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Volumn 29, Issue 1, 2010, Pages 2-12

Temperature-induced unfolding of epidermal growth factor (EGF): Insight from molecular dynamics simulation

Author keywords

Free energy landscape; Human epidermal growth factor (EGF); Molten globule; Replica exchange molecular dynamics simulations; Thermal denaturation; Transition state; Unfolding kinetics

Indexed keywords

FREE-ENERGY LANDSCAPE; HUMAN EPIDERMAL GROWTH FACTOR; MOLTEN GLOBULE; REPLICA-EXCHANGE MOLECULAR DYNAMICS SIMULATIONS; THERMAL DENATURATIONS; TRANSITION STATE; UNFOLDING KINETICS;

EID: 77955842900     PISSN: 10933263     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmgm.2010.03.011     Document Type: Article
Times cited : (22)

References (65)
  • 1
    • 0029249945 scopus 로고
    • The nature of protein-folding pathways-the classical versus the new view
    • Baldwin R.L. The nature of protein-folding pathways-the classical versus the new view. J. Biomol. NMR 1995, 5:103-109.
    • (1995) J. Biomol. NMR , vol.5 , pp. 103-109
    • Baldwin, R.L.1
  • 2
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg A.L. Protein degradation and protection against misfolded or damaged proteins. Nature 2003, 426:895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 3
    • 33646257222 scopus 로고    scopus 로고
    • Selective laser photo-thermal therapy of epithelial carcinoma using anti-EGFR antibody conjugated gold nanoparticles
    • El-Sayed I.H., Huang X., El-Sayed M.A. Selective laser photo-thermal therapy of epithelial carcinoma using anti-EGFR antibody conjugated gold nanoparticles. Cancer Lett. 2005, 239:129-135.
    • (2005) Cancer Lett. , vol.239 , pp. 129-135
    • El-Sayed, I.H.1    Huang, X.2    El-Sayed, M.A.3
  • 6
    • 27744452242 scopus 로고    scopus 로고
    • Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing
    • Anil B., Sato S., Cho J.H., Raleigh D.P. Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J. Mol. Biol. 2005, 354:693-705.
    • (2005) J. Mol. Biol. , vol.354 , pp. 693-705
    • Anil, B.1    Sato, S.2    Cho, J.H.3    Raleigh, D.P.4
  • 7
    • 0032812796 scopus 로고    scopus 로고
    • Mapping the interactions present in the transition state for unfolding/folding of FKBP12
    • Fulton K.F., Main E.R.G., Daggett V., Jackson S.E. Mapping the interactions present in the transition state for unfolding/folding of FKBP12. J. Mol. Biol. 1999, 291:445-461.
    • (1999) J. Mol. Biol. , vol.291 , pp. 445-461
    • Fulton, K.F.1    Main, E.R.G.2    Daggett, V.3    Jackson, S.E.4
  • 8
    • 0037076334 scopus 로고    scopus 로고
    • Molecular dynamics simulations of protein folding from the transition state
    • Gsponer J., Caflisch A. Molecular dynamics simulations of protein folding from the transition state. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:6719-6724.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 6719-6724
    • Gsponer, J.1    Caflisch, A.2
  • 9
    • 0024358426 scopus 로고
    • Mapping the transition-state and pathways of protein folding by protein engineering
    • Matouschek A., Kellis J.T., Serrano L., Fersht A.R. Mapping the transition-state and pathways of protein folding by protein engineering. Nature 1989, 340:122-126.
