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Volumn 94, Issue 7, 2008, Pages 2529-2545

Spectrin folding versus unfolding reactions and RBC membrane stiffness

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; SPECTRIN;

EID: 41649086164     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.119438     Document Type: Article
Times cited : (38)

References (57)
  • 2
    • 0035957720 scopus 로고    scopus 로고
    • Reversible infolding of single RNA molecules by mechanical force
    • Liphardt, J., B. Onoa, S. B. Simth, I. Tinoco, Jr., and C. Bustamonte. 2001. Reversible infolding of single RNA molecules by mechanical force. Science. 292:733-737.
    • (2001) Science , vol.292 , pp. 733-737
    • Liphardt, J.1    Onoa, B.2    Simth, S.B.3    Tinoco Jr., I.4    Bustamonte, C.5
  • 3
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief, M., M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub. 1997. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 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
  • 4
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • Rief, M., J. Pascual, M. Saraste, and H. E. Gaub. 1999. Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. J. Mol. Biol. 286:553-561.
    • (1999) J. Mol. Biol , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 6
    • 33751223863 scopus 로고    scopus 로고
    • Examining the influence of linkers and tertiary structure in the forced unfolding of multiple-repeat spectrin molecules
    • Paramore, S., and G. A. Voth. 2006. Examining the influence of linkers and tertiary structure in the forced unfolding of multiple-repeat spectrin molecules. Biophys. J. 91:3436-3445.
    • (2006) Biophys. J , vol.91 , pp. 3436-3445
    • Paramore, S.1    Voth, G.A.2
  • 7
    • 0034612284 scopus 로고    scopus 로고
    • Unfolding proteins by external force and temperature: The importance of topology and energetics
    • Paci, E., and M. Karplus. 2000. Unfolding proteins by external force and temperature: the importance of topology and energetics. Proc. Natl. Acad. Sci. USA. 97:6521-6526.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6521-6526
    • Paci, E.1    Karplus, M.2
  • 8
    • 34249930159 scopus 로고    scopus 로고
    • Single-molecule experiments in vitro and in silico
    • Sotomayor, M., and K. Schulten. 2007. Single-molecule experiments in vitro and in silico. Science. 316:1144-1148.
    • (2007) Science , vol.316 , pp. 1144-1148
    • Sotomayor, M.1    Schulten, K.2
  • 10
    • 0030053840 scopus 로고    scopus 로고
    • An elastic network model based on the structure of the red blood cell membrane skeleton
    • Hansen, J. C., R. Skalak, S. Chien, and A. Hoger. 1996. An elastic network model based on the structure of the red blood cell membrane skeleton. Biophys. J. 70:146-166.
    • (1996) Biophys. J , vol.70 , pp. 146-166
    • Hansen, J.C.1    Skalak, R.2    Chien, S.3    Hoger, A.4
  • 11
    • 0031705402 scopus 로고    scopus 로고
    • Simulations of the erythrocyte cytoskeleton at large deformation. II. Micropipette aspiration
    • Discher, D. E., D. H. Boal, and S. K. Boey. 1998. Simulations of the erythrocyte cytoskeleton at large deformation. II. Micropipette aspiration. Biophys. J. 75:1584-1597.
    • (1998) Biophys. J , vol.75 , pp. 1584-1597
    • Discher, D.E.1    Boal, D.H.2    Boey, S.K.3
  • 12
    • 33746693025 scopus 로고    scopus 로고
    • Molecularly based analysis of deformation of spectrin network and human erythrocyte
    • Dao, M., J. Li, and S. Suresh. 2006. Molecularly based analysis of deformation of spectrin network and human erythrocyte. Mater. Sci. Eng. C. 26:1232-1244.
