272 , pp. 112-115
    • Guerette, P.A.1    Ginzinger, D.G.2    Weber, B.H.3    Gosline, J.M.4
  • 14
    • 0032963575 scopus 로고    scopus 로고
    • Hypotheses that correlate the sequence, structure, and mechanical properties of spider silk proteins
    • Hayashi, C. Y.; Shipley, N. H.; Lewis, R. V. Hypotheses that correlate the sequence, structure, and mechanical properties of spider silk proteins Int. J. Biol. Macromol. 1999, 24, 271-5 10.1016/S0141-8130(98)00089-0
    • (1999) Int. J. Biol. Macromol. , vol.24 , pp. 271-275
    • Hayashi, C.Y.1    Shipley, N.H.2    Lewis, R.V.3
  • 15
    • 0000453056 scopus 로고
    • Amino acid composition of spider silk
    • Andersen, S. O. Amino acid composition of spider silk Comparative Biochemistry and Physiology 1970, 35, 705-711 10.1016/0010-406X(70)90988-6
    • (1970) Comparative Biochemistry and Physiology , vol.35 , pp. 705-711
    • Andersen, S.O.1
  • 16
    • 0033378773 scopus 로고    scopus 로고
    • Hexagonal columnar liquid crystal in the cells secreting spider silk
    • Knight, D.; Vollrath, F. Hexagonal columnar liquid crystal in the cells secreting spider silk Tissue Cell 1999, 31, 617-20 10.1054/tice.1999.0076
    • (1999) Tissue Cell , vol.31 , pp. 617-620
    • Knight, D.1    Vollrath, F.2
  • 17
    • 0034704173 scopus 로고    scopus 로고
    • Silk fibroin of Bombyx mori is secreted, assembling a high molecular mass elementary unit consisting of H-chain, L-chain, and P25, with a 6:6:1 molar ratio
    • Inoue, S.; Tanaka, K.; Arisaka, F.; Kimura, S.; Ohtomo, K.; Mizuno, S. Silk fibroin of Bombyx mori is secreted, assembling a high molecular mass elementary unit consisting of H-chain, L-chain, and P25, with a 6:6:1 molar ratio J. Biol. Chem. 2000, 275, 40517-28 10.1074/jbc.M006897200
    • (2000) J. Biol. Chem. , vol.275 , pp. 40517-40528
    • Inoue, S.1    Tanaka, K.2    Arisaka, F.3    Kimura, S.4    Ohtomo, K.5    Mizuno, S.6
  • 18
    • 0042364941 scopus 로고    scopus 로고
    • Mechanism of silk processing in insects and spiders
    • Jin, H. J.; Kaplan, D. L. Mechanism of silk processing in insects and spiders Nature (London, U. K.) 2003, 424, 1057-61 10.1038/nature01809
    • (2003) Nature (London, U. K.) , vol.424 , pp. 1057-1061
    • Jin, H.J.1    Kaplan, D.L.2
  • 20
    • 0030014956 scopus 로고    scopus 로고
    • Progress Towards Understanding [beta-Sheet Structure
    • Nesloney, C. L.; Kelly, J. W. Progress Towards Understanding [beta-Sheet Structure Bioorg. Med. Chem. 1996, 4, 739-766 10.1016/0968-0896(96)00051-X
    • (1996) Bioorg. Med. Chem. , vol.4 , pp. 739-766
    • Nesloney, C.L.1    Kelly, J.W.2
  • 21
    • 33845724091 scopus 로고    scopus 로고
    • Beta-silks: Enhancing and controlling aggregation
    • Dicko, C.; Kenney, J. M.; Vollrath, F. Beta-silks: enhancing and controlling aggregation Adv. Protein Chem. 2006, 73, 17-53
    • (2006) Adv. Protein Chem. , vol.73 , pp. 17-53
    • Dicko, C.1    Kenney, J.M.2    Vollrath, F.3
  • 22
    • 0032492935 scopus 로고    scopus 로고
    • Silk production in a spider involves acid bath treatment
