메뉴 건너뛰기




Volumn 28, Issue 8, 2010, Pages 755-765

Molecular basis of the structural stability of a Top7-based scaffold at extreme pH and temperature conditions

Author keywords

Affinity reagents; CD4 binding protein; Chemical and thermal denaturation; Experimental interpretation; Protein engineering; Temperature and pH dependent conformations; Thermostable proteins

Indexed keywords

AFFINITY REAGENTS; BINDING PROTEINS; CD4 BINDING PROTEIN; PH-DEPENDENT; PROTEIN ENGINEERING; THERMAL DENATURATIONS; THERMOSTABLE PROTEINS;

EID: 77952102931     PISSN: 10933263     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmgm.2010.01.013     Document Type: Article
Times cited : (12)

References (90)
  • 1
    • 33646943202 scopus 로고    scopus 로고
    • Molecular dynamics: survey of methods for simulating the activity of proteins
    • Adcock S.A., and McCammon J.A. Molecular dynamics: survey of methods for simulating the activity of proteins. Chem. Rev. 106 (2006) 1589-1615
    • (2006) Chem. Rev. , vol.106 , pp. 1589-1615
    • Adcock, S.A.1    McCammon, J.A.2
  • 3
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx F., and Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 22 (2004) 1399-1408
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 4
    • 4544386044 scopus 로고    scopus 로고
    • Carbopeptoid folding: effects of stereochemistry, chain length, and solvent
    • Baron R., Bakowies D., and van Gunsteren W.F. Carbopeptoid folding: effects of stereochemistry, chain length, and solvent. Angew. Chem. Int. Ed. 43 (2004) 4055-4059
    • (2004) Angew. Chem. Int. Ed. , vol.43 , pp. 4055-4059
    • Baron, R.1    Bakowies, D.2    van Gunsteren, W.F.3
  • 5
    • 34548667196 scopus 로고    scopus 로고
    • Dynamics, hydration, and motional averaging of a loop-gated artificial protein cavity: the w191g mutant of cytochrome c peroxidase in water as revealed by molecular dynamics simulations
    • Baron R., and McCammon J.A. Dynamics, hydration, and motional averaging of a loop-gated artificial protein cavity: the w191g mutant of cytochrome c peroxidase in water as revealed by molecular dynamics simulations. Biochemistry 46 (2007) 10629-10642
    • (2007) Biochemistry , vol.46 , pp. 10629-10642
    • Baron, R.1    McCammon, J.A.2
  • 6
    • 58149149594 scopus 로고    scopus 로고
    • E9-im9 colicin dnase-immunity protein biomolecular association in water: a multiple-copy and accelerated molecular dynamics simulation study
    • Baron R., Wong S.E., de Oliveira C.A., and McCammon J.A. E9-im9 colicin dnase-immunity protein biomolecular association in water: a multiple-copy and accelerated molecular dynamics simulation study. J. Phys. Chem. B 112 (2008) 16802-16814
    • (2008) J. Phys. Chem. B , vol.112 , pp. 16802-16814
    • Baron, R.1    Wong, S.E.2    de Oliveira, C.A.3    McCammon, J.A.4
  • 8
    • 27144511241 scopus 로고    scopus 로고
    • Engineering novel binding proteins from non-immunoglobulin domains
    • Binz H.K., Amstutz P., and Plueckthun A. Engineering novel binding proteins from non-immunoglobulin domains. Nat. Biotechnol. 23 (2005) 1257-1268
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1257-1268
    • Binz, H.K.1    Amstutz, P.2    Plueckthun, A.3
  • 9
    • 23644452792 scopus 로고    scopus 로고
    • Engineered proteins as specific binding reagents
    • Binz H.K., and Plueckthun A. Engineered proteins as specific binding reagents. Curr. Opin. Biotechnol. 16 (2005) 459-469