    • (1989) Nature , vol.340 , pp. 122-126
    • Matouschek, A.1    Kellis, J.T.2    Serrano, L.3    Fersht, A.R.4
  • 10
    • 10644261303 scopus 로고    scopus 로고
    • Differences in the folding transition state of ubiquitin indicated by phi and psi analyses
    • Sosnick T.R., Dothager R.S., Krantz B.A. Differences in the folding transition state of ubiquitin indicated by phi and psi analyses. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:17377-17382.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 17377-17382
    • Sosnick, T.R.1    Dothager, R.S.2    Krantz, B.A.3
  • 11
    • 43849090358 scopus 로고    scopus 로고
    • Thermal unfolding simulations of bacterial flagellin: insight into its refolding before assembly
    • Chng C.P., Kitao A. Thermal unfolding simulations of bacterial flagellin: insight into its refolding before assembly. Biophys. J. 2008, 94:3858-3871.
    • (2008) Biophys. J. , vol.94 , pp. 3858-3871
    • Chng, C.P.1    Kitao, A.2
  • 12
    • 33750060447 scopus 로고    scopus 로고
    • Thermal denaturing of mutant lysozyme with both the OPLSAA and the CHARMM force fields
    • Eleftheriou M., Germain R.S., Royyuru A.K., Zhou R.H. Thermal denaturing of mutant lysozyme with both the OPLSAA and the CHARMM force fields. J. Am. Chem. Soc. 2006, 128:13388-13395.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 13388-13395
    • Eleftheriou, M.1    Germain, R.S.2    Royyuru, A.K.3    Zhou, R.H.4
  • 13
    • 49649099523 scopus 로고    scopus 로고
    • Temperature-induced unfolding pathway of a type III antifreeze protein: insight from molecular dynamics simulation
    • Kunda S., Roy D. Temperature-induced unfolding pathway of a type III antifreeze protein: insight from molecular dynamics simulation. J. Mol. Graph. Model. 2008, 27:88-94.
    • (2008) J. Mol. Graph. Model. , vol.27 , pp. 88-94
    • Kunda, S.1    Roy, D.2
  • 14
    • 27344455346 scopus 로고    scopus 로고
    • Reproducible polypeptide folding and structure prediction using molecular dynamics simulations
    • Seibert M.M., Patriksson A., Hess B., van der Spoel D. Reproducible polypeptide folding and structure prediction using molecular dynamics simulations. J. Mol. Biol. 2005, 354:173-183.
    • (2005) J. Mol. Biol. , vol.354 , pp. 173-183
    • Seibert, M.M.1    Patriksson, A.2    Hess, B.3    van der Spoel, D.4
  • 15
    • 0037174385 scopus 로고    scopus 로고
    • All-atom structure prediction and folding simulations of a stable protein
    • Simmerling C., Strockbine B., Roitberg A.E. All-atom structure prediction and folding simulations of a stable protein. J. Am. Chem. Soc. 2002, 124:11258-11259.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11258-11259
    • Simmerling, C.1    Strockbine, B.2    Roitberg, A.E.3
  • 16
    • 0037038372 scopus 로고    scopus 로고
    • Absolute comparison of simulated and experimental protein-folding dynamics
    • Snow C.D., Nguyen N., Pande V.S., Gruebele M. Absolute comparison of simulated and experimental protein-folding dynamics. Nature 2002, 420:102-106.
    • (2002) Nature , vol.420 , pp. 102-106
    • Snow, C.D.1    Nguyen, N.2    Pande, V.S.3    Gruebele, M.4
  • 17
    • 44849116304 scopus 로고    scopus 로고
    • High temperature unfolding simulations of the TRPZ1 peptide
    • Settanni G., Fersht A.R. High temperature unfolding simulations of the TRPZ1 peptide. Biophys. J. 2008, 94:4444-4453.
    • (2008) Biophys. J. , vol.94 , pp. 4444-4453
    • Settanni, G.1    Fersht, A.R.2
  • 18
    • 1942455272 scopus 로고    scopus 로고
    • Generalized-ensemble algorithms: enhanced sampling techniques for Monte Carlo and molecular dynamics simulations
    • Okamoto Y. Generalized-ensemble algorithms: enhanced sampling techniques for Monte Carlo and molecular dynamics simulations. J. Mol. Graph. Model. 2004, 22:425-439.
