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Volumn 100, Issue 5, 2011, Pages 1306-1315

Assisted peptide folding by surface pattern recognition

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EID: 79953898194     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.12.3735     Document Type: Article
Times cited : (18)

References (66)
  • 1
    • 67650045816 scopus 로고    scopus 로고
    • Limitations of induced folding in molecular recognition by intrinsically disordered proteins
    • Hazy, E., and P. Tompa. 2009. Limitations of induced folding in molecular recognition by intrinsically disordered proteins. ChemPhysChem. 10:1415-1419.
    • (2009) ChemPhysChem. , vol.10 , pp. 1415-1419
    • Hazy, E.1    Tompa, P.2
  • 2
    • 57049095821 scopus 로고    scopus 로고
    • Function and structure of inherently disordered proteins
    • Dunker, A. K., I. Silman, J. L. Sussman. 2008. Function and structure of inherently disordered proteins. Curr. Opin. Struct. Biol. 18:756-764.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 756-764
    • Dunker, A.K.1    Silman, I.2    Sussman, J.L.3
  • 3
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • DOI 10.1038/nrm1589
    • Dyson, H. J., and P. E. Wright. 2005. Intrinsically unstructured proteins and their functions. Nat. Rev. 6:197-208. (Pubitemid 40314921)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 4
    • 47649102449 scopus 로고    scopus 로고
    • Regulation of cell division by intrinsically unstructured proteins: Intrinsic flexibility, modularity, and signaling conduits
    • DOI 10.1021/bi8006803
    • Galea, C. A., Y. Wang, R. W. Kriwacki. 2008. Regulation of cell division by intrinsically unstructured proteins: intrinsic flexibility, modularity, and signaling conduits. Biochemistry. 47:7598-7609. (Pubitemid 352019491)
    • (2008) Biochemistry , vol.47 , Issue.29 , pp. 7598-7609
    • Galea, C.A.1    Wang, Y.2    Sivakolundu, S.G.3    Kriwacki, R.W.4
  • 5
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • DOI 10.1016/j.febslet.2005.03.072, PII S0014579305004242
    • Tompa, P. 2005. The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett. 579:3346-3354. (Pubitemid 40804685)
    • (2005) FEBS Letters , vol.579 , Issue.15 , pp. 3346-3354
    • Tompa, P.1
  • 6
    • 69249142709 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: From kinetics to thermodynamics
    • Almeida, P. F., and A. Pokorny. 2009. Mechanisms of antimicrobial, cytolytic, and cell-penetrating peptides: from kinetics to thermodynamics. Biochemistry. 48:8083-8093.
    • (2009) Biochemistry , vol.48 , pp. 8083-8093
    • Almeida, P.F.1    Pokorny, A.2
  • 7
    • 66249119965 scopus 로고    scopus 로고
    • Molecular simulation of protein-surface interactions: Benefits, problems, solutions, and future directions
    • Latour, R. A. 2008. Molecular simulation of protein-surface interactions: benefits, problems, solutions, and future directions. Biointerphases. 3:FC2-FC12.
    • (2008) Biointerphases , vol.3
    • Latour, R.A.1
  • 8
    • 68249102600 scopus 로고    scopus 로고
    • Mechanism of ligandinduced folding of a natively unfolded helixless variant of rabbit I-BABP
    • Rea, A. M., V. Thurston, and M. S. Searle. 2009. Mechanism of ligandinduced folding of a natively unfolded helixless variant of rabbit I-BABP. Biochemistry. 48:7556-7564.