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 459-469
    • Binz, H.K.1    Plueckthun, A.2
  • 15
    • 0037195912 scopus 로고    scopus 로고
    • Dual effects of an extra disulfide bond on the activity and stability of a cold-adapted alpha-amylase
    • D'Amico S., Gerday C., and Feller G. Dual effects of an extra disulfide bond on the activity and stability of a cold-adapted alpha-amylase. J. Biol. Chem. 277 (2002) 46110-46115
    • (2002) J. Biol. Chem. , vol.277 , pp. 46110-46115
    • D'Amico, S.1    Gerday, C.2    Feller, G.3
  • 16
    • 0035854688 scopus 로고    scopus 로고
    • Structural determinants of cold adaptation and stability in a large protein
    • D'Amico S., Gerday C., and Feller G. Structural determinants of cold adaptation and stability in a large protein. J. Biol. Chem. 276 (2001) 25791-25796
    • (2001) J. Biol. Chem. , vol.276 , pp. 25791-25796
    • D'Amico, S.1    Gerday, C.2    Feller, G.3
  • 17
    • 0041384407 scopus 로고    scopus 로고
    • Temperature adaptation of proteins: engineering mesophilic-like activity and stability in a cold-adapted alpha-amylase
    • D'Amico S., Gerday C., and Feller G. Temperature adaptation of proteins: engineering mesophilic-like activity and stability in a cold-adapted alpha-amylase. J. Mol. Biol. 332 (2003) 981-988
    • (2003) J. Mol. Biol. , vol.332 , pp. 981-988
    • D'Amico, S.1    Gerday, C.2    Feller, G.3
  • 18
    • 0037424370 scopus 로고    scopus 로고
    • Activity-stability relationships in extremophilic enzymes
    • D'Amico S., Marx J.C., Gerday C., and Feller G. Activity-stability relationships in extremophilic enzymes. J. Biol. Chem. 278 (2003) 7891-7896
    • (2003) J. Biol. Chem. , vol.278 , pp. 7891-7896
    • D'Amico, S.1    Marx, J.C.2    Gerday, C.3    Feller, G.4
  • 21
    • 18744382161 scopus 로고    scopus 로고
    • Comparative study of generalized born models: protein dynamics
    • Fan H., Mark A.E., Zhu J., and Honig B. Comparative study of generalized born models: protein dynamics. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 6760-6764
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 6760-6764
    • Fan, H.1    Mark, A.E.2    Zhu, J.3    Honig, B.4
  • 22
    • 0032524655 scopus 로고    scopus 로고
    • Characterization of the c-terminal propeptide involved in bacterial wall spanning of alpha-amylase from the psychrophile alteromonas haloplanctis
    • Feller G., D'Amico S., Benotmane A.M., Joly F., Van Beeumen J., and Gerday C. Characterization of the c-terminal propeptide involved in bacterial wall spanning of alpha-amylase from the psychrophile alteromonas haloplanctis. J. Biol. Chem. 273 (1998) 12109-12115
    • (1998) J. Biol. Chem. , vol.273 , pp. 12109-12115
    • Feller, G.1    D'Amico, S.2    Benotmane, A.M.3    Joly, F.4    Van Beeumen, J.5    Gerday, C.6
  • 23
    • 33644536727 scopus 로고    scopus 로고
    • Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway
    • Fisher A.C., Kim W., and DeLisa M.P. Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway. Protein Sci. 15 (2006) 449-458
    • (2006) Protein Sci. , vol.15 , pp. 449-458
    • Fisher, A.C.1    Kim, W.2    DeLisa, M.P.3
  • 24
    • 0030037332 scopus 로고    scopus 로고
    • The application of different solvation and electrostatic models in molecular dynamics simulations of ubiquitin: how well is the X-ray structure "maintained"?
