메뉴 건너뛰기




Volumn 349, Issue 5, 2005, Pages 1045-1059

Cooperative folding in a multi-domain protein

Author keywords

Alpha helix; Cooperativity; m value; Multi domain; Protein folding

Indexed keywords

FODRIN; PROTEIN SUBUNIT; SODIUM CHLORIDE; SPECTRIN;

EID: 20344406783     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.04.028     Document Type: Article
Times cited : (62)

References (32)
  • 1
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • S.E. Jackson How do small single-domain proteins fold? Fold. Des. 3 1998 R81 R91
    • (1998) Fold. Des. , vol.3
    • Jackson, S.E.1
  • 2
    • 0037221599 scopus 로고    scopus 로고
    • Is there a unifying mechanism for protein folding?
    • V. Daggett, and A.R. Fersht Is there a unifying mechanism for protein folding? Trends Biochem. Sci. 28 2003 18 25
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 18-25
    • Daggett, V.1    Fersht, A.R.2
  • 4
    • 23444449882 scopus 로고
    • Building protein structure and function from modular units
    • I.D. Campbell, and A.K. Downing Building protein structure and function from modular units Trends Biotechnol. 12 1994 168 172
    • (1994) Trends Biotechnol. , vol.12 , pp. 168-172
    • Campbell, I.D.1    Downing, A.K.2
  • 6
    • 0031556949 scopus 로고    scopus 로고
    • Module-module interactions in the cell binding region of fibronectin: Stability, flexibility and specificity
    • C. Spitzfaden, R.P. Grant, H.J. Mardon, and I.D. Campbell Module-module interactions in the cell binding region of fibronectin: stability, flexibility and specificity J. Mol. Biol. 265 1997 565 579
    • (1997) J. Mol. Biol. , vol.265 , pp. 565-579
    • Spitzfaden, C.1    Grant, R.P.2    Mardon, H.J.3    Campbell, I.D.4
  • 7
    • 0035914421 scopus 로고    scopus 로고
    • The eighth FIII domain of human fibronectin promotes integrin alpha5beta1 binding via stabilization of the ninth FIII domain
    • H. Altroff, C.F. van der Walle, J. Asselin, R. Fairless, I.D. Campbell, and H.J. Mardon The eighth FIII domain of human fibronectin promotes integrin alpha5beta1 binding via stabilization of the ninth FIII domain J. Biol. Chem. 276 2001 38885 38892
    • (2001) J. Biol. Chem. , vol.276 , pp. 38885-38892
    • Altroff, H.1    Van Der Walle, C.F.2    Asselin, J.3    Fairless, R.4    Campbell, I.D.5    Mardon, H.J.6
  • 9
    • 0028058747 scopus 로고
    • Immunoglobulin-type domains of titin are stabilized by amino-terminal extension
    • A.S. Politou, M. Gautel, C. Joseph, and A. Pastore Immunoglobulin-type domains of titin are stabilized by amino-terminal extension FEBS Letters 352 1994 27 31
    • (1994) FEBS Letters , vol.352 , pp. 27-31
    • Politou, A.S.1    Gautel, M.2    Joseph, C.3    Pastore, A.4
  • 10
    • 0032474435 scopus 로고    scopus 로고
    • The effect of boundary selection on the stability and folding of the third fibronectin type III domain from human tenascin
    • S.J. Hamill, A.E. Meekhof, and J. Clarke The effect of boundary selection on the stability and folding of the third fibronectin type III domain from human tenascin Biochemistry 37 1998 8071 8079
    • (1998) Biochemistry , vol.37 , pp. 8071-8079
    • Hamill, S.J.1    Meekhof, A.E.2    Clarke, J.3
  • 11
    • 0037053429 scopus 로고    scopus 로고
    • Sequence conservation in Ig-like domains: The role of highly conserved proline residues in the fibronectin type III superfamily
    • A. Steward, S. Adhya, and J. Clarke Sequence conservation in Ig-like domains: the role of highly conserved proline residues in the fibronectin type III superfamily J. Mol. Biol. 318 2002 935 940
    • (2002) J. Mol. Biol. , vol.318 , pp. 935-940
    • Steward, A.1    Adhya, S.2    Clarke, J.3
  • 12
    • 0036304229 scopus 로고    scopus 로고
    • Titin; A multidomain protein that behaves as the sum of its parts