    • (2009) Biochemistry , vol.48 , pp. 7556-7564
    • Rea, A.M.1    Thurston, V.2    Searle, M.S.3
  • 10
    • 33750586279 scopus 로고    scopus 로고
    • Coupling ligand recognition to protein folding in an engineered variant of rabbit ileal lipid binding protein
    • DOI 10.1039/b610130e
    • Kouvatsos, N., J. K. Meldrum, N. R. Thomas. 2006. Coupling ligand recognition to protein folding in an engineered variant of rabbit ileal lipid binding protein. Chem. Commun. (Camb.). 44:4623-4625. (Pubitemid 44684560)
    • (2006) Chemical Communications , Issue.44 , pp. 4623-4625
    • Kouvatsos, N.1    Meldrum, J.K.2    Searle, M.S.3    Thomas, N.R.4
  • 11
    • 62349086577 scopus 로고    scopus 로고
    • Beyond molecular beacons: Optical sensors based on the binding-induced folding of proteins and polypeptides
    • Oh, K. J., K. J. Cash, and K. W. Plaxco. 2009. Beyond molecular beacons: optical sensors based on the binding-induced folding of proteins and polypeptides. Chemistry. 15:2244-2251.
    • (2009) Chemistry , vol.15 , pp. 2244-2251
    • Oh, K.J.1    Cash, K.J.2    Plaxco, K.W.3
  • 12
    • 32444436232 scopus 로고    scopus 로고
    • Structure-function analysis of the epitope for 4E10, a broadly neutralizing human immunodeficiency virus type 1 antibody
    • DOI 10.1128/JVI.80.4.1680-1687.2006
    • Brunel, F. M., M. B. Zwick, P. E. Dawson. 2006. Structure-function analysis of the epitope for 4E10, a broadly neutralizing human immunodeficiency virus type 1 antibody. J. Virol. 80:1680-1687. (Pubitemid 43228710)
    • (2006) Journal of Virology , vol.80 , Issue.4 , pp. 1680-1687
    • Brunel, F.M.1    Zwick, M.B.2    Cardoso, R.M.F.3    Nelson, J.D.4    Wilson, I.A.5    Burton, D.R.6    Dawson, P.E.7
  • 13
    • 33750458342 scopus 로고    scopus 로고
    • Excimer-based peptide beacons: A convenient experimental approach for monitoring polypeptide-protein and polypeptide-oligonucleotide interactions
    • DOI 10.1021/ja0651310
    • Oh, K. J., K. J. Cash, and K. W. Plaxco. 2006. Excimer-based peptide beacons: a convenient experimental approach for monitoring polypeptide-protein and polypeptide-oligonucleotide interactions. J. Am. Chem. Soc. 128:14018-14019. (Pubitemid 44657481)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.43 , pp. 14018-14019
    • Oh, K.J.1    Cash, K.J.2    Plaxco, K.W.3
  • 14
    • 34347353352 scopus 로고    scopus 로고
    • Peptide beacons: A new design for polypeptide-based optical biosensors
    • DOI 10.1021/bc060319u
    • Oh, K. J., K. J. Cash, . , K. W. Plaxco. 2007. Peptide beacons: a new design for polypeptide-based optical biosensors. Bioconjug. Chem. 18:607-609. (Pubitemid 47010776)
    • (2007) Bioconjugate Chemistry , vol.18 , Issue.3 , pp. 607-609
    • Oh, K.J.1    Cash, K.J.2    Hugenberg, V.3    Plaxco, K.W.4
  • 15
    • 40949117264 scopus 로고    scopus 로고
    • Flexible nets: Disorder and induced fit in the associations of p53 and 14-3-3 with their partners
    • Oldfield, C. J., J. Meng, A. K. Dunker. 2008. Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners. BMC Genomics. 9(Suppl 1):S1.
    • (2008) BMC Genomics. , vol.9 , Issue.SUPPL. 1
    • Oldfield, C.J.1    Meng, J.2    Dunker, A.K.3
  • 16
    • 72149094848 scopus 로고    scopus 로고
    • The adherence of platelets to adsorbed albumin by receptor-mediated recognition of binding sites exposed by adsorption-induced unfolding
    • Sivaraman, B., and R. A. Latour. 2010. The adherence of platelets to adsorbed albumin by receptor-mediated recognition of binding sites exposed by adsorption-induced unfolding. Biomaterials. 31:1036-1044.