    • Fox T., and Kollman P.A. The application of different solvation and electrostatic models in molecular dynamics simulations of ubiquitin: how well is the X-ray structure "maintained"?. Proteins: Struct. Funct. Bioinformatics 25 (1996) 315-334
    • (1996) Proteins: Struct. Funct. Bioinformatics , vol.25 , pp. 315-334
    • Fox, T.1    Kollman, P.A.2
  • 26
    • 67649872364 scopus 로고    scopus 로고
    • Engineered protein scaffolds as next-generation antibody therapeutics
    • Gebauer M., and Skerra A. Engineered protein scaffolds as next-generation antibody therapeutics. Curr. Opin. Chem. Biol. 13 (2009) 245-255
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 245-255
    • Gebauer, M.1    Skerra, A.2
  • 27
    • 0029989229 scopus 로고    scopus 로고
    • Expression of correctly folded proteins in Escherichia coli
    • Georgiou G., and Valax P. Expression of correctly folded proteins in Escherichia coli. Curr. Opin. Biotechnol. 7 (1996) 190-197
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 190-197
    • Georgiou, G.1    Valax, P.2
  • 30
    • 33646740974 scopus 로고    scopus 로고
    • Antagonists to human and mouse vascular endothelial growth factor receptor 2 generated by directed protein evolution in vitro
    • Getmanova E.V., Chen Y., Bloom L., Gokemeijer J., Shamah S., Warikoo V., Wang J., Ling V., and Sun L. Antagonists to human and mouse vascular endothelial growth factor receptor 2 generated by directed protein evolution in vitro. Chem. Biol. 13 (2006) 549-556
    • (2006) Chem. Biol. , vol.13 , pp. 549-556
    • Getmanova, E.V.1    Chen, Y.2    Bloom, L.3    Gokemeijer, J.4    Shamah, S.5    Warikoo, V.6    Wang, J.7    Ling, V.8    Sun, L.9
  • 32
    • 0038692924 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the unfolding of the human prion protein domain under low ph and high temperature conditions
    • Gu W., Wang T.T., Zhu J., Shi Y.Y., and Liu H.Y. Molecular dynamics simulation of the unfolding of the human prion protein domain under low ph and high temperature conditions. Biophys. Chem. 104 (2003) 79-94
    • (2003) Biophys. Chem. , vol.104 , pp. 79-94
    • Gu, W.1    Wang, T.T.2    Zhu, J.3    Shi, Y.Y.4    Liu, H.Y.5
  • 33
    • 0000432120 scopus 로고
    • The potential calculation and some applications
    • Alder B., Fernbach S., and Rotenberg M. (Eds), Academic Press, New York/London
    • Hockney R.W. The potential calculation and some applications. In: Alder B., Fernbach S., and Rotenberg M. (Eds). Methods in Computational Physics (1970), Academic Press, New York/London 135-211
    • (1970) Methods in Computational Physics , pp. 135-211
    • Hockney, R.W.1
  • 34
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm L., and Sander C. Mapping the protein universe. Science 273 (1996) 595-602
    • (1996) Science , vol.273 , pp. 595-602
    • Holm, L.1    Sander, C.2
  • 35
    • 29344448254 scopus 로고    scopus 로고
    • A new generation of protein display scaffolds for molecular recognition
    • Hosse R.J., Rothe A., and Power B.E. A new generation of protein display scaffolds for molecular recognition. Protein Sci. 15 (2006) 14-27
    • (2006) Protein Sci. , vol.15 , pp. 14-27
    • Hosse, R.J.1    Rothe, A.2    Power, B.E.3
  • 36
    • 42449111198 scopus 로고    scopus 로고
    • Stabilization of a beta-hairpin in monomeric alzheimer's amyloid-beta peptide inhibits amyloid formation
    • Hoyer W., Gronwall C., Jonsson A., Stahl S., and Hard T. Stabilization of a beta-hairpin in monomeric alzheimer's amyloid-beta peptide inhibits amyloid formation. Proc. Natl. Acad. Sci. U.S.A. 105 (2008) 5099-5104
