메뉴 건너뛰기




Volumn 80, Issue 12, 2012, Pages 2780-2798

Folding of multidomain proteins: Biophysical consequences of tethering even in apparently independent folding

Author keywords

Coarse grained simulation; Conjugated protein; Energy landscape; Flexible linker; Multidomain protein

Indexed keywords

CONNECTIN; PROTEIN;

EID: 84868198303     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24161     Document Type: Article
Times cited : (40)

References (72)
  • 2
    • 58149196295 scopus 로고    scopus 로고
    • The evolutionary mechanics of domain organization in proteomes and the rise of modularity in the protein world
    • Wang M, Caetano-Anolles G. The evolutionary mechanics of domain organization in proteomes and the rise of modularity in the protein world. Structure 2009; 17: 66-78.
    • (2009) Structure , vol.17 , pp. 66-78
    • Wang, M.1    Caetano-Anolles, G.2
  • 3
    • 16244423379 scopus 로고    scopus 로고
    • Multi-domain proteins in the three kingdoms of life: orphan domains and other unassigned regions
    • Ekman D, Bjorklund AK, Frey-Skott J, Elofsson A. Multi-domain proteins in the three kingdoms of life: orphan domains and other unassigned regions. J Mol Biol 2005; 348: 231-243.
    • (2005) J Mol Biol , vol.348 , pp. 231-243
    • Ekman, D.1    Bjorklund, A.K.2    Frey-Skott, J.3    Elofsson, A.4
  • 4
    • 0035816218 scopus 로고    scopus 로고
    • Domain combinations in archaeal, eubacterial and eukaryotic proteomes
    • Apic G, Gough J, Teichmann SA. Domain combinations in archaeal, eubacterial and eukaryotic proteomes. J Mol Biol 2001; 310: 311-325.
    • (2001) J Mol Biol , vol.310 , pp. 311-325
    • Apic, G.1    Gough, J.2    Teichmann, S.A.3
  • 5
    • 67650497792 scopus 로고    scopus 로고
    • Nature of the protein universe
    • Levitt M. Nature of the protein universe. Proc Natl Acad Sci USA 2009; 106: 11079-11084.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 11079-11084
    • Levitt, M.1
  • 6
  • 7
    • 0028961335 scopus 로고
    • Scop-a structural classification of proteins database for the investigation of sequences and structures
    • Murzin A, Brenner S, Hubbard T, Chothia C. Scop-a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 1995; 247: 536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.1    Brenner, S.2    Hubbard, T.3    Chothia, C.4
  • 9
    • 77958156358 scopus 로고    scopus 로고
    • How do proteins gain new domains?
    • Marsh JA, Teichmann SA. How do proteins gain new domains? Genome Biol 2010; 11: 126.
    • (2010) Genome Biol , vol.11 , pp. 126
    • Marsh, J.A.1    Teichmann, S.A.2
  • 10
    • 0842268045 scopus 로고    scopus 로고
    • Supra-domains: evolutionary units larger than single protein domains
    • Vogel C, Berzuini C, Bashton M, Gough J, Teichmann SA. Supra-domains: evolutionary units larger than single protein domains. J Mol Biol 2004; 336: 809-823.
    • (2004) J Mol Biol , vol.336 , pp. 809-823
    • Vogel, C.1    Berzuini, C.2    Bashton, M.3    Gough, J.4    Teichmann, S.A.5
  • 11
    • 34548815693 scopus 로고    scopus 로고
    • Modular architecture of protein structures and allosteric communications: potential implications for signaling proteins and regulatory linkages
    • Del Sol A, Arauzo-Bravo MJ, Amoros D, Nussinov R. Modular architecture of protein structures and allosteric communications: potential implications for signaling proteins and regulatory linkages. Genome Biol 2007; 8: R92.
    • (2007) Genome Biol , vol.8
    • Del Sol, A.1    Arauzo-Bravo, M.J.2    Amoros, D.3    Nussinov, R.4
  • 12
    • 0036307754 scopus 로고    scopus 로고
    • The geometry of domain combination in proteins
    • Bashton M, Chothia C. The geometry of domain combination in proteins. J Mol Biol 2002; 315: 927-939.
    • (2002) J Mol Biol , vol.315 , pp. 927-939
    • Bashton, M.1    Chothia, C.2
  • 15
    • 33646000631 scopus 로고    scopus 로고
    • Complex folding kinetics of a multidomain protein
    • Batey S, Scott KA, Clarke J. Complex folding kinetics of a multidomain protein. Biophys J 2006; 90: 2120-2130.