    • (2010) Biomaterials , vol.31 , pp. 1036-1044
    • Sivaraman, B.1    Latour, R.A.2
  • 17
    • 70649114517 scopus 로고    scopus 로고
    • The relationship between platelet adhesion on surfaces and the structure versus the amount of adsorbed fibrinogen
    • Sivaraman, B., and R. A. Latour. 2010. The relationship between platelet adhesion on surfaces and the structure versus the amount of adsorbed fibrinogen. Biomaterials. 31:832-839.
    • (2010) Biomaterials , vol.31 , pp. 832-839
    • Sivaraman, B.1    Latour, R.A.2
  • 18
    • 41349094526 scopus 로고    scopus 로고
    • Surface-induced conformational changes in lattice model proteins by Monte Carlo simulation
    • Castells, V., S. Yang, and P. R. Van Tassel. 2002. Surface-induced conformational changes in lattice model proteins by Monte Carlo simulation. Phys. Rev. E Stat. Nonlin. Soft Matter Phys. 65:031912.
    • (2002) Phys. Rev. e Stat. Nonlin. Soft Matter Phys. , vol.65 , pp. 031912
    • Castells, V.1    Yang, S.2    Van Tassel, P.R.3
  • 19
    • 0031574008 scopus 로고    scopus 로고
    • Adsorption-induced conformational changes in the serine proteinase savinase: A tryptophan fluorescence and circular dichroism study
    • DOI 10.1006/jcis.1997.5205
    • Maste, M. C. L., W. Norde, and A. J. W. G. Visser. 1997. Adsorptioninduced conformational changes in the serine proteinase savinase: a tryptophan fluorescence and circular dichroism study. J. Colloid Interface Sci. 196:224-230. (Pubitemid 28080785)
    • (1997) Journal of Colloid and Interface Science , vol.196 , Issue.2 , pp. 224-230
    • Maste, M.C.L.1    Norde, W.2    Visser, A.J.W.G.3
  • 22
    • 0028500779 scopus 로고
    • A short linear peptide that folds into a native stable β-hairpin in aqueous solution
    • Blanco, F. J., G. Rivas, and L. Serrano. 1994. A short linear peptide that folds into a native stable β-hairpin in aqueous solution. Nat. Struct. Biol. 1:584-590.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 584-590
    • Blanco, F.J.1    Rivas, G.2    Serrano, L.3
  • 23
    • 0032246263 scopus 로고    scopus 로고
    • Minimal model systems for β sheet secondary structure in proteins
    • Gellman, S. H. 1998. Minimal model systems for β sheet secondary structure in proteins. Curr. Opin. Chem. Biol. 2:717-725. (Pubitemid 128646742)
    • (1998) Current Opinion in Chemical Biology , vol.2 , Issue.6 , pp. 717-725
    • Gellman, S.H.1
  • 24
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of β-hairpin formation
    • DOI 10.1038/36626
    • Muñoz, V., P. A. Thompson, W. A. Eaton. 1997. Folding dynamics and mechanism of β-hairpin formation. Nature. 390:196-199. (Pubitemid 27507992)
    • (1997) Nature , vol.390 , Issue.6656 , pp. 196-199
    • Munoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 26
    • 0029351694 scopus 로고
    • Protein motifs. 7. the four-helix bundle: What determines a fold?
    • Kamtekar, S., and M. H. Hecht. 1995. Protein motifs. 7. The four-helix bundle: what determines a fold? FASEB J. 9:1013-1022.
    • (1995) FASEB J. , vol.9 , pp. 1013-1022
    • Kamtekar, S.1    Hecht, M.H.2
  • 27
    • 0028846974 scopus 로고
    • Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteins
    • West, M. W., and M. H. Hecht. 1995. Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteins. Protein Sci. 4:2032-2039.