    • (2004) J. Mol. Graph. Model. , vol.22 , pp. 425-439
    • Okamoto, Y.1
  • 19
    • 0345133287 scopus 로고    scopus 로고
    • Folding a protein in a computer: an atomic description of the folding/unfolding of protein A
    • Garcia A.E., Onuchic J.N. Folding a protein in a computer: an atomic description of the folding/unfolding of protein A. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:13898-13903.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 13898-13903
    • Garcia, A.E.1    Onuchic, J.N.2
  • 20
    • 47249119770 scopus 로고    scopus 로고
    • Folding processes of the B domain of protein A to the native state observed in all-atom ab initio folding simulations
    • Lei H.X., Wu C., Wang Z.X., Zhou Y.Q., Duan Y. Folding processes of the B domain of protein A to the native state observed in all-atom ab initio folding simulations. J. Chem. Phys. 2008, 128:235105-235113.
    • (2008) J. Chem. Phys. , vol.128 , pp. 235105-235113
    • Lei, H.X.1    Wu, C.2    Wang, Z.X.3    Zhou, Y.Q.4    Duan, Y.5
  • 21
    • 84962393635 scopus 로고    scopus 로고
    • Molecular modeling of conformational properties of oligodepsipeptides
    • Zhang J.J., King M., Suggs L., Ren P.Y. Molecular modeling of conformational properties of oligodepsipeptides. Biomacromolecules 2007, 8:3015-3024.
    • (2007) Biomacromolecules , vol.8 , pp. 3015-3024
    • Zhang, J.J.1    King, M.2    Suggs, L.3    Ren, P.Y.4
  • 22
    • 0344824394 scopus 로고    scopus 로고
    • Trp-cage: folding free energy landscape in explicit water
    • Zhou R.H. Trp-cage: folding free energy landscape in explicit water. Natl. Acad. Sci. U.S.A. 2003, 100:13280-13285.
    • (2003) Natl. Acad. Sci. U.S.A. , vol.100 , pp. 13280-13285
    • Zhou, R.H.1
  • 23
    • 55349105436 scopus 로고    scopus 로고
    • Free energy landscapes of a highly structured beta-hairpin peptide and its single mutant
    • Kim E., Yang C.W., Jang S.M., Pak Y. Free energy landscapes of a highly structured beta-hairpin peptide and its single mutant. J. Chem. Phys. 2008, 129:165104-165110.
    • (2008) J. Chem. Phys. , vol.129 , pp. 165104-165110
    • Kim, E.1    Yang, C.W.2    Jang, S.M.3    Pak, Y.4
  • 24
    • 23944494644 scopus 로고    scopus 로고
    • Folding cooperativity in a three-stranded beta-sheet model
    • Roe D.R., Hornak V., Simmerling C. Folding cooperativity in a three-stranded beta-sheet model. J. Mol. Biol. 2005, 352:370-381.
    • (2005) J. Mol. Biol. , vol.352 , pp. 370-381
    • Roe, D.R.1    Hornak, V.2    Simmerling, C.3
  • 25
    • 33645722974 scopus 로고    scopus 로고
    • Convergence of replica exchange molecular dynamics
    • Zhang W., Wu C., Duan Y. Convergence of replica exchange molecular dynamics. J. Chem. Phys. 2005, 123:154105-154113.
    • (2005) J. Chem. Phys. , vol.123 , pp. 154105-154113
    • Zhang, W.1    Wu, C.2    Duan, Y.3
  • 26
    • 0037934616 scopus 로고    scopus 로고
    • Understanding folding and design: replica-exchange simulations of " Trp-cage" fly miniproteins
    • Pitera J.W., Swope W. Understanding folding and design: replica-exchange simulations of " Trp-cage" fly miniproteins. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:7587-7592.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 7587-7592
    • Pitera, J.W.1    Swope, W.2
  • 27
    • 45849119074 scopus 로고    scopus 로고
    • Observation of noncooperative folding thermodynamics in simulations of 1BBL
    • Pitera J.W., Swope W.C., Abraham F.F. Observation of noncooperative folding thermodynamics in simulations of 1BBL. Biophys. J. 2008, 94:4837-4846.