    • (2006) Biophys J , vol.90 , pp. 2120-2130
    • Batey, S.1    Scott, K.A.2    Clarke, J.3
  • 16
    • 84856433534 scopus 로고    scopus 로고
    • Two immunoglobulin tandem proteins with a linking beta-strand reveal unexpected differences in cooperativity and folding pathways
    • Steward A, Chen Q, Chapman RI, Borgia MB, Rogers JM, Wojtala A, Wilmanns M, Clarke J. Two immunoglobulin tandem proteins with a linking beta-strand reveal unexpected differences in cooperativity and folding pathways. J Mol Biol 2012; 416: 137-147.
    • (2012) J Mol Biol , vol.416 , pp. 137-147
    • Steward, A.1    Chen, Q.2    Chapman, R.I.3    Borgia, M.B.4    Rogers, J.M.5    Wojtala, A.6    Wilmanns, M.7    Clarke, J.8
  • 17
    • 80755127361 scopus 로고    scopus 로고
    • Domain cooperativity in multidomain proteins: what can we learn from molecular alignment in anisotropic media?
    • Yuwen T, Post CB, Skrynnikov NR. Domain cooperativity in multidomain proteins: what can we learn from molecular alignment in anisotropic media? J Biomol NMR 2011; 51: 131-150.
    • (2011) J Biomol NMR , vol.51 , pp. 131-150
    • Yuwen, T.1    Post, C.B.2    Skrynnikov, N.R.3
  • 18
    • 76649091072 scopus 로고    scopus 로고
    • Studying the folding of multidomain proteins
    • Batey S, Nickson AA, Clarke J. Studying the folding of multidomain proteins. HSFP J 2008; 2: 365-377.
    • (2008) HSFP J , vol.2 , pp. 365-377
    • Batey, S.1    Nickson, A.A.2    Clarke, J.3
  • 19
    • 0036304229 scopus 로고    scopus 로고
    • Titin; a multidomain protein that behaves as the sum of its parts
    • Scott KA, Steward A, Fowler SB, Clarke J. Titin; a multidomain protein that behaves as the sum of its parts. J Mol Biol 2002; 315: 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
  • 20
    • 0033982651 scopus 로고    scopus 로고
    • Role of linkers in communication between protein modules
    • Gokhale RS, Khosla C. Role of linkers in communication between protein modules. Curr Opin Chem Biol 2000; 4: 22-27.
    • (2000) Curr Opin Chem Biol , vol.4 , pp. 22-27
    • Gokhale, R.S.1    Khosla, C.2
  • 21
    • 33144464467 scopus 로고    scopus 로고
    • Control of protein functional dynamics by peptide linkers
    • Wriggers W, Chakravarty S, Jennings PA. Control of protein functional dynamics by peptide linkers. Biopolymers 2005; 80: 736-746.
    • (2005) Biopolymers , vol.80 , pp. 736-746
    • Wriggers, W.1    Chakravarty, S.2    Jennings, P.A.3
  • 22
    • 79960189344 scopus 로고    scopus 로고
    • Dynamic allostery: linkers are not merely flexible
    • Ma B, Tsai CJ, Haliloglu T, Nussinov R. Dynamic allostery: linkers are not merely flexible. Structure 2011; 19: 907-917.
    • (2011) Structure , vol.19 , pp. 907-917
    • Ma, B.1    Tsai, C.J.2    Haliloglu, T.3    Nussinov, R.4
  • 23
    • 77952694236 scopus 로고    scopus 로고
    • Mapping the conformational mobility of multidomain proteins
    • Blackledge M. Mapping the conformational mobility of multidomain proteins. Biophys J 2010; 98: 2043-2044.
    • (2010) Biophys J , vol.98 , pp. 2043-2044
    • Blackledge, M.1
  • 24
    • 77949513778 scopus 로고    scopus 로고
    • Conformational dynamics and ligand binding in the multi-domain protein PDC109
    • Kim HJ, Choi MY, Kim HJ, Llinas M. Conformational dynamics and ligand binding in the multi-domain protein PDC109. PloS One 2010; 5: e9180.
    • (2010) PloS One , vol.5
    • Kim, H.J.1    Choi, M.Y.2    Kim, H.J.3    Llinas, M.4
  • 25
    • 34548209898 scopus 로고    scopus 로고
    • Nanoscale dewetting transition in protein complex folding
    • Hua L, Huang X, Liu P, Zhou R, Berne BJ. Nanoscale dewetting transition in protein complex folding. J Phys Chem 2007; 111: 9069-9077.
