메뉴 건너뛰기




Volumn 83, Issue 1, 2011, Pages

Sequence dependence of the binding energy in chaperone-driven polymer translocation through a nanopore

Author keywords

[No Author keywords available]

Indexed keywords

BINDING AFFINITIES; BINDING PROTEINS; MEAN FIRST PASSAGE TIME; MONOMER TYPES; NEAREST-NEIGHBORS; POLYMER TRANSLOCATION; POTENTIAL GRADIENTS; STIFF POLYMERS; TRANS SIDE; TRANSLOCATION DYNAMICS;

EID: 78751501439     PISSN: 15393755     EISSN: 15502376     Source Type: Journal    
DOI: 10.1103/PhysRevE.83.011902     Document Type: Article
Times cited : (48)

References (48)
  • 3
    • 34347237191 scopus 로고    scopus 로고
    • ABBSE4 1056-8700 10.1146/annurev.biophys.36.040306.132622
    • M. Muthukumar, Annu. Rev. Biophys. Biomol. Struct. ABBSE4 1056-8700 10.1146/annurev.biophys.36.040306.132622 36, 435 (2007).
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 435
    • Muthukumar, M.1
  • 4
    • 36749001066 scopus 로고    scopus 로고
    • NATUAS 0028-0836 10.1038/nature06384
    • T. A. Rapoport, Nature (London) NATUAS 0028-0836 10.1038/nature06384 450, 663 (2007).
    • (2007) Nature (London) , vol.450 , pp. 663
    • Rapoport, T.A.1
  • 5
    • 0023699871 scopus 로고
    • See, for instance, NATUAS 0233-111X 10.1002/jobm.3620280703
    • See, for instance, B. B. Griffiths and O. McClain, J. Basic Microbiol. NATUAS 0233-111X 10.1002/jobm.3620280703 28, 427 (1988).
    • (1988) J. Basic Microbiol. , vol.28 , pp. 427
    • Griffiths, B.B.1    McClain, O.2
  • 6
    • 0037855911 scopus 로고    scopus 로고
    • JCOMEL 0953-8984 10.1088/0953-8984/15/17/202
    • A. Meller, J. Phys.: Condens. Matter JCOMEL 0953-8984 10.1088/0953-8984/15/17/202 15, R581 (2003).
    • (2003) J. Phys.: Condens. Matter , vol.15 , pp. 581
    • Meller, A.1
  • 10
    • 34248351114 scopus 로고    scopus 로고
    • NALEFD 1748-3387 10.1038/nnano.2007.27
    • C. Dekker, Nat. Nanotech. NALEFD 1748-3387 10.1038/nnano.2007.27 2, 209 (2007).
    • (2007) Nat. Nanotech. , vol.2 , pp. 209
    • Dekker, C.1
  • 14
    • 0031918163 scopus 로고    scopus 로고
    • BIOJAU 0006-3495 10.1016/S0006-3495(98)77884-1
    • J.-F. Chauwin, G. Oster, and S. Glick, Biophys. J. BIOJAU 0006-3495 10.1016/S0006-3495(98)77884-1 74, 1732 (1998).
    • (1998) Biophys. J. , vol.74 , pp. 1732
    • Chauwin, J.-F.1    Oster, G.2    Glick, S.3
  • 16
  • 19
    • 6144254211 scopus 로고    scopus 로고
    • PRLTAO 0031-9007 10.1103/PhysRevLett.77.783
    • W. Sung and P. J. Park, Phys. Rev. Lett. PRLTAO 0031-9007 10.1103/PhysRevLett.77.783 77, 783 (1996).
    • (1996) Phys. Rev. Lett. , vol.77 , pp. 783
    • Sung, W.1    Park, P.J.2
  • 20
    • 0000102029 scopus 로고    scopus 로고
    • JCPSA6 0021-9606 10.1063/1.480386
    • M. Muthukumar, J. Chem. Phys. JCPSA6 0021-9606 10.1063/1.480386 111, 10371 (1999);
    • (1999) J. Chem. Phys. , vol.111 , pp. 10371
    • Muthukumar, M.1
  • 21
    • 0035794251 scopus 로고    scopus 로고
    • PRLTAO 0031-9007 10.1103/PhysRevLett.86.3188
    • M. Muthukumar, Phys. Rev. Lett. PRLTAO 0031-9007 10.1103/PhysRevLett.86. 3188 86, 3188 (2001);
    • (2001) Phys. Rev. Lett. , vol.86 , pp. 3188
    • Muthukumar, M.1
  • 22
    • 0037444762 scopus 로고    scopus 로고
    • 0021-9606 JCPSA6 10.1063/1.1553753
    • M. Muthukumar, J. Chem. Phys. 0021-9606 JCPSA6 10.1063/1.1553753 118, 5174 (2003).
    • (2003) J. Chem. Phys. , vol.118 , pp. 5174
    • Muthukumar, M.1
  • 23
    • 0032845645 scopus 로고    scopus 로고
    • BIOJAU 0006-3495 10.1016/S0006-3495(99)77027-X
    • D. K. Lubensky and D. R. Nelson, Biophys. J. BIOJAU 0006-3495 10.1016/S0006-3495(99)77027-X 77, 1824 (1999).
    • (1999) Biophys. J. , vol.77 , pp. 1824