    • (2006) Mater. Sci. Eng. C , vol.26 , pp. 1232-1244
    • Dao, M.1    Li, J.2    Suresh, S.3
  • 13
    • 0035193296 scopus 로고    scopus 로고
    • Deformation-enhanced fluctuations in the red cell skeleton with theoretical relations to elasticity, connectivity, and spectrin unfolding
    • Lee, J. C. M., and D. E. Discher. 2001. Deformation-enhanced fluctuations in the red cell skeleton with theoretical relations to elasticity, connectivity, and spectrin unfolding. Biophys. J. 81:3178-3192.
    • (2001) Biophys. J , vol.81 , pp. 3178-3192
    • Lee, J.C.M.1    Discher, D.E.2
  • 14
    • 0037200093 scopus 로고    scopus 로고
    • Shear-response of the spectrin dimer-tetramer equilibrium in the red blood cell membrane
    • An, X., M. C. Lecomte, J. A. Chasis, N. Mohandas, and W. Gratzer. 2002. Shear-response of the spectrin dimer-tetramer equilibrium in the red blood cell membrane. J. Biol. Chem. 277:31796-31800.
    • (2002) J. Biol. Chem , vol.277 , pp. 31796-31800
    • An, X.1    Lecomte, M.C.2    Chasis, J.A.3    Mohandas, N.4    Gratzer, W.5
  • 16
    • 17844376298 scopus 로고    scopus 로고
    • Nonlinear elastic and viscoelastic deformation of the human red blood cell with optical tweezers
    • Mills, J. P., L. Qie, M. Dao, C. T. Lim, and S. Suresh. 2004. Nonlinear elastic and viscoelastic deformation of the human red blood cell with optical tweezers. Mech. Chem. Biosys. 1:169-180.
    • (2004) Mech. Chem. Biosys , vol.1 , pp. 169-180
    • Mills, J.P.1    Qie, L.2    Dao, M.3    Lim, C.T.4    Suresh, S.5
  • 17
    • 34447305217 scopus 로고    scopus 로고
    • A hybrid model for erythrocyte membrane: A single unit of protein network coupled with lipid bilayer
    • Zhu, Q., C. Vera, R. Asaro, P. Sche, and A. L. P. Sung. 2007. A hybrid model for erythrocyte membrane: a single unit of protein network coupled with lipid bilayer. Biophys. J. 93:386-400.
    • (2007) Biophys. J , vol.93 , pp. 386-400
    • Zhu, Q.1    Vera, C.2    Asaro, R.3    Sche, P.4    Sung, A.L.P.5
  • 18
    • 0022599356 scopus 로고
    • The present status of erythrocyte spectrin structure: The 106-residue repetitive structure is a basic feature of an entire class of proteins
    • Speicher, D. W. 1986. The present status of erythrocyte spectrin structure: the 106-residue repetitive structure is a basic feature of an entire class of proteins. J. Cell Biol. 30:245-258.
    • (1986) J. Cell Biol , vol.30 , pp. 245-258
    • Speicher, D.W.1
  • 21
    • 0027333413 scopus 로고
    • The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane
    • Bennet, V., and D. M. Gilligan. 1993. The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane. Annu. Rev. Cell Biol. 9:27-66.
    • (1993) Annu. Rev. Cell Biol , vol.9 , pp. 27-66
    • Bennet, V.1    Gilligan, D.M.2
  • 23
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell, G. J. 1978. Models for the specific adhesion of cells to cells. Science. 200:618-627.
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.J.1
  • 24
    • 36749076615 scopus 로고    scopus 로고
    • Single molecule studies of protein folding using atomic force microscopy
    • Ng, S. P., L. G. Randles, and J. Clarke. 2007. Single molecule studies of protein folding using atomic force microscopy. Methods Mol. Biol. 350:139-167.
    • (2007) Methods Mol. Biol , vol.350 , pp. 139-167
    • Ng, S.P.1    Randles, L.G.2    Clarke, J.3
  • 25
    • 0032988663 scopus 로고    scopus 로고
    • Strength of a weak bond connecting flexible polymer chains
    • Evans, E., and K. Ritchie. 1999. Strength of a weak bond connecting flexible polymer chains. Biophys. J. 76:2439-2447.