    • (2007) J Phys Chem , vol.111 , pp. 9069-9077
    • Hua, L.1    Huang, X.2    Liu, P.3    Zhou, R.4    Berne, B.J.5
  • 26
    • 63449135082 scopus 로고    scopus 로고
    • An all-atom structure-based potential for proteins: bridging minimal models with all-atom empirical forcefields
    • Whitford PC, Noel JK, Gosavi S, Schug A, Sanbonmatsu KY, Onuchic JN. An all-atom structure-based potential for proteins: bridging minimal models with all-atom empirical forcefields. Proteins 2009; 75: 430-441.
    • (2009) Proteins , vol.75 , pp. 430-441
    • Whitford, P.C.1    Noel, J.K.2    Gosavi, S.3    Schug, A.4    Sanbonmatsu, K.Y.5    Onuchic, J.N.6
  • 27
    • 36749023459 scopus 로고    scopus 로고
    • Mutations as trapdoors to two competing native conformations of the Rop-dimer
    • Schug A, Whitford PC, Levy Y, Onuchic JN. Mutations as trapdoors to two competing native conformations of the Rop-dimer. Proc Natl Acad Sci USA 2007; 104: 17674-17679.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 17674-17679
    • Schug, A.1    Whitford, P.C.2    Levy, Y.3    Onuchic, J.N.4
  • 28
    • 78149495375 scopus 로고    scopus 로고
    • From protein folding to protein function and biomolecular binding by energy landscape theory
    • Schug A, Onuchic JN. From protein folding to protein function and biomolecular binding by energy landscape theory. Curr Opin Pharmacol 2010; 10: 709-714.
    • (2010) Curr Opin Pharmacol , vol.10 , pp. 709-714
    • Schug, A.1    Onuchic, J.N.2
  • 30
    • 58849083668 scopus 로고    scopus 로고
    • Quantitative criteria for native energetic heterogeneity influences in the prediction of protein folding kinetics
    • Cho SS, Levy Y, Wolynes P. Quantitative criteria for native energetic heterogeneity influences in the prediction of protein folding kinetics. Proc Natl Acad Sci USA 2009; 106: 434-439.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 434-439
    • Cho, S.S.1    Levy, Y.2    Wolynes, P.3
  • 31
    • 76649123968 scopus 로고    scopus 로고
    • Ubiquitin not only serves as a tag but also assists degradation by inducing protein unfolding
    • Hagai T, Levy Y. Ubiquitin not only serves as a tag but also assists degradation by inducing protein unfolding. Proc Natl Acad Sci USA 2010; 107: 2001-2006.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 2001-2006
    • Hagai, T.1    Levy, Y.2
  • 33
    • 46149089907 scopus 로고    scopus 로고
    • Effect of glycosylation on protein folding: a close look at thermodynamic stabilization
    • Shental-Bechor D, Levy Y. Effect of glycosylation on protein folding: a close look at thermodynamic stabilization. Proc Natl Acad Sci USA 2008; 105: 8256-8261.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 8256-8261
    • Shental-Bechor, D.1    Levy, Y.2
  • 34
    • 70349886556 scopus 로고    scopus 로고
    • Folding of glycoproteins: toward understanding the biophysics of the glycosylation code
    • Shental-Bechor D, Levy Y. Folding of glycoproteins: toward understanding the biophysics of the glycosylation code. Curr Opin Struct Biol 2009; 19: 524-533.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 524-533
    • Shental-Bechor, D.1    Levy, Y.2
  • 35
    • 46149089973 scopus 로고    scopus 로고
    • Simulations of proteins with inhomogeneous degrees of freedom: the effect of thermostats
    • Mor A, Ziv G, Levy Y. Simulations of proteins with inhomogeneous degrees of freedom: the effect of thermostats. J Comput Chem 2008; 29: 1992-1998.
    • (2008) J Comput Chem , vol.29 , pp. 1992-1998
    • Mor, A.1    Ziv, G.2    Levy, Y.3
  • 36
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method
    • Kumar S, Rosenberg, JM, Bouzida D, Swendsen RH, Kollman PA. The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method. J Comput Chem 1992; 13: 1011-1021.