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 5099-5104
    • Hoyer, W.1    Gronwall, C.2    Jonsson, A.3    Stahl, S.4    Hard, T.5
  • 39
    • 44949233215 scopus 로고    scopus 로고
    • How to lose a kink and gain a helix: Ph independent conformational changes of the fusion domains from influenza hemagglutinin in heterogeneous lipid bilayers
    • Jang H., Michaud-Agrawal N., Johnston J.M., and Woolf T.B. How to lose a kink and gain a helix: Ph independent conformational changes of the fusion domains from influenza hemagglutinin in heterogeneous lipid bilayers. Proteins: Struct. Funct. Bioinformatics 72 (2008) 299-312
    • (2008) Proteins: Struct. Funct. Bioinformatics , vol.72 , pp. 299-312
    • Jang, H.1    Michaud-Agrawal, N.2    Johnston, J.M.3    Woolf, T.B.4
  • 40
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure-pattern-recognition of hydrogen-bonded and geometrical features
    • Kabsch W., and Sander C. Dictionary of protein secondary structure-pattern-recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983) 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 41
    • 70349240216 scopus 로고    scopus 로고
    • Adaptive evolution of p53 thermodynamic stability
    • Khoo K.H., Andreeva A., and Fersht A.R. Adaptive evolution of p53 thermodynamic stability. J. Mol. Biol. 393 (2009) 161-175
    • (2009) J. Mol. Biol. , vol.393 , pp. 161-175
    • Khoo, K.H.1    Andreeva, A.2    Fersht, A.R.3
  • 42
    • 0035813165 scopus 로고    scopus 로고
    • High thermostability and lack of cooperative DNA binding distinguish the p63 core domain from the homologous tumor suppressor p53
    • Klein C., Georges G., Kunkele K.P., Huber R., Engh R.A., and Hansen S. High thermostability and lack of cooperative DNA binding distinguish the p63 core domain from the homologous tumor suppressor p53. J. Biol. Chem. 276 (2001) 37390-37401
    • (2001) J. Biol. Chem. , vol.276 , pp. 37390-37401
    • Klein, C.1    Georges, G.2    Kunkele, K.P.3    Huber, R.4    Engh, R.A.5    Hansen, S.6
  • 44
    • 34547457742 scopus 로고    scopus 로고
    • Antibody mimics based on the scaffold of the fibronectin type iii domain
    • Koide A., Koide S., and Monobodies:. Antibody mimics based on the scaffold of the fibronectin type iii domain. Methods Mol. Biol. 352 (2007) 95-109
    • (2007) Methods Mol. Biol. , vol.352 , pp. 95-109
    • Koide, A.1    Koide, S.2
  • 45
    • 34249780547 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the native and partially folded states of ubiquitin: influence of methanol cosolvent, ph, and temperature on the protein structure and dynamics
    • Kony D.B., Hunenberger P.H., and van Gunsteren W.F. Molecular dynamics simulations of the native and partially folded states of ubiquitin: influence of methanol cosolvent, ph, and temperature on the protein structure and dynamics. Protein Sci. 16 (2007) 1101-1118
    • (2007) Protein Sci. , vol.16 , pp. 1101-1118
    • Kony, D.B.1    Hunenberger, P.H.2    van Gunsteren, W.F.3
  • 46
    • 0032584722 scopus 로고    scopus 로고
    • Protein folding stability can determine the efficiency of escape from endoplasmic reticulum quality control
    • Kowalski J.M., Parekh R.N., Mao J., and Wittrup K.D. Protein folding stability can determine the efficiency of escape from endoplasmic reticulum quality control. J. Biol. Chem. 273 (1998) 19453-19458
    • (1998) J. Biol. Chem. , vol.273 , pp. 19453-19458
