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Volumn 104, Issue 19, 2010, Pages

Molecular dynamics simulation of the α-helix to β-sheet transition in coiled protein filaments: Evidence for a critical filament length scale

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA-HELICAL PROTEINS; ALPHA-HELIX; ASYMPTOTIC LIMITS; BETA-SHEET; CELLULAR PROTEINS; DEFORMATION MECHANISM; ENERGY DISSIPATION CAPACITIES; FUNDAMENTAL PHYSICS; HELICAL COILED-COIL; HELICAL DOMAINS; LARGE DEFORMATIONS; LENGTH SCALE; MOLECULAR DYNAMICS SIMULATIONS; PROTEIN FILAMENTS; THEORETICAL MODELING;

EID: 77952330147     PISSN: 00319007     EISSN: 10797114     Source Type: Journal    
DOI: 10.1103/PhysRevLett.104.198304     Document Type: Article
Times cited : (137)

References (33)
  • 2
    • 0028176595 scopus 로고
    • NATUAS 0028-0836 10.1038/367660a0
    • D.L. Minor and P.S. Kim, Nature (London) 367, 660 (1994). NATUAS 0028-0836 10.1038/367660a0
    • (1994) Nature (London) , vol.367 , pp. 660
    • Minor, D.L.1    Kim, P.S.2
  • 3
    • 0037416708 scopus 로고    scopus 로고
    • CEUJED 0947-6539 10.1002/chem.200390132
    • T. Koga, Chem. Eur. J. 9, 1146 (2003). CEUJED 0947-6539 10.1002/chem.200390132
    • (2003) Chem. Eur. J. , vol.9 , pp. 1146
    • Koga, T.1
  • 5
    • 38349121952 scopus 로고    scopus 로고
    • JACSAT 0002-7863 10.1021/ja077231r
    • M. Meier and J. Seelig, J. Am. Chem. Soc. 130, 1017 (2008). JACSAT 0002-7863 10.1021/ja077231r
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 1017
    • Meier, M.1    Seelig, J.2
  • 6
    • 0031973356 scopus 로고    scopus 로고
    • The effects of stretching on wool fibres as monitored by FT-Raman spectroscopy
    • DOI 10.1016/S0022-2860(97)00227-5, PII S0022286097002275
    • J.S. Church, G.L. Corino, and A.L. Woodhead, J. Mol. Struct. 440, 15 (1998). JMOSB4 0022-2860 10.1016/S0022-2860(97)00227-5 (Pubitemid 28042652)
    • (1998) Journal of Molecular Structure , vol.440 , Issue.1-3 , pp. 15-23
    • Church, J.S.1    Corino, G.L.2    Woodhead, A.L.3
  • 7
    • 3042816944 scopus 로고    scopus 로고
    • New aspects of the α-helix to β-sheet transition in stretched hard α-keratin fibers
    • DOI 10.1529/biophysj.103.036749
    • L. Kreplak, Biophys. J. 87, 640 (2004). BIOJAU 0006-3495 10.1529/biophysj.103.036749 (Pubitemid 38880116)
    • (2004) Biophysical Journal , vol.87 , Issue.1 , pp. 640-647
    • Kreplak, L.1    Doucet, J.2    Dumas, P.3    Briki, F.4
  • 8
    • 0041319662 scopus 로고    scopus 로고
    • BIOJAU 0006-3495 10.1016/S0006-3495(03)74629-3
    • D.S. Fudge, Biophys. J. 85, 2015 (2003). BIOJAU 0006-3495 10.1016/S0006-3495(03)74629-3
    • (2003) Biophys. J. , vol.85 , pp. 2015
    • Fudge, D.S.1
  • 9
    • 41649116913 scopus 로고    scopus 로고
    • BIOJAU 0006-3495 10.1529/biophysj.107.119826
    • L. Kreplak, Biophys. J. 94, 2790 (2008). BIOJAU 0006-3495 10.1529/biophysj.107.119826
    • (2008) Biophys. J. , vol.94 , pp. 2790
    • Kreplak, L.1
  • 10
    • 70349713574 scopus 로고    scopus 로고
    • 1932-6203 10.1371/journal.pone.0007294