    • (1992) J Comput Chem , vol.13 , pp. 1011-1021
    • Kumar, S.1    Rosenberg, J.M.2    Bouzida, D.3    Swendsen, R.H.4    Kollman, P.A.5
  • 37
    • 31444452031 scopus 로고    scopus 로고
    • P versus Q: structural reaction coordinates capture protein folding on smooth landscapes
    • Cho SS, Levy Y, Wolynes PG. P versus Q: structural reaction coordinates capture protein folding on smooth landscapes. Proc Natl Acad Sci USA 2006; 103: 586-591.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 586-591
    • Cho, S.S.1    Levy, Y.2    Wolynes, P.G.3
  • 39
    • 0141482088 scopus 로고    scopus 로고
    • How protein thermodynamics and folding mechanisms are altered by the chaperonin cage: molecular simulations
    • Takagi F, Koga N, Takada S. How protein thermodynamics and folding mechanisms are altered by the chaperonin cage: molecular simulations. Proc Natl Acad Sci USA 2003; 100: 11367-11372.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11367-11372
    • Takagi, F.1    Koga, N.2    Takada, S.3
  • 40
    • 28644434901 scopus 로고    scopus 로고
    • Folding behavior of chaperonin-mediated substrate protein
    • Xu WX, Wang J, Wang W. Folding behavior of chaperonin-mediated substrate protein. Proteins 2005; 61: 777-794.
    • (2005) Proteins , vol.61 , pp. 777-794
    • Xu, W.X.1    Wang, J.2    Wang, W.3
  • 42
    • 20544435097 scopus 로고    scopus 로고
    • Exploring the helix-coil transition via all-atom equilibrium ensemble simulations
    • Sorin EJ, Pande VS. Exploring the helix-coil transition via all-atom equilibrium ensemble simulations. Biophys J 2005; 88: 2472-2493.
    • (2005) Biophys J , vol.88 , pp. 2472-2493
    • Sorin, E.J.1    Pande, V.S.2
  • 43
    • 0037053429 scopus 로고    scopus 로고
    • Sequence conservation in Ig-like domains: the role of highly conserved proline residues in the fibronectin type III superfamily
    • Steward A, Adhya S, Clarke J. Sequence conservation in Ig-like domains: the role of highly conserved proline residues in the fibronectin type III superfamily. J Mol Biol 2002; 318: 935-940.
    • (2002) J Mol Biol , vol.318 , pp. 935-940
    • Steward, A.1    Adhya, S.2    Clarke, J.3
  • 44
    • 0031556949 scopus 로고    scopus 로고
    • Module-module interactions in the cell binding region of fibronectin: stability, flexibility and specificity
    • Spitzfaden C, Grant R, Mardon H, Cambell I. Module-module interactions in the cell binding region of fibronectin: stability, flexibility and specificity. J Mol Biol 1997; 265: 565-579.
    • (1997) J Mol Biol , vol.265 , pp. 565-579
    • Spitzfaden, C.1    Grant, R.2    Mardon, H.3    Cambell, I.4
  • 45
    • 0033200251 scopus 로고    scopus 로고
    • Folding studies of immunoglobulin-like b-sandwich proteins suggest that they share a common folding pathway
    • Clarke J, Cota E, Fowler SB, Hamill SJ. Folding studies of immunoglobulin-like b-sandwich proteins suggest that they share a common folding pathway. Structure 1999; 7: 1145-1153.
    • (1999) Structure , vol.7 , pp. 1145-1153
    • Clarke, J.1    Cota, E.2    Fowler, S.B.3    Hamill, S.J.4
  • 46
    • 20544435808 scopus 로고    scopus 로고
    • Biophysical investigations of engineered polyproteins: implications for force data
    • Rounsevell RW, Steward A, Clarke J. Biophysical investigations of engineered polyproteins: implications for force data. Biophys J 2005; 88: 2022-2029.
    • (2005) Biophys J , vol.88 , pp. 2022-2029
    • Rounsevell, R.W.1    Steward, A.2    Clarke, J.3
  • 47
    • 36549021676 scopus 로고    scopus 로고
    • Crosstalk between the protein surface and hydrophobic core in a core-swapped fibronectin type III domain
    • Billings KS, Best RB, Rutherford TJ, Clarke J. Crosstalk between the protein surface and hydrophobic core in a core-swapped fibronectin type III domain. J Mol Biol 2008; 375: 560-571.