    • (1999) Biophys. J , vol.76 , pp. 2439-2447
    • Evans, E.1    Ritchie, K.2
  • 26
    • 7044226061 scopus 로고    scopus 로고
    • The folding of spectrin domains. I. Wild-type domains have the same stability but very different kinetic properties
    • Scott, K. A., S. Batey, K. A. Hooton, and J. Clarke. 2004. The folding of spectrin domains. I. Wild-type domains have the same stability but very different kinetic properties. J. Mol. Biol. 344:195-205.
    • (2004) J. Mol. Biol , vol.344 , pp. 195-205
    • Scott, K.A.1    Batey, S.2    Hooton, K.A.3    Clarke, J.4
  • 27
    • 33646000631 scopus 로고    scopus 로고
    • Complex folding kinetics of a multidomain protein
    • Batey, S., K. A. Scott, and J. Clarke. 2006. Complex folding kinetics of a multidomain protein. Biophys. J. 90:2120-2130.
    • (2006) Biophys. J , vol.90 , pp. 2120-2130
    • Batey, S.1    Scott, K.A.2    Clarke, J.3
  • 28
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans, E., and K. Ritchie. 1997. Dynamic strength of molecular adhesion bonds. Biophys. J. 72:1541-1555.
    • (1997) Biophys. J , vol.72 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 29
    • 0022344550 scopus 로고
    • Visualization of the protein associations in the RBC membrane skeleton
    • Byers, T. J., and D. Branton. 1985. Visualization of the protein associations in the RBC membrane skeleton. Proc. Natl. Acad. Sci. USA. 82:6153-6157.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6153-6157
    • Byers, T.J.1    Branton, D.2
  • 30
    • 0022486512 scopus 로고
    • Ultrastructure of the intact skeleton of the human RBC membrane
    • Shen, B. W., R. Josephs, and T. L. Steck. 1986. Ultrastructure of the intact skeleton of the human RBC membrane. J. Cell Biol. 102:997-1006.
    • (1986) J. Cell Biol , vol.102 , pp. 997-1006
    • Shen, B.W.1    Josephs, R.2    Steck, T.L.3
  • 31
    • 0023150141 scopus 로고
    • Visualization of the hexagonal lattice in the RBC membrane skeleton
    • Liu, S. C., L. H. Derick, and J. Palek. 1987. Visualization of the hexagonal lattice in the RBC membrane skeleton. J. Cell Biol. 104:527-536.
    • (1987) J. Cell Biol , vol.104 , pp. 527-536
    • Liu, S.C.1    Derick, L.H.2    Palek, J.3
  • 32
    • 1042289028 scopus 로고    scopus 로고
    • Protofilament and Hexagon: A three-dimensional mechanical model for the junctional complex in the erythrocyte membrane skeleton
    • Sung, L. A., and C. Vera. 2003. Protofilament and Hexagon: A three-dimensional mechanical model for the junctional complex in the erythrocyte membrane skeleton. Ann. Biomed. Eng. 31:1314-1326.
    • (2003) Ann. Biomed. Eng , vol.31 , pp. 1314-1326
    • Sung, L.A.1    Vera, C.2
  • 33
    • 27244459575 scopus 로고    scopus 로고
    • 3-D nanomechanics of an erythrocyte junctional complex in equibiaxial and anisotropic deformations
    • Vera, C., R. Skelton, F. Bossens, and L. A. Sung. 2005. 3-D nanomechanics of an erythrocyte junctional complex in equibiaxial and anisotropic deformations. Ann. Biomed. Eng. 33:1387-1404.
    • (2005) Ann. Biomed. Eng , vol.33 , pp. 1387-1404
    • Vera, C.1    Skelton, R.2    Bossens, F.3    Sung, L.A.4
  • 34
    • 0031386328 scopus 로고    scopus 로고
    • From semi-flexible polymers to membranes: Anomalous diffusion and reptation
    • Granek, R. 1997. From semi-flexible polymers to membranes: anomalous diffusion and reptation. J. Phys. III (Fr.). 7:1761-1788.