    • (2008) Biophys. J. , vol.94 , pp. 4837-4846
    • Pitera, J.W.1    Swope, W.C.2    Abraham, F.F.3
  • 28
    • 0030023486 scopus 로고    scopus 로고
    • The roles of partly folded intermediates in protein folding
    • Creighton T.E., Darby N.J., Kemmink J. The roles of partly folded intermediates in protein folding. FASEB J. 1996, 10:110-118.
    • (1996) FASEB J. , vol.10 , pp. 110-118
    • Creighton, T.E.1    Darby, N.J.2    Kemmink, J.3
  • 29
    • 0030057477 scopus 로고    scopus 로고
    • Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues
    • Khorasanizadeh S., Peters I.D., Roder H. Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues. Nat. Struct. Biol. 1996, 3:193-205.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 30
    • 0034581327 scopus 로고    scopus 로고
    • Role of the molten globule state in protein folding
    • Arai M., Kuwajima K. Role of the molten globule state in protein folding. Adv. Protein Chem. 2000, 53:209-282.
    • (2000) Adv. Protein Chem. , vol.53 , pp. 209-282
    • Arai, M.1    Kuwajima, K.2
  • 31
    • 0031026007 scopus 로고    scopus 로고
    • How important is the molten globule for correct protein folding?
    • Creighton T.E. How important is the molten globule for correct protein folding?. Trends Biochem. Sci. 1997, 22:6-10.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 6-10
    • Creighton, T.E.1
  • 32
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn O.B. Molten globule and protein folding. Adv. Protein Chem. 1995, 47:83-229.
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 33
    • 0030575785 scopus 로고    scopus 로고
    • Is apomyoglobin a molten globule? Structural characterization by NMR
    • Eliezer D., Wright P.E. Is apomyoglobin a molten globule? Structural characterization by NMR. J. Mol. Biol. 1996, 263:531-538.
    • (1996) J. Mol. Biol. , vol.263 , pp. 531-538
    • Eliezer, D.1    Wright, P.E.2
  • 34
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings P.A., Wright P.E. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 1993, 262:892-896.
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 35
    • 0038532258 scopus 로고    scopus 로고
    • Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation
    • Kim Y.S., Randolph T.W., Manning M.C., Stevens F.J., Carpenter J.F. Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation. J. Mol. Biol. 2003, 278:10842-10850.
    • (2003) J. Mol. Biol. , vol.278 , pp. 10842-10850
    • Kim, Y.S.1    Randolph, T.W.2    Manning, M.C.3    Stevens, F.J.4    Carpenter, J.F.5
  • 36
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: the importance of being unfolded
    • Uversky V.N., Fink A.L. Conformational constraints for amyloid fibrillation: the importance of being unfolded. BBA-Proteins Proteom. 2004, 1698:131-153.
    • (2004) BBA-Proteins Proteom. , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 37
    • 0028955388 scopus 로고
    • Epidermal growth factor-related peptides and their receptors in human malignancies
    • Salomon D.S., Brandt R., Ciardello F., Normanno N. Epidermal growth factor-related peptides and their receptors in human malignancies. Crit. Rev. Oncol. Hematol. 1995, 19:183-232.
    • (1995) Crit. Rev. Oncol. Hematol. , vol.19 , pp. 183-232
    • Salomon, D.S.1    Brandt, R.2    Ciardello, F.3    Normanno, N.4
  • 38
    • 0015502199 scopus 로고
    • Epidermal growth-factor and a new derivative-rapid isolation procedures and biological and chemical characterization
    • Savage C.R., Cohen S. Epidermal growth-factor and a new derivative-rapid isolation procedures and biological and chemical characterization. J. Biol. Chem. 1972, 247:7609-7611.