    • Z. Qin, PLoS ONE 4, e7294 (2009). 1932-6203 10.1371/journal.pone.0007294
    • (2009) PLoS ONE , vol.4 , pp. 7294
    • Qin, Z.1
  • 11
    • 0034584899 scopus 로고    scopus 로고
    • CPPSCM 1389-2037 10.2174/1389203003381289
    • M. Gross, Current Protein & Peptide Science CPPSCM 1389-2037 1, 339 (2000). 10.2174/1389203003381289
    • (2000) Current Protein & Peptide Science , vol.1 , pp. 339
    • Gross, M.1
  • 13
    • 60949107887 scopus 로고    scopus 로고
    • NMAACR 1476-1122 10.1038/nmat2387
    • M.J. Buehler and Y.C. Yung, Nature Mater. 8, 175 (2009). NMAACR 1476-1122 10.1038/nmat2387
    • (2009) Nature Mater. , vol.8 , pp. 175
    • Buehler, M.J.1    Yung, Y.C.2
  • 14
    • 0033954256 scopus 로고    scopus 로고
    • NARHAD 0305-1048 10.1093/nar/28.1.235
    • H.M. Berman, Nucleic Acids Res. 28, 235 (2000). NARHAD 0305-1048 10.1093/nar/28.1.235
    • (2000) Nucleic Acids Res. , vol.28 , pp. 235
    • Berman, H.M.1
  • 15
    • 0031465967 scopus 로고    scopus 로고
    • 'New view' of protein folding reconciled with the old through multiple unfolding simulations
    • DOI 10.1126/science.278.5345.1928
    • T. Lazaridis and M. Karplus, Science 278, 1928 (1997). SCIEAS 0036-8075 10.1126/science.278.5345.1928 (Pubitemid 28013230)
    • (1997) Science , vol.278 , Issue.5345 , pp. 1928-1931
    • Lazaridis, T.1    Karplus, M.2
  • 16
    • 0033135638 scopus 로고    scopus 로고
    • Effective energy function for proteins in solution
    • DOI 10.1002/(SICI)1097-0134(19990501)35:2<133::AID-PROT1>3.0.CO;2-N
    • T. Lazaridis and M. Karplus, Proteins: Struct. Funct. Genet. PSFGEY 0887-3585 35, 133 (1999). 10.1002/(SICI)1097-0134(19990501)35:2<133::AID- PROT1>3.0.CO;2-N (Pubitemid 29165128)
    • (1999) Proteins: Structure, Function and Genetics , vol.35 , Issue.2 , pp. 133-152
    • Lazaridis, T.1    Karplus, M.2
  • 18
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • DOI 10.1016/0263-7855(96)00018-5
    • We use visual molecular dynamics (VMD), W. Humphrey, A. Dalke, and K. Schulten, J. Mol. Graphics JMGRDV 0263-7855 14, 33 (1996), for visualization. The rupture length of H bonds is defined to be 5 Å for visualization purposes. 10.1016/0263-7855(96)00018-5 (Pubitemid 26152973)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 19
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • DOI 10.1002/prot.340230412
    • D. Frishman and P. Argos, Proteins: Struct. Funct. Genet. PSFGEY 0887-3585 23, 566 (1995). 10.1002/prot.340230412 (Pubitemid 26009520)
    • (1995) Proteins: Structure, Function and Genetics , vol.23 , Issue.4 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 20
    • 0036977558 scopus 로고    scopus 로고
    • NMAACR 1476-1122 10.1038/nmat776
    • I. Schwaiger, Nature Mater. 1, 232 (2002). NMAACR 1476-1122 10.1038/nmat776
    • (2002) Nature Mater. , vol.1 , pp. 232
    • Schwaiger, I.1
  • 21
    • 33646172749 scopus 로고    scopus 로고
    • BIOJAU 0006-3495 10.1529/biophysj.105.071597
    • D.D. Root, Biophys. J. 90, 2852 (2006). BIOJAU 0006-3495 10.1529/biophysj.105.071597
    • (2006) Biophys. J. , vol.90 , pp. 2852