    • (1997) J. Phys. III (Fr.) , vol.7 , pp. 1761-1788
    • Granek, R.1
  • 35
    • 27244439049 scopus 로고    scopus 로고
    • Dynamic simulations of membranes with cytoskeletal interactions
    • Lin, L. C., and F. L. Brown. 2005. Dynamic simulations of membranes with cytoskeletal interactions. Phys. Rev. E Stat. Nonlin. Soft Matter Phys. 72:011910.
    • (2005) Phys. Rev. E Stat. Nonlin. Soft Matter Phys , vol.72 , pp. 011910
    • Lin, L.C.1    Brown, F.L.2
  • 37
    • 85003368853 scopus 로고    scopus 로고
    • Cytoskeleton confinement and tension of red blood cell membranes
    • Gov, N., A. G. Zilman, and S. Safran. 2003. Cytoskeleton confinement and tension of red blood cell membranes. Phys. Rev. Lett. 90:228101.
    • (2003) Phys. Rev. Lett , vol.90 , pp. 228101
    • Gov, N.1    Zilman, A.G.2    Safran, S.3
  • 38
    • 17844385622 scopus 로고    scopus 로고
    • Red blood cell membrane fluctuations and shape controlled by ATP-induced cytoskeleton defects
    • Gov, N., and S. Safran. 2005. Red blood cell membrane fluctuations and shape controlled by ATP-induced cytoskeleton defects. Biophys. J. 88:1859-1874.
    • (2005) Biophys. J , vol.88 , pp. 1859-1874
    • Gov, N.1    Safran, S.2
  • 40
    • 0000279210 scopus 로고
    • Flagellar hydrodynamics: The John von Neumann Lecture
    • Lighthill, J. 1976. Flagellar hydrodynamics: The John von Neumann Lecture. SIAM Rev. 18:161-230.
    • (1976) SIAM Rev , vol.18 , pp. 161-230
    • Lighthill, J.1
  • 41
    • 0004168443 scopus 로고
    • 6th Ed. Dover Publications, Mineola, NY
    • Lamb, H. 1932. Hydrodynamics, 6th Ed. Dover Publications, Mineola, NY.
    • (1932) Hydrodynamics
    • Lamb, H.1
  • 42
    • 0027938023 scopus 로고
    • Molecular maps of red cell deformation: Hidden elasticity and in situ connectivity
    • Discher, D. E., N. Mohandas, and E. A. Evans. 1994. Molecular maps of red cell deformation: hidden elasticity and in situ connectivity. Science. 266:1032-1035.
    • (1994) Science , vol.266 , pp. 1032-1035
    • Discher, D.E.1    Mohandas, N.2    Evans, E.A.3
  • 43
    • 0036978164 scopus 로고    scopus 로고
    • Elasticity of the human red blood cell skeleton
    • Lenormand, G., S. Henon, A. Richert, and F. Gallet. 2003. Elasticity of the human red blood cell skeleton. Biorheology. 40:247-251.
    • (2003) Biorheology , vol.40 , pp. 247-251
    • Lenormand, G.1    Henon, S.2    Richert, A.3    Gallet, F.4
  • 44
    • 0026671203 scopus 로고
    • Conformation and elasticity of the isolated red-blood-cell membrane skeleton
    • Scoboda, K., C. F. Schmidt, D. Branton, and S. M. Block. 1992. Conformation and elasticity of the isolated red-blood-cell membrane skeleton. Biophys. J. 63:784-793.
    • (1992) Biophys. J , vol.63 , pp. 784-793
    • Scoboda, K.1    Schmidt, C.F.2    Branton, D.3    Block, S.M.4
  • 46
    • 0016920748 scopus 로고
    • Brownian motion in thin sheets of viscous fluid
    • Saffman, P. G. 1976. Brownian motion in thin sheets of viscous fluid. J. Fluid Mech. 73:593-602.