    • Kowalski, J.M.1    Parekh, R.N.2    Mao, J.3    Wittrup, K.D.4
  • 47
    • 1342324030 scopus 로고    scopus 로고
    • Exploring folding free energy landscapes using computational protein design
    • Kuhlman B., and Baker D. Exploring folding free energy landscapes using computational protein design. Curr. Opin. Struct. Biol. 14 (2004) 89-95
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 89-95
    • Kuhlman, B.1    Baker, D.2
  • 49
    • 0030472210 scopus 로고    scopus 로고
    • Relationship between thermal stability, degradation rate and expression yield of barnase variants in the periplasm of Escherichia coli
    • Kwon W.S., Da Silva N.A., and Kellis J.T. Relationship between thermal stability, degradation rate and expression yield of barnase variants in the periplasm of Escherichia coli. Protein Eng. Des. Sel. 9 (1996) 1197-1202
    • (1996) Protein Eng. Des. Sel. , vol.9 , pp. 1197-1202
    • Kwon, W.S.1    Da Silva, N.A.2    Kellis, J.T.3
  • 50
    • 0037235978 scopus 로고    scopus 로고
    • The molecular basis of the temperature- and ph-induced conformational transitions in elastin-based peptides
    • Li B., and Daggett V. The molecular basis of the temperature- and ph-induced conformational transitions in elastin-based peptides. Biopolymers 68 (2003) 121-129
    • (2003) Biopolymers , vol.68 , pp. 121-129
    • Li, B.1    Daggett, V.2
  • 51
    • 28644432877 scopus 로고    scopus 로고
    • Very fast empirical prediction and interpretation of protein pKa values
    • Li H., Robertson A.D., and Jensen J.H. Very fast empirical prediction and interpretation of protein pKa values. Proteins: Struct. Funct. Bioinf. (2005) 704-721
    • (2005) Proteins: Struct. Funct. Bioinf. , pp. 704-721
    • Li, H.1    Robertson, A.D.2    Jensen, J.H.3
  • 52
    • 48649094750 scopus 로고    scopus 로고
    • Fully human antibodies from transgenic mouse and phage display platforms
    • Lonberg N. Fully human antibodies from transgenic mouse and phage display platforms. Curr. Opin. Immunol. 20 (2008) 450-459
    • (2008) Curr. Opin. Immunol. , vol.20 , pp. 450-459
    • Lonberg, N.1
  • 53
    • 55549108089 scopus 로고    scopus 로고
    • Engineered enzymes for chemical production
    • Luetz S., Giver L., and Lalonde J. Engineered enzymes for chemical production. Biotechnol. Bioeng. 101 (2008) 647-653
    • (2008) Biotechnol. Bioeng. , vol.101 , pp. 647-653
    • Luetz, S.1    Giver, L.2    Lalonde, J.3
  • 54
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides S.C. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 60 (1996) 512-538
    • (1996) Microbiol. Rev. , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 56
    • 34547687667 scopus 로고    scopus 로고
    • Correlation of levels of folded recombinant p53 in Escherichia coli with thermodynamic stability in vitro
    • Mayer S., Rudiger S., Ang H.C., Joerger A.C., and Fersht A.R. Correlation of levels of folded recombinant p53 in Escherichia coli with thermodynamic stability in vitro. J. Mol. Biol. 372 (2007) 268-276
    • (2007) J. Mol. Biol. , vol.372 , pp. 268-276
    • Mayer, S.1    Rudiger, S.2    Ang, H.C.3    Joerger, A.C.4    Fersht, A.R.5
  • 57
    • 54849406976 scopus 로고    scopus 로고
    • Display scaffolds: protein engineering for novel therapeutics
    • Nuttall S.D., and Walsh R.B. Display scaffolds: protein engineering for novel therapeutics. Curr. Opin. Pharmacol. 8 (2008) 609-615
    • (2008) Curr. Opin. Pharmacol. , vol.8 , pp. 609-615
    • Nuttall, S.D.1    Walsh, R.B.2
  • 58