    • K.A. Scott, A. Steward, S.B. Fowler, and J. Clarke Titin; a multidomain protein that behaves as the sum of its parts J. Mol. Biol. 315 2002 819 829
    • (2002) J. Mol. Biol. , vol.315 , pp. 819-829
    • Scott, K.A.1    Steward, A.2    Fowler, S.B.3    Clarke, J.4
  • 13
    • 0034874601 scopus 로고    scopus 로고
    • Stability and folding rates of domains spanning the large A-band super-repeat of titin
    • J.G. Head, A. Houmeida, P.J. Knight, A.R. Clarke, J. Trinick, and R.L. Brady Stability and folding rates of domains spanning the large A-band super-repeat of titin Biophys. J. 81 2001 1570 1579
    • (2001) Biophys. J. , vol.81 , pp. 1570-1579
    • Head, J.G.1    Houmeida, A.2    Knight, P.J.3    Clarke, A.R.4    Trinick, J.5    Brady, R.L.6
  • 14
    • 0035799317 scopus 로고    scopus 로고
    • Free energies of urea and of thermal unfolding show that two tandem repeats of spectrin are thermodynamically more stable than a single repeat
    • R.I. Macdonald, and E.V. Pozharski Free energies of urea and of thermal unfolding show that two tandem repeats of spectrin are thermodynamically more stable than a single repeat Biochemistry 40 2001 3974 3984
    • (2001) Biochemistry , vol.40 , pp. 3974-3984
    • MacDonald, R.I.1    Pozharski, E.V.2
  • 15
    • 0022646311 scopus 로고
    • Spectrin, human-erythrocyte shapes, and mechanochemical properties
    • B.T. Stokke, A. Mikkelsen, and A. Elgsaeter Spectrin, human-erythrocyte shapes, and mechanochemical properties Biophys J. 49 1986 319 327
    • (1986) Biophys J. , vol.49 , pp. 319-327
    • Stokke, B.T.1    Mikkelsen, A.2    Elgsaeter, A.3
  • 16
    • 0021272595 scopus 로고
    • Erythrocyte spectrin is comprised of many homologous triple helical segments
    • D.W. Speicher, and V.T. Marchesi Erythrocyte spectrin is comprised of many homologous triple helical segments Nature 311 1984 177 180
    • (1984) Nature , vol.311 , pp. 177-180
    • Speicher, D.W.1    Marchesi, V.T.2
  • 17
    • 0031592935 scopus 로고    scopus 로고
    • Solution structure of the spectrin repeat: A left-handed antipararallel triple-helical coiled-coil
    • J. Pascual, M. Pfuhl, D. Walther, M. Saraste, and M. Nilges Solution structure of the spectrin repeat: a left-handed antipararallel triple-helical coiled-coil J. Mol. Biol. 273 1997 740 751
    • (1997) J. Mol. Biol. , vol.273 , pp. 740-751
    • Pascual, J.1    Pfuhl, M.2    Walther, D.3    Saraste, M.4    Nilges, M.5
  • 18
    • 0033588274 scopus 로고    scopus 로고
    • Structures of two repeats of spectrin suggest models of flexibility
    • V.L. Grum, D. Li, R.I. Macdonald, and A. Mondragon Structures of two repeats of spectrin suggest models of flexibility Cell 98 1999 523 535
    • (1999) Cell , vol.98 , pp. 523-535
    • Grum, V.L.1    Li, D.2    MacDonald, R.I.3    Mondragon, A.4
  • 19
    • 7444232111 scopus 로고    scopus 로고
    • Independent movement, dimerization and stability of tandem repeats of chicken brain alpha-spectrin
    • H. Kusunoki, G. Minasov, R.I. Macdonald, and A. Mondragon Independent movement, dimerization and stability of tandem repeats of chicken brain alpha-spectrin J. Mol. Biol. 344 2004 495 511
    • (2004) J. Mol. Biol. , vol.344 , pp. 495-511
    • Kusunoki, H.1    Minasov, G.2    MacDonald, R.I.3    Mondragon, A.4
  • 20
    • 0033588277 scopus 로고    scopus 로고
    • Structure of the alpha-actinin rod: Molecular basis for cross-linking of actin filaments
    • K. Djinovic-Carugo, P. Young, M. Gautel, and M. Saraste Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments Cell 98 1999 537 546
    • (1999) Cell , vol.98 , pp. 537-546
    • Djinovic-Carugo, K.1    Young, P.2    Gautel, M.3    Saraste, M.4
  • 21
    • 0034933167 scopus 로고    scopus 로고
    • Crystal structure of the alpha-actinin rod reveals an extensive torsional twist