    • (1976) J. Fluid Mech , vol.73 , pp. 593-602
    • Saffman, P.G.1
  • 47
    • 0032774449 scopus 로고    scopus 로고
    • Actin protofilament orientation at the erythrocyte membrane
    • Picart, C., and D. E. Discher. 1999. Actin protofilament orientation at the erythrocyte membrane. Biophys. J. 77:865-878.
    • (1999) Biophys. J , vol.77 , pp. 865-878
    • Picart, C.1    Discher, D.E.2
  • 48
    • 0033638280 scopus 로고    scopus 로고
    • Actin protofilament orientation in deformation of the erythrocyte membrane skeleton
    • Picart, C., P. Dalhaimer, and D. E. Discher. 2000. Actin protofilament orientation in deformation of the erythrocyte membrane skeleton. Biophys. J. 79:2987-3000.
    • (2000) Biophys. J , vol.79 , pp. 2987-3000
    • Picart, C.1    Dalhaimer, P.2    Discher, D.E.3
  • 52
    • 0024418550 scopus 로고
    • A thermodynamic model for the self-association of human spectrin
    • Morris, M., and G. B. Ralston. 1989. A thermodynamic model for the self-association of human spectrin. Biochemistry. 28:8561-8667.
    • (1989) Biochemistry , vol.28 , pp. 8561-8667
    • Morris, M.1    Ralston, G.B.2
  • 53
    • 0026470325 scopus 로고
    • Analysis of human red cell spectrin tetramer (head-to-head) assembly using complimentary univalent peptides
    • DeSilva, T. M., K.-C. Peng, K. D. Speicher, and D. W. Speicher. 1992. Analysis of human red cell spectrin tetramer (head-to-head) assembly using complimentary univalent peptides. Biochemistry. 31:10872-10878.
    • (1992) Biochemistry , vol.31 , pp. 10872-10878
    • DeSilva, T.M.1    Peng, K.-C.2    Speicher, K.D.3    Speicher, D.W.4
  • 54
    • 0009509734 scopus 로고
    • Defective spectrin dimerdimer association in hereditary elliptocytosis
    • Liu, S.-C., J. Palek, and J. T. Prchal. 1982. Defective spectrin dimerdimer association in hereditary elliptocytosis. Proc. Natl. Acad. Sci. USA. 79:2072-2076.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2072-2076
    • Liu, S.-C.1    Palek, J.2    Prchal, J.T.3
  • 55
    • 0018099901 scopus 로고
    • Self-association of human spectrin, a thermodynamic and kinetic study
    • Ungewickell, E., and W. Gratzer. 1978. Self-association of human spectrin, a thermodynamic and kinetic study. Eur. J. Biochem. 88:379-385.
    • (1978) Eur. J. Biochem , vol.88 , pp. 379-385
    • Ungewickell, E.1    Gratzer, W.2
  • 56
    • 33846314328 scopus 로고    scopus 로고
    • Reversible stress softening of actin networks
    • Chaudhuri, O., S. H. Parekh, and D. A. Fletcher. 2007. Reversible stress softening of actin networks. Nature. 445:295-298.
    • (2007) Nature , vol.445 , pp. 295-298
    • Chaudhuri, O.1    Parekh, S.H.2    Fletcher, D.A.3
  • 57
    • 0031708414 scopus 로고    scopus 로고
    • Simulations of the erythrocyte cytoskeleton at large deformations. I. Microscopic models
    • Boey, S. K., D. H. Boal, and D. E. Discher. 1998. Simulations of the erythrocyte cytoskeleton at large deformations. I. Microscopic models. Biophys. J. 75:1573-1583.
    • (1998) Biophys. J , vol.75 , pp. 1573-1583
    • Boey, S.K.1    Boal, D.H.2    Discher, D.E.3


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