    • (1972) J. Biol. Chem. , vol.247 , pp. 7609-7611
    • Savage, C.R.1    Cohen, S.2
  • 41
    • 0037291769 scopus 로고    scopus 로고
    • EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization
    • Ferguson K.M., Berger M.B., Mendrola J.M., Cho H.S., Leahy D.J., Lemmon M.A. EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Mol. Cell. 2003, 11:507-517.
    • (2003) Mol. Cell. , vol.11 , pp. 507-517
    • Ferguson, K.M.1    Berger, M.B.2    Mendrola, J.M.3    Cho, H.S.4    Leahy, D.J.5    Lemmon, M.A.6
  • 42
    • 0035860766 scopus 로고    scopus 로고
    • Crystal structure of human epidermal growth factor and its dimerization
    • Lu H.S., Chai J.J., Li M., Huang B.R., He C.H., Bi R.C. Crystal structure of human epidermal growth factor and its dimerization. J. Biol. Chem. 2001, 276:34913-34917.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34913-34917
    • Lu, H.S.1    Chai, J.J.2    Li, M.3    Huang, B.R.4    He, C.H.5    Bi, R.C.6
  • 45
    • 0026508986 scopus 로고
    • Solution structure of murine epidermal growth-factor determined by NMR-spectroscopy and refined by energy minimization with restraints
    • Montelione G.T., Wuthrich K., Burgess A.W., Nice E.C., Wagner G., Gibson K.D., Scheraga H.A. Solution structure of murine epidermal growth-factor determined by NMR-spectroscopy and refined by energy minimization with restraints. Biochemistry 1992, 31:236-249.
    • (1992) Biochemistry , vol.31 , pp. 236-249
    • Montelione, G.T.1    Wuthrich, K.2    Burgess, A.W.3    Nice, E.C.4    Wagner, G.5    Gibson, K.D.6    Scheraga, H.A.7
  • 46
    • 0036235377 scopus 로고    scopus 로고
    • The disulfide structure of denatured epidermal growth factor: preparation of scrambled disulfide isomers
    • Chang J.Y., Li L. The disulfide structure of denatured epidermal growth factor: preparation of scrambled disulfide isomers. J. Protein Chem. 2002, 21:203-213.
    • (2002) J. Protein Chem. , vol.21 , pp. 203-213
    • Chang, J.Y.1    Li, L.2
  • 47
    • 33845933462 scopus 로고    scopus 로고
    • Entropic folding pathway of human epidermal growth factor explored by disulfide scrambling and amplified collective motion simulations
    • Zhang Z.Y., Boyle P.C., Lu B.Y., Chang J.Y., Wriggers W. Entropic folding pathway of human epidermal growth factor explored by disulfide scrambling and amplified collective motion simulations. Biochemistry 2006, 45:15269-15278.
    • (2006) Biochemistry , vol.45 , pp. 15269-15278
    • Zhang, Z.Y.1    Boyle, P.C.2    Lu, B.Y.3    Chang, J.Y.4    Wriggers, W.5
  • 48
    • 0017083620 scopus 로고
    • Conformation and unfolding thermodynamics of epidermal growth-factor and derivatives
    • Holladay L.A., Savage C.R., Cohen S., Puett D. Conformation and unfolding thermodynamics of epidermal growth-factor and derivatives. Biochemistry 1976, 15:2624-2633.
    • (1976) Biochemistry , vol.15 , pp. 2624-2633
    • Holladay, L.A.1    Savage, C.R.2    Cohen, S.3    Puett, D.4
  • 49
    • 0031954924 scopus 로고    scopus 로고
    • Trapping of intermediates during the refolding of recombinant human epidermal growth factor (hEGF) by cyanylation, and subsequent structural elucidation by mass spectrometry
    • Wu.J., Yang Y., Watson J.T. Trapping of intermediates during the refolding of recombinant human epidermal growth factor (hEGF) by cyanylation, and subsequent structural elucidation by mass spectrometry. Protein Sci. 1998, 7:1017-1028.