    • 3142677981 scopus 로고    scopus 로고
    • Binding proteins from alternative scaffolds
    • Nygren P.A., and Skerra A. Binding proteins from alternative scaffolds. J. Immunol. Methods 290 (2004) 3-28
    • (2004) J. Immunol. Methods , vol.290 , pp. 3-28
    • Nygren, P.A.1    Skerra, A.2
  • 60
    • 0024363466 scopus 로고
    • Amino acid substitutions that increase the thermal stability of the lambda cro protein
    • Pakula A.A., and Sauer R.T. Amino acid substitutions that increase the thermal stability of the lambda cro protein. Proteins: Struct. Funct. Bioinf. 5 (1989) 202-210
    • (1989) Proteins: Struct. Funct. Bioinf. , vol.5 , pp. 202-210
    • Pakula, A.A.1    Sauer, R.T.2
  • 61
    • 29344458564 scopus 로고    scopus 로고
    • Simulation of ph-dependent edge strand rearrangement in human beta-2 microglobulin
    • Park S., and Saven J.G. Simulation of ph-dependent edge strand rearrangement in human beta-2 microglobulin. Protein Sci. 15 (2006) 200-207
    • (2006) Protein Sci. , vol.15 , pp. 200-207
    • Park, S.1    Saven, J.G.2
  • 62
    • 70349970427 scopus 로고    scopus 로고
    • Dynamic properties of a psychrophilic alpha-amylase in comparison with a mesophilic homologue
    • Pasi M., Riccardi L., Fantucci P., De Gioia L., and Papaleo E. Dynamic properties of a psychrophilic alpha-amylase in comparison with a mesophilic homologue. J. Phys. Chem. B 113 (2009) 13585-13595
    • (2009) J. Phys. Chem. B , vol.113 , pp. 13585-13595
    • Pasi, M.1    Riccardi, L.2    Fantucci, P.3    De Gioia, L.4    Papaleo, E.5
  • 63
    • 40549119464 scopus 로고    scopus 로고
    • The p73 DNA binding domain displays enhanced stability relative to its homologue, the tumor suppressor p53, and exhibits cooperative DNA binding
    • Patel S., Bui T.T.T., Drake A.F., Fraternali F., and Nikolova P.V. The p73 DNA binding domain displays enhanced stability relative to its homologue, the tumor suppressor p53, and exhibits cooperative DNA binding. Biochemistry 47 (2008) 3235-3244
    • (2008) Biochemistry , vol.47 , pp. 3235-3244
    • Patel, S.1    Bui, T.T.T.2    Drake, A.F.3    Fraternali, F.4    Nikolova, P.V.5
  • 64
    • 34247876138 scopus 로고    scopus 로고
    • Outlook-development trends for monoclonal antibody cancer therapeutics
    • Reichert J.M., and Valge-Archer V.E. Outlook-development trends for monoclonal antibody cancer therapeutics. Nat. Rev. Drug Discov. 6 (2007) 349-356
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 349-356
    • Reichert, J.M.1    Valge-Archer, V.E.2
  • 65
    • 33749328523 scopus 로고    scopus 로고
    • In vitro display technologies reveal novel biopharmaceutics
    • Rothe A., Hosse R.J., and Power B.E. In vitro display technologies reveal novel biopharmaceutics. FASEB J. 20 (2006) 1599-1610
    • (2006) FASEB J. , vol.20 , pp. 1599-1610
    • Rothe, A.1    Hosse, R.J.2    Power, B.E.3
  • 66
    • 33646940952 scopus 로고
    • Numerical-integration of cartesian equations of motion of a system with constraints-molecular-dynamics of n-alkanes
    • Ryckaert J.P., Ciccotti G., and Berendsen H.J.C. Numerical-integration of cartesian equations of motion of a system with constraints-molecular-dynamics of n-alkanes. J. Comp. Phys. 23 (1977) 327-341
    • (1977) J. Comp. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 67
    • 1842635571 scopus 로고    scopus 로고
    • Characterization of the folding energy landscapes of computer generated proteins suggests high folding free energy barriers and cooperativity may be consequences of natural selection