    • Vollrath, F.; Knight, D. P.; Hu, X. W. Silk production in a spider involves acid bath treatment Proc. R. Soc. London, Ser. B 1998, 265, 817-820 10.1098/rspb.1998.0365
    • (1998) Proc. R. Soc. London, Ser. B , vol.265 , pp. 817-820
    • Vollrath, F.1    Knight, D.P.2    Hu, X.W.3
  • 23
    • 8344220569 scopus 로고    scopus 로고
    • Transition to a beta-sheet-rich structure in spidroin in vitro: The effects of pH and cations
    • Dicko, C.; Kenney, J. M.; Knight, D.; Vollrath, F. Transition to a beta-sheet-rich structure in spidroin in vitro: the effects of pH and cations Biochemistry 2004, 43, 14080-7 10.1021/bi0483413
    • (2004) Biochemistry , vol.43 , pp. 14080-14087
    • Dicko, C.1    Kenney, J.M.2    Knight, D.3    Vollrath, F.4
  • 24
    • 2542585370 scopus 로고    scopus 로고
    • Spider silk protein refolding is controlled by changing pH
    • Dicko, C.; Vollrath, F.; Kenney, J. M. Spider silk protein refolding is controlled by changing pH Biomacromolecules 2004, 5, 704-10 10.1021/bm034307c
    • (2004) Biomacromolecules , vol.5 , pp. 704-710
    • Dicko, C.1    Vollrath, F.2    Kenney, J.M.3
  • 27
    • 78650693161 scopus 로고    scopus 로고
    • PH-dependent dimerization and salt-dependent stabilization of the N-terminal domain of spider dragline silk-implications for fiber formation
    • Hagn, F.; Thamm, C.; Scheibel, T.; Kessler, H. pH-dependent dimerization and salt-dependent stabilization of the N-terminal domain of spider dragline silk-implications for fiber formation Angew. Chem., Int. Ed. 2011, 50, 310-3 10.1002/anie.201003795
    • (2011) Angew. Chem., Int. Ed. , vol.50 , pp. 310-313
    • Hagn, F.1    Thamm, C.2    Scheibel, T.3    Kessler, H.4
  • 28
    • 84857744963 scopus 로고    scopus 로고
    • Unraveling A Trap-and-Trigger Mechanism in the pH-Sensitive Self-Assembly of Spider Silk Proteins
    • Wallace, J.; Shen, J. Unraveling A Trap-and-Trigger Mechanism in the pH-Sensitive Self-Assembly of Spider Silk Proteins J. Phys. Chem. Lett. 2012, 3, 658-662 10.1021/jz2016846
    • (2012) J. Phys. Chem. Lett. , vol.3 , pp. 658-662
    • Wallace, J.1    Shen, J.2
  • 29
    • 84889564783 scopus 로고    scopus 로고
    • The N-terminal domains of spider silk proteins assemble ultrafast and protected from charge screening
    • Schwarze, S.; Zwettler, F. U.; Johnson, C. M.; Neuweiler, H. The N-terminal domains of spider silk proteins assemble ultrafast and protected from charge screening Nat. Commun. 2013, 4, 2815 10.1038/ncomms3815
    • (2013) Nat. Commun. , vol.4 , pp. 2815
    • Schwarze, S.1    Zwettler, F.U.2    Johnson, C.M.3    Neuweiler, H.4
  • 31
    • 77955025365 scopus 로고    scopus 로고
    • The molecular mechanism of spider-silk formation
    • Silvers, R.; Buhr, F.; Schwalbe, H. The molecular mechanism of spider-silk formation Angew. Chem., Int. Ed. 2010, 49, 5410-2 10.1002/anie.201003033
    • (2010) Angew. Chem., Int. Ed. , vol.49 , pp. 5410-5412
    • Silvers, R.1    Buhr, F.2    Schwalbe, H.3
  • 32
    • 84858859727 scopus 로고    scopus 로고
    • Review the role of terminal domains during storage and assembly of spider silk proteins