    • (2008) J Mol Biol , vol.375 , pp. 560-571
    • Billings, K.S.1    Best, R.B.2    Rutherford, T.J.3    Clarke, J.4
  • 48
    • 20544465799 scopus 로고    scopus 로고
    • Mechanical unfolding of TNfn3: the unfolding pathway of a fnIII domain probed by protein engineering, AFM and MD simulation
    • Ng SP, Rounsevell RW, Steward A, Geierhaas CD, Williams PM, Paci E, Clarke J. Mechanical unfolding of TNfn3: the unfolding pathway of a fnIII domain probed by protein engineering, AFM and MD simulation. J Mol Biol 2005; 350: 776-789.
    • (2005) J Mol Biol , vol.350 , pp. 776-789
    • Ng, S.P.1    Rounsevell, R.W.2    Steward, A.3    Geierhaas, C.D.4    Williams, P.M.5    Paci, E.6    Clarke, J.7
  • 49
    • 0032474435 scopus 로고    scopus 로고
    • The effect of boundary selectionon the stability and folding of the third fibronectin typeIII domain from human tenascin
    • Hamill SJ, Meekhof AE, Clarke J. The effect of boundary selectionon the stability and folding of the third fibronectin typeIII domain from human tenascin. Biochemistry 1998; 37: 8071-8079.
    • (1998) Biochemistry , vol.37 , pp. 8071-8079
    • Hamill, S.J.1    Meekhof, A.E.2    Clarke, J.3
  • 50
    • 52949100202 scopus 로고    scopus 로고
    • Cooperativity, connectivity, and folding pathways of multidomain proteins
    • Itoh K, Sasai M. Cooperativity, connectivity, and folding pathways of multidomain proteins. Proc Natl Acad Sci USA 2008; 105: 13865-13870.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 13865-13870
    • Itoh, K.1    Sasai, M.2
  • 51
    • 33846847773 scopus 로고    scopus 로고
    • The conformational transition of adenylate kinase: switching by cracking
    • Whitford P, Miyashita O, Levy Y, Onuchic JN. The conformational transition of adenylate kinase: switching by cracking. J Mol Biol 2006; 366: 1661-1671.
    • (2006) J Mol Biol , vol.366 , pp. 1661-1671
    • Whitford, P.1    Miyashita, O.2    Levy, Y.3    Onuchic, J.N.4
  • 52
    • 50049118547 scopus 로고    scopus 로고
    • Subdomain competition, cooperativity, and topological frustration in the folding of CheY
    • Hills RD, Jr, Brooks CL, 3rd. Subdomain competition, cooperativity, and topological frustration in the folding of CheY. J Mol Biol 2008; 382: 485-495.
    • (2008) J Mol Biol , vol.382 , pp. 485-495
    • Hills Jr., R.D.1    Brooks 3rd, C.L.2
  • 53
  • 54
    • 33744802398 scopus 로고    scopus 로고
    • Effects of surface tethering on protein folding mechanisms
    • Friedel M, Baumketner A, Shea JE. Effects of surface tethering on protein folding mechanisms. Proc Natl Acad Sci USA 2006; 103: 8396-8401.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8396-8401
    • Friedel, M.1    Baumketner, A.2    Shea, J.E.3
  • 55
    • 33847737459 scopus 로고    scopus 로고
    • Stability of a protein tethered to a surface
    • Friedel M, Baumketner A, Shea JE. Stability of a protein tethered to a surface. J Chem Phys 2007; 126: 095101.
    • (2007) J Chem Phys , vol.126 , pp. 095101
    • Friedel, M.1    Baumketner, A.2    Shea, J.E.3
  • 56
    • 62449169742 scopus 로고    scopus 로고
    • The effect of surface tethering on the folding of the src-SH3 protein domain
    • Zhuang Z, Jewett AI, Soto P, Shea JE. The effect of surface tethering on the folding of the src-SH3 protein domain. Phys Biol 2009; 6: 15004.
    • (2009) Phys Biol , vol.6 , pp. 15004
    • Zhuang, Z.1    Jewett, A.I.2    Soto, P.3    Shea, J.E.4
  • 57
    • 35648997078 scopus 로고    scopus 로고
    • Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin
    • Mills IA, Flaugh SL, Kosinski-Collins MS, King JA. Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin. Protein Sci 2007; 16: 2427-2444.
    • (2007) Protein Sci , vol.16 , pp. 2427-2444
    • Mills, I.A.1    Flaugh, S.L.2    Kosinski-Collins, M.S.3    King, J.A.4
  • 59
    • 1042275583 scopus 로고    scopus 로고
    • A dissection of specific and non-specific protein-protein interfaces
    • Bahadur RP, Chakrabarti P, Rodier F, Janin J. A dissection of specific and non-specific protein-protein interfaces. J Mol Biol 2004; 336: 943-955.