    • Lubensky, D.K.1    Nelson, D.R.2
  • 24
    • 37649029134 scopus 로고    scopus 로고
    • BIOJAU 1539-3755 10.1103/PhysRevE.65.011802
    • J. Chuang, Y. Kantor, and M. Kardar, Phys. Rev. E BIOJAU 1539-3755 10.1103/PhysRevE.65.011802 65, 011802 (2001).
    • (2001) Phys. Rev. e , vol.65 , pp. 011802
    • Chuang, J.1    Kantor, Y.2    Kardar, M.3
  • 25
    • 42749107580 scopus 로고    scopus 로고
    • BIOJAU 1539-3755 10.1103/PhysRevE.69.021806
    • Y. Kantor and M. Kardar, Phys. Rev. E BIOJAU 1539-3755 10.1103/PhysRevE.69.021806 69, 021806 (2004).
    • (2004) Phys. Rev. e , vol.69 , pp. 021806
    • Kantor, Y.1    Kardar, M.2
  • 29
    • 77957033308 scopus 로고    scopus 로고
    • EULEEJ 1742-5468 10.1088/1742-5468/2010/07/P07007
    • P. L. Krapivsky and K. Mallick, J. Stat. Mech. EULEEJ 1742-5468 10.1088/1742-5468/2010/07/P07007 (2010) P07007.
    • J. Stat. Mech. , vol.2010 , pp. 07007
    • Krapivsky, P.L.1    Mallick, K.2
  • 34
    • 18744384874 scopus 로고    scopus 로고
    • JCOMEL 1478-3967 10.1088/1478-3967/1/2/004
    • T. Ambjörnsson and R. Metzler, Phys. Biol. JCOMEL 1478-3967 10.1088/1478-3967/1/2/004 1, 77 (2004).
    • (2004) Phys. Biol. , vol.1 , pp. 77
    • Ambjörnsson, T.1    Metzler, R.2
  • 35
    • 2942685818 scopus 로고    scopus 로고
    • BIOJAU 0006-3495 10.1529/biophysj.103.036152
    • Y. Kafri, D. K. Lubensky, and D. R. Nelson, Biophys. J. BIOJAU 0006-3495 10.1529/biophysj.103.036152 86, 3373 (2004).
    • (2004) Biophys. J. , vol.86 , pp. 3373
    • Kafri, Y.1    Lubensky, D.K.2    Nelson, D.R.3
  • 37
    • 78751509423 scopus 로고    scopus 로고
    • Typically, in membrane channels the diffusion of the polymer chain is much slower than in the free solution. This is particularly true for situations in vivo, in which additional effects such as binding of the chain-to-be- translocated to the membrane itself come into play. From that point of view we expect that even for typical chaperone sizes of 60-90 kDA (in comparison, a typical DNA binding protein is twice the size), the assumption of fast kinetics is in order.
    • Typically, in membrane channels the diffusion of the polymer chain is much slower than in the free solution. This is particularly true for situations in vivo, in which additional effects such as binding of the chain-to-be- translocated to the membrane itself come into play. From that point of view we expect that even for typical chaperone sizes of 60-90 kDA (in comparison, a typical DNA binding protein is twice the size), the assumption of fast kinetics is in order.
  • 40
    • 0018196563 scopus 로고
    • BICIAZ 0301-4622 10.1016/0301-4622(78)80015-5
    • I. R. Epstein, Biophys. Chem. BICIAZ 0301-4622 10.1016/0301-4622(78) 80015-5 8, 327 (1978).
    • (1978) Biophys. Chem. , vol.8 , pp. 327
    • Epstein, I.R.1
  • 42
    • 78751546324 scopus 로고    scopus 로고
    • -1.
    • -1.
  • 43
    • 50249187742 scopus 로고    scopus 로고
    • BICIAZ 1539-3755 10.1103/PhysRevE.78.021129
    • C. Chatelain, Y. Kantor, and M. Kardar, Phys. Rev. E BICIAZ 1539-3755 10.1103/PhysRevE.78.021129 78, 021129 (2008).
    • (2008) Phys. Rev. e , vol.78 , pp. 021129
    • Chatelain, C.1    Kantor, Y.2    Kardar, M.3
  • 46
    • 33646411772 scopus 로고    scopus 로고
    • JCOMEL 1539-3755 10.1103/PhysRevE.73.046126
    • J. Alvarez and B. Hajek, Phys. Rev. E JCOMEL 1539-3755 10.1103/PhysRevE.73.046126 73, 046126 (2006).
    • (2006) Phys. Rev. e , vol.73 , pp. 046126
    • Alvarez, J.1    Hajek, B.2
  • 47
    • 78751500053 scopus 로고    scopus 로고
    • +1-rλ-(χλ)r=0.
    • +1 - r λ - (χ λ) r = 0.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.