    • Eisoldt, L.; Thamm, C.; Scheibel, T. Review the role of terminal domains during storage and assembly of spider silk proteins Biopolymers 2012, 97, 355-61 10.1002/bip.22006
    • (2012) Biopolymers , vol.97 , pp. 355-361
    • Eisoldt, L.1    Thamm, C.2    Scheibel, T.3
  • 34
    • 84858665589 scopus 로고    scopus 로고
    • Anisotropic Interactions in Protein Mixtures: Self Assembly and Phase Behavior in Aqueous Solution
    • Kurut, A.; Persson, B. A.; Åkesson, T.; Forsman, J.; Lund, M. Anisotropic Interactions in Protein Mixtures: Self Assembly and Phase Behavior in Aqueous Solution J. Phys. Chem. Lett. 2012, 3, 731-734 10.1021/jz201680m
    • (2012) J. Phys. Chem. Lett. , vol.3 , pp. 731-734
    • Kurut, A.1    Persson, B.A.2    Åkesson, T.3    Forsman, J.4    Lund, M.5
  • 35
    • 84884175429 scopus 로고    scopus 로고
    • Charge regulation in biomolecular solution
    • Lund, M.; Jönsson, B. Charge regulation in biomolecular solution Q. Rev. Biophys. 2013, 46, 265-81 10.1017/S003358351300005X
    • (2013) Q. Rev. Biophys. , vol.46 , pp. 265-281
    • Lund, M.1    Jönsson, B.2
  • 36
    • 84906842224 scopus 로고    scopus 로고
    • Weak Self-Interactions of Globular Proteins Studied by Small-Angle X-ray Scattering and Structure-Based Modeling
    • Kaieda, S.; Lund, M.; Plivelic, T. S.; Halle, B. Weak Self-Interactions of Globular Proteins Studied by Small-Angle X-ray Scattering and Structure-Based Modeling J. Phys. Chem. B 2014, 118, 10111-9 10.1021/jp505809v
    • (2014) J. Phys. Chem. B , vol.118 , pp. 10111-10119
    • Kaieda, S.1    Lund, M.2    Plivelic, T.S.3    Halle, B.4
  • 37
    • 67651207529 scopus 로고    scopus 로고
    • Enhanced protein steering: Cooperative electrostatic and van der Waals forces in antigen-antibody complexes
    • Persson, B. A.; Jönsson, B.; Lund, M. Enhanced protein steering: cooperative electrostatic and van der Waals forces in antigen-antibody complexes J. Phys. Chem. B 2009, 113, 10459-64 10.1021/jp904541g
    • (2009) J. Phys. Chem. B , vol.113 , pp. 10459-10464
    • Persson, B.A.1    Jönsson, B.2    Lund, M.3
  • 39
    • 0001461682 scopus 로고
    • Hirs, C. H. W., Ed.; Methods in Enzymology; Academic Press: New York
    • Nozaki, Y.; Tanford, C. In Enzyme Structure; Hirs, C. H. W., Ed.; Methods in Enzymology; Academic Press: New York, 1967; Vol. 11, pp 715-734.
    • (1967) Enzyme Structure , vol.11 , pp. 715-734
    • Nozaki, Y.1    Tanford, C.2
  • 40
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • Humphrey, W.; Dalke, a.; Schulten, K. VMD: visual molecular dynamics J. Mol. Graphics 1996, 14 (1) 33-38 10.1016/0263-7855(96)00018-5
    • (1996) J. Mol. Graphics , vol.14 , Issue.1 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 41
    • 0035943181 scopus 로고    scopus 로고
    • Surface Tension of Electrolytes: Specific Ion Effects Explained by Dispersion Forces
    • Boström, M.; Williams, D. R. M.; Ninham, B. W. Surface Tension of Electrolytes: Specific Ion Effects Explained by Dispersion Forces Langmuir 2001, 17, 4475-4478 10.1021/la0102298
    • (2001) Langmuir , vol.17 , pp. 4475-4478
    • Boström, M.1    Williams, D.R.M.2    Ninham, B.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.