    • (2004) J Mol Biol , vol.336 , pp. 943-955
    • Bahadur, R.P.1    Chakrabarti, P.2    Rodier, F.3    Janin, J.4
  • 60
    • 28644437048 scopus 로고    scopus 로고
    • The importance of sequence diversity in the aggregation and evolution of proteins
    • Wright CF, Teichmann SA, Clarke J, Dobson CM. The importance of sequence diversity in the aggregation and evolution of proteins. Nature 2005; 438: 878-881.
    • (2005) Nature , vol.438 , pp. 878-881
    • Wright, C.F.1    Teichmann, S.A.2    Clarke, J.3    Dobson, C.M.4
  • 62
    • 79955565416 scopus 로고    scopus 로고
    • Minimum energy compact structures in force-quench polyubiquitin folding are domain swapped
    • Xia F, Thirumalai D, Grater F. Minimum energy compact structures in force-quench polyubiquitin folding are domain swapped. Proc Natl Acad Sci USA 2011; 108: 6963-6968.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 6963-6968
    • Xia, F.1    Thirumalai, D.2    Grater, F.3
  • 64
    • 22244447465 scopus 로고    scopus 로고
    • Overcoming residual frustration in domain-swapping: the roles of disulfide bonds in dimerization and aggregation
    • Cho SS, Levy Y, Onuchic JN, Wolynes PG. Overcoming residual frustration in domain-swapping: the roles of disulfide bonds in dimerization and aggregation. Phys Biol 2005; 2: S44-S55.
    • (2005) Phys Biol , vol.2
    • Cho, S.S.1    Levy, Y.2    Onuchic, J.N.3    Wolynes, P.G.4
  • 65
    • 49749097883 scopus 로고    scopus 로고
    • Effects of excluded volume upon protein stability in covalently cross-linked proteins with variable linker lengths
    • Kim YH, Stites WE. Effects of excluded volume upon protein stability in covalently cross-linked proteins with variable linker lengths. Biochemistry 2008; 47: 8804-8814.
    • (2008) Biochemistry , vol.47 , pp. 8804-8814
    • Kim, Y.H.1    Stites, W.E.2
  • 67
    • 0033572725 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on protein folding and aggregation
    • van den Berg B, Ellis RJ, Dobson CM. Effects of macromolecular crowding on protein folding and aggregation. EMBO J 1999; 18: 6927-6933.
    • (1999) EMBO J , vol.18 , pp. 6927-6933
    • van den Berg, B.1    Ellis, R.J.2    Dobson, C.M.3
  • 68
    • 65249154187 scopus 로고    scopus 로고
    • Confinement effects on the kinetics and thermodynamics of protein dimerization
    • Wang W, Xu WX, Levy Y, Trizac E, Wolynes PG. Confinement effects on the kinetics and thermodynamics of protein dimerization. Proc Natl Acad Sci USA 2009; 106: 5517-5522.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 5517-5522
    • Wang, W.1    Xu, W.X.2    Levy, Y.3    Trizac, E.4    Wolynes, P.G.5
  • 70
    • 0030009318 scopus 로고    scopus 로고
    • The elastic I-band region of titin is assembled in a "modular" fashion by weakly interacting Ig-like domains
    • Politou AS, Gautel M, Improta S, Vangelista L, Pastore A. The elastic I-band region of titin is assembled in a "modular" fashion by weakly interacting Ig-like domains. J Mol Biol 1996; 255: 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
  • 71
    • 79955724209 scopus 로고    scopus 로고
    • Mechanical stability of multidomain proteins and novel mechanical clamps
    • Sikora M, Cieplak M. Mechanical stability of multidomain proteins and novel mechanical clamps. Proteins 2011; 79: 1786-1799.
    • (2011) Proteins , vol.79 , pp. 1786-1799
    • Sikora, M.1    Cieplak, M.2
  • 72
    • 22444431560 scopus 로고    scopus 로고
    • Asymmetric effect of domain interactions on the kinetics of folding in yeast phosphoglycerate kinase
    • Osvath S, Kohler G, Zavodszky P, Fidy J. Asymmetric effect of domain interactions on the kinetics of folding in yeast phosphoglycerate kinase. Protein Sci 2005; 14: 1609-1616.
    • (2005) Protein Sci , vol.14 , pp. 1609-1616
    • Osvath, S.1    Kohler, G.2    Zavodszky, P.3    Fidy, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.