    • J. Ylanne, K. Scheffzek, P. Young, and M. Saraste Crystal structure of the alpha-actinin rod reveals an extensive torsional twist Structure 9 2001 597 604
    • (2001) Structure , vol.9 , pp. 597-604
    • Ylanne, J.1    Scheffzek, K.2    Young, P.3    Saraste, M.4
  • 22
    • 1242319561 scopus 로고    scopus 로고
    • Stabilities of folding of clustered, two-repeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer
    • R.I. Macdonald, and J.A. Cummings Stabilities of folding of clustered, two-repeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer Proc. Natl Acad. Sci. USA 101 2004 1502 1507
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 1502-1507
    • MacDonald, R.I.1    Cummings, J.A.2
  • 24
    • 0242353807 scopus 로고    scopus 로고
    • Pathway shifts and thermal softening in temperature-coupled forced unfolding of spectrin domains
    • R. Law, G. Liao, S. Harper, G. Yang, D.W. Speicher, and D.E. Discher Pathway shifts and thermal softening in temperature-coupled forced unfolding of spectrin domains Biophys. J. 85 2003 3286 3293
    • (2003) Biophys. J. , vol.85 , pp. 3286-3293
    • Law, R.1    Liao, G.2    Harper, S.3    Yang, G.4    Speicher, D.W.5    Discher, D.E.6
  • 25
    • 7044226061 scopus 로고    scopus 로고
    • The folding of spectrin domains I: Wild-type domains have the same stability but very different kinetic properties
    • K.A. Scott, S. Batey, K.A. Hooton, and J. Clarke The folding of spectrin domains I: wild-type domains have the same stability but very different kinetic properties J. Mol. Biol. 344 2004 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
  • 26
    • 7044222120 scopus 로고    scopus 로고
    • The folding of spectrin domains II: Phi-value analysis of R16
    • K.A. Scott, L.G. Randles, and J. Clarke The folding of spectrin domains II: phi-value analysis of R16 J. Mol. Biol. 344 2004 207 221
    • (2004) J. Mol. Biol. , vol.344 , pp. 207-221
    • Scott, K.A.1    Randles, L.G.2    Clarke, J.3
  • 27
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • J.K. Myers, N. Pace, and J.M. Scholtz Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding Protein Sci. 4 1995 2138 2148
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, N.2    Scholtz, J.M.3
  • 29
    • 0030009318 scopus 로고    scopus 로고
    • The elastic I-band region of titin is assembled in a "modular" fashion by weakly interacting Ig-like domains
    • A.S. Politou, M. Gautel, S. Improta, L. Vangelista, and A. Pastore The elastic I-band region of titin is assembled in a "modular" fashion by weakly interacting Ig-like domains J. Mol. Biol. 255 1996 604 616
    • (1996) J. Mol. Biol. , vol.255 , pp. 604-616
    • Politou, A.S.1    Gautel, M.2    Improta, S.3    Vangelista, L.4    Pastore, A.5
  • 30
    • 0030623398 scopus 로고    scopus 로고
    • An inverse correlation between loop length and stability in a four-helix-bundle protein
    • A.D. Nagi, and L. Regan An inverse correlation between loop length and stability in a four-helix-bundle protein Fold. Des. 2 1997 67 75
    • (1997) Fold. Des. , vol.2 , pp. 67-75
    • Nagi, A.D.1    Regan, L.2
  • 31
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • C.N. Pace Determination and analysis of urea and guanidine hydrochloride denaturation curves Methods Enzymol. 131 1986 266 280
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 32
    • 0028011014 scopus 로고
    • Invariant tryptophan at a shielded site promotes folding of the conformational unit of spectrin
    • R.I. Macdonald, A. Musacchio, R.A. Holmgren, and M. Saraste Invariant tryptophan at a shielded site promotes folding of the conformational unit of spectrin Proc. Natl Acad. Sci. USA 91 1994 1299 1303
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 1299-1303
    • MacDonald, R.I.1    Musacchio, A.2    Holmgren, R.A.3    Saraste, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.