    • Scalley-Kim M., and Baker D. Characterization of the folding energy landscapes of computer generated proteins suggests high folding free energy barriers and cooperativity may be consequences of natural selection. J. Mol. Biol. 338 (2004) 573-583
    • (2004) J. Mol. Biol. , vol.338 , pp. 573-583
    • Scalley-Kim, M.1    Baker, D.2
  • 68
    • 34547151186 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy reveals a mechanically stable protein fold and the rational tuning of its mechanical stability
    • Sharma D., Perisic O., Peng Q., Cao Y., Lam C., Lu H., and Li H. Single-molecule force spectroscopy reveals a mechanically stable protein fold and the rational tuning of its mechanical stability. Proc. Natl. Acad. Sci. U.S.A. 104 (2007) 9278-9283
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 9278-9283
    • Sharma, D.1    Perisic, O.2    Peng, Q.3    Cao, Y.4    Lam, C.5    Lu, H.6    Li, H.7
  • 69
    • 34147174947 scopus 로고    scopus 로고
    • Pharma consolidates its grip on post-antibody landscape
    • Sheridan C. Pharma consolidates its grip on post-antibody landscape. Nat. Biotechnol. 25 (2007) 365-366
    • (2007) Nat. Biotechnol. , vol.25 , pp. 365-366
    • Sheridan, C.1
  • 70
    • 24344486447 scopus 로고    scopus 로고
    • The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted alpha-amylase
    • Siddiqui K.S., Feller G., D'Amico S., Gerday C., Giaquinto L., and Cavicchioli R. The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted alpha-amylase. J. Bacteriol. 187 (2005) 6197-6205
    • (2005) J. Bacteriol. , vol.187 , pp. 6197-6205
    • Siddiqui, K.S.1    Feller, G.2    D'Amico, S.3    Gerday, C.4    Giaquinto, L.5    Cavicchioli, R.6
  • 72
    • 32344436215 scopus 로고    scopus 로고
    • Multivalent avimer proteins evolved by exon shuffling of a family of human receptor domains (vol 23, pg 1556, 2005)
    • Silverman J., Lu Q., Bakker A., To W., Duguay A., Alba B.M., Smith R., Rivas A., Li P., Le H., et al. Multivalent avimer proteins evolved by exon shuffling of a family of human receptor domains (vol 23, pg 1556, 2005). Nat. Biotechnol. 24 (2006) 220-1220
    • (2006) Nat. Biotechnol. , vol.24 , pp. 220-1220
    • Silverman, J.1    Lu, Q.2    Bakker, A.3    To, W.4    Duguay, A.5    Alba, B.M.6    Smith, R.7    Rivas, A.8    Li, P.9    Le, H.10
  • 73
    • 0033865190 scopus 로고    scopus 로고
    • Engineered protein scaffolds for molecular recognition
    • Skerra A. Engineered protein scaffolds for molecular recognition. J. Mol. Recogn. 13 (2000) 167-187
    • (2000) J. Mol. Recogn. , vol.13 , pp. 167-187
    • Skerra, A.1
  • 74
    • 0344033650 scopus 로고    scopus 로고
    • Imitating the humoral immune response
    • Skerra A. Imitating the humoral immune response. Curr. Opin. Chem. Biol. 7 (2003) 683-693
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 683-693
    • Skerra, A.1
  • 75
    • 3843129852 scopus 로고    scopus 로고
    • Alpha- and beta-polypeptides show a different stability of helical secondary structure
    • Soares T., Christen M., Hu K.F., and van Gunsteren W.F. Alpha- and beta-polypeptides show a different stability of helical secondary structure. Tetrahedron 60 (2004) 7775-7780
    • (2004) Tetrahedron , vol.60 , pp. 7775-7780
    • Soares, T.1    Christen, M.2    Hu, K.F.3    van Gunsteren, W.F.4
  • 76
    • 34248147938 scopus 로고    scopus 로고
    • Comparative md analysis of the stability of transthyretin providing insight into the fibrillation mechanism