    • (1998) Protein Sci. , vol.7 , pp. 1017-1028
    • Wu, J.1    Yang, Y.2    Watson, J.T.3
  • 50
  • 52
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides
    • Kaminski G.A., Friesner R.A., Tirado-Rives J., Jorgensen W.L. Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides. J. Phys. Chem. B 2001, 105:6474-6487.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 53
    • 0011746241 scopus 로고
    • A molecular-dynamics study of the decane water interface
    • Vanbuuren A.R., Marrink S.J., Berendsen H.J.C. A molecular-dynamics study of the decane water interface. J. Phys. Chem. 1993, 97:9206-9212.
    • (1993) J. Phys. Chem. , vol.97 , pp. 9206-9212
    • Vanbuuren, A.R.1    Marrink, S.J.2    Berendsen, H.J.C.3
  • 54
    • 38749123962 scopus 로고    scopus 로고
    • P-LINCS: a parallel linear constraint solver for molecular simulation
    • Hess B. P-LINCS: a parallel linear constraint solver for molecular simulation. J. Chem. Theory Comput. 2008, 4:116-122.
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 116-122
    • Hess, B.1
  • 55
    • 33846823909 scopus 로고
    • Particle mesh ewald-an N.Log(N) method for ewald sums in large systems
    • Darden T., York D., Pedersen L. Particle mesh ewald-an N.Log(N) method for ewald sums in large systems. J. Chem. Phys. 1993, 98:10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 60
    • 1942423619 scopus 로고    scopus 로고
    • MMTSB Tool Set: enhanced sampling and multiscale modeling methods for applications in structural biology
    • Feig M., Karanicolas J., Brooks C.L. MMTSB Tool Set: enhanced sampling and multiscale modeling methods for applications in structural biology. J. Mol. Graph. Model. 2004, 22:377-395.
    • (2004) J. Mol. Graph. Model. , vol.22 , pp. 377-395
    • Feig, M.1    Karanicolas, J.2    Brooks, C.L.3
  • 61
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure-pattern-recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure-pattern-recognition of hydrogen-bonded and geometrical features. Biopolymers 1983, 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 62
    • 41549127613 scopus 로고    scopus 로고
    • A temperature predictor for parallel tempering simulations
    • Patriksson A., van der Spoel D. A temperature predictor for parallel tempering simulations. Phys. Chem. Chem. Phys. 2008, 10:2073-2077.
    • (2008) Phys. Chem. Chem. Phys. , vol.10 , pp. 2073-2077
    • Patriksson, A.1    van der Spoel, D.2
  • 63
    • 77955844109 scopus 로고    scopus 로고
    • http://en.wikipedia.org/wiki/Force_field_%28chemistry%29.
  • 64
    • 17744395510 scopus 로고    scopus 로고
    • Sensitivity of the folding/unfolding transition state ensemble of chymotrypsin inhibitor 2 to changes in temperature and solvent
    • Day R., Daggett V. Sensitivity of the folding/unfolding transition state ensemble of chymotrypsin inhibitor 2 to changes in temperature and solvent. Protein Sci. 2005, 14:1242-1252.
    • (2005) Protein Sci. , vol.14 , pp. 1242-1252
    • Day, R.1    Daggett, V.2
  • 65
    • 0033308033 scopus 로고    scopus 로고
    • On the possibility of high-precision photothermal microeffects and the measurement of fast thermal denaturation of proteins
    • Huttmann G., Birngruber R. On the possibility of high-precision photothermal microeffects and the measurement of fast thermal denaturation of proteins. IEEE J. Sel. Top. Quant. Electron. 1999, 5:954-962.
    • (1999) IEEE J. Sel. Top. Quant. Electron. , vol.5 , pp. 954-962
    • Huttmann, G.1    Birngruber, R.2


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