    • Root, D.D.1
  • 22
    • 34249930159 scopus 로고    scopus 로고
    • Single-molecule experiments in vitro and in silico
    • DOI 10.1126/science.1137591
    • M. Sotomayor and K. Schulten, Science 316, 1144 (2007). SCIEAS 0036-8075 10.1126/science.1137591 (Pubitemid 46877468)
    • (2007) Science , vol.316 , Issue.5828 , pp. 1144-1148
    • Sotomayor, M.1    Schulten, K.2
  • 23
    • 40449091784 scopus 로고    scopus 로고
    • Geometric confinement governs the rupture strength of h-bond assemblies at a critical length scale
    • DOI 10.1021/nl0731670
    • S. Keten and M.J. Buehler, Nano Lett. 8, 743 (2008). NALEFD 1530-6984 10.1021/nl0731670 (Pubitemid 351346050)
    • (2008) Nano Letters , vol.8 , Issue.2 , pp. 743-748
    • Keten, S.1    Buehler, M.J.2
  • 24
    • 43449096360 scopus 로고    scopus 로고
    • Asymptotic strength limit of hydrogen-bond assemblies in proteins at vanishing pulling rates
    • DOI 10.1103/PhysRevLett.100.198301
    • S. Keten and M.J. Buehler, Phys. Rev. Lett. 100, 198301 (2008). PRLTAO 0031-9007 10.1103/PhysRevLett.100.198301 (Pubitemid 351671510)
    • (2008) Physical Review Letters , vol.100 , Issue.19 , pp. 198301
    • Keten, S.1    Buehler, M.J.2
  • 26
    • 11544281834 scopus 로고    scopus 로고
    • PRLTAO 0031-9007 10.1103/PhysRevLett.81.4764
    • M. Rief, Phys. Rev. Lett. 81, 4764 (1998). PRLTAO 0031-9007 10.1103/PhysRevLett.81.4764
    • (1998) Phys. Rev. Lett. , vol.81 , pp. 4764
    • Rief, M.1
  • 27
    • 0034979287 scopus 로고    scopus 로고
    • Probing the relation between force - Lifetime - And chemistry in single molecular bonds
    • DOI 10.1146/annurev.biophys.30.1.105
    • E. Evans, Annu. Rev. Biophys. Biomol. Struct. 30, 105 (2001). ABBSE4 1056-8700 10.1146/annurev.biophys.30.1.105 (Pubitemid 32566158)
    • (2001) Annual Review of Biophysics and Biomolecular Structure , vol.30 , pp. 105-128
    • Evans, E.1
  • 28
    • 0018101150 scopus 로고
    • SCIEAS 0036-8075 10.1126/science.347575
    • G.I. Bell, Science 200, 618 (1978). SCIEAS 0036-8075 10.1126/science. 347575
    • (1978) Science , vol.200 , pp. 618
    • Bell, G.I.1
  • 29
    • 40849142370 scopus 로고    scopus 로고
    • Elastic bond network model for protein unfolding mechanics
    • DOI 10.1103/PhysRevLett.100.098101
    • H. Dietz and M. Rief, Phys. Rev. Lett. 100, 098101 (2008). PRLTAO 0031-9007 10.1103/PhysRevLett.100.098101 (Pubitemid 351399047)
    • (2008) Physical Review Letters , vol.100 , Issue.9 , pp. 098101
    • Dietz, H.1    Rief, M.2
  • 31
    • 70349662344 scopus 로고    scopus 로고
    • NNOTER 0957-4484 10.1088/0957-4484/20/42/425101
    • Z. Qin, Nanotechnology 20, 425101 (2009). NNOTER 0957-4484 10.1088/0957-4484/20/42/425101
    • (2009) Nanotechnology , vol.20 , pp. 425101
    • Qin, Z.1
  • 32
    • 70350536555 scopus 로고    scopus 로고
    • 1932-6203 10.1371/journal.pone.0007296
    • M. de Leeuw, PLoS ONE 4, e7296 (2009). 1932-6203 10.1371/journal.pone. 0007296
    • (2009) PLoS ONE , vol.4 , pp. 7296
    • De Leeuw, M.1


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