    • Sorensen J., Hamelberg D., Schiott B., and McCammon J.A. Comparative md analysis of the stability of transthyretin providing insight into the fibrillation mechanism. Biopolymers 86 (2007) 73-82
    • (2007) Biopolymers , vol.86 , pp. 73-82
    • Sorensen, J.1    Hamelberg, D.2    Schiott, B.3    McCammon, J.A.4
  • 79
    • 27344443434 scopus 로고    scopus 로고
    • Ph-dependent conformational flexibility of the sars-cov main proteinase (m-pro) dimer: molecular dynamics simulations and multiple X-ray structure analyses
    • Tan J.Z., Verschueren K.H.G., Anand K., Shen J.H., Yang M.J., Xu Y.C., Rao Z.H., Bigalke J., Heisen B., Mesters J.R., et al. Ph-dependent conformational flexibility of the sars-cov main proteinase (m-pro) dimer: molecular dynamics simulations and multiple X-ray structure analyses. J. Mol. Biol. 354 (2005) 25-40
    • (2005) J. Mol. Biol. , vol.354 , pp. 25-40
    • Tan, J.Z.1    Verschueren, K.H.G.2    Anand, K.3    Shen, J.H.4    Yang, M.J.5    Xu, Y.C.6    Rao, Z.H.7    Bigalke, J.8    Heisen, B.9    Mesters, J.R.10
  • 83
    • 0023380976 scopus 로고
    • Thermodynamic cycle integration by computer simulation as a tool for obtaining free energy differences in molecular chemistry
    • van Gunsteren W.F., and Berendsen H.J. Thermodynamic cycle integration by computer simulation as a tool for obtaining free energy differences in molecular chemistry. J. Comput. Aided Mol. Des. 1 (1987) 171-176
    • (1987) J. Comput. Aided Mol. Des. , vol.1 , pp. 171-176
    • van Gunsteren, W.F.1    Berendsen, H.J.2
  • 85
    • 0030627407 scopus 로고    scopus 로고
    • Recovery of protein structure from contact maps
    • Vendruscolo M., Kussell E., and Domany E. Recovery of protein structure from contact maps. Fold. Des. 2 (1997) 295-306
    • (1997) Fold. Des. , vol.2 , pp. 295-306
    • Vendruscolo, M.1    Kussell, E.2    Domany, E.3
  • 86
    • 33846708445 scopus 로고    scopus 로고
    • The highly cooperative folding of small naturally occurring proteins is likely the result of natural selection
    • Watters A.L., Deka P., Corrent C., Callender D., Varani G., Sosnick T., and Baker D. The highly cooperative folding of small naturally occurring proteins is likely the result of natural selection. Cell (2007) 128
    • (2007) Cell , pp. 128
    • Watters, A.L.1    Deka, P.2    Corrent, C.3    Callender, D.4    Varani, G.5    Sosnick, T.6    Baker, D.7
  • 88
    • 0037188507 scopus 로고    scopus 로고
    • Evaluating conformational free energies: the colony energy and its application to the problem of loop prediction
    • Xiang Z., Soto C.S., and Honig B. Evaluating conformational free energies: the colony energy and its application to the problem of loop prediction. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 7432-7437
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 7432-7437
    • Xiang, Z.1    Soto, C.S.2    Honig, B.3
  • 89
    • 3042616027 scopus 로고    scopus 로고
    • Effect of methylation on the stability and solvation free energy of amylose and cellulose fragments: a molecular dynamics study
    • Yu H.B., Amann M., Hansson T., Kohler J., Wich G., and van Gunsteren W.F. Effect of methylation on the stability and solvation free energy of amylose and cellulose fragments: a molecular dynamics study. Carbohydr. Res. 339 (2004) 1697-1709
    • (2004) Carbohydr. Res. , vol.339 , pp. 1697-1709
    • Yu, H.B.1    Amann, M.2    Hansson, T.3    Kohler, J.4    Wich, G.5    van Gunsteren, W.F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.