    • (1995) Protein Sci. , vol.4 , pp. 2032-2039
    • West, M.W.1    Hecht, M.H.2
  • 28
    • 0029064713 scopus 로고
    • Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides
    • Xiong, H., B. L. Buckwalter, M. H. Hecht. 1995. Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides. Proc. Natl. Acad. Sci. USA. 92:6349-6353.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6349-6353
    • Xiong, H.1    Buckwalter, B.L.2    Hecht, M.H.3
  • 29
    • 77951128761 scopus 로고    scopus 로고
    • Engineering a twohelix bundle protein for folding studies
    • Dodson, C. A., N. Ferguson, . , A. R. Fersht. 2010. Engineering a twohelix bundle protein for folding studies. Protein Eng. Des. Sel. 23:357-364.
    • (2010) Protein Eng. Des. Sel. , vol.23 , pp. 357-364
    • Dodson, C.A.1    Ferguson, N.2    Fersht, A.R.3
  • 30
    • 0033694923 scopus 로고    scopus 로고
    • De novo design of helical bundles as models for understanding protein folding and function
    • Hill, R. B., D. P. Raleigh, W. F. DeG]\rado. 2000. De novo design of helical bundles as models for understanding protein folding and function. Acc. Chem. Res. 33:745-754.
    • (2000) Acc. Chem. Res. , vol.33 , pp. 745-754
    • Hill, R.B.1    Raleigh, D.P.2    Degrado, W.F.3
  • 31
    • 52249085709 scopus 로고    scopus 로고
    • Theunfoldomics decade: An update on intrinsically disordered proteins
    • Dunker, A. K., C. J. Oldfield, ..., V. N. Uversky. 2008. Theunfoldomics decade: an update on intrinsically disordered proteins. BMC Genomics. 9(Suppl 2):S1.
    • (2008) BMC Genomics. , vol.9 , Issue.SUPPL. 2
    • Dunker, A.K.1    Oldfield, C.J.2    Uversky, V.N.3
  • 33
    • 0029662315 scopus 로고    scopus 로고
    • Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: Conformational disorder mediates binding diversity
    • Kriwacki, R. W., L. Hengst, .., P. E. Wright. 1996. Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. Proc. Natl. Acad. Sci. USA. 93:11504-11509.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11504-11509
    • Kriwacki, R.W.1    Hengst, L.2    Wright, P.E.3
  • 34
    • 75149194975 scopus 로고    scopus 로고
    • Sequence periodicity and secondary structure propensity in model proteins
    • Bellesia, G., A. I. Jewett, and J. E. Shea. 2010. Sequence periodicity and secondary structure propensity in model proteins. Protein Sci. 19:141-154.
    • (2010) Protein Sci. , vol.19 , pp. 141-154
    • Bellesia, G.1    Jewett, A.I.2    Shea, J.E.3
  • 35
    • 0030601851 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of folding of a de novo designed four-helix bundle protein
    • DOI 10.1006/jmbi.1996.0578
    • Guo, Z., and D. Thirumalai. 1996. Kinetics and thermodynamics of folding of a de novo designed four-helix bundle protein. J. Mol. Biol. 263:323-343. (Pubitemid 26363091)
    • (1996) Journal of Molecular Biology , vol.263 , Issue.2 , pp. 323-343
    • Guo, Z.1    Thirumalai, D.2
  • 36
    • 0025368288 scopus 로고
    • Metastability of the folded states of globular proteins
    • Honeycutt, J. D., and D. Thirumalai. 1990. Metastability of the folded states of globular proteins. Proc. Natl. Acad. Sci. USA. 87:3526-3529.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3526-3529
    • Honeycutt, J.D.1    Thirumalai, D.2
  • 37
    • 0026643094 scopus 로고
    • The nature of folded states of globular proteins
    • Honeycutt, J. D., and D. Thirumalai. 1992. The nature of folded states of globular proteins. Biopolymers. 32:695-709.
    • (1992) Biopolymers. , vol.32 , pp. 695-709
    • Honeycutt, J.D.1    Thirumalai, D.2
  • 38
    • 0015217634 scopus 로고
    • The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale
    • Nozaki, Y., and C. Tanford. 1971. The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale. J. Biol. Chem. 246:2211-2217.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2211-2217
    • Nozaki, Y.1    Tanford, C.2
  • 39
    • 0038519321 scopus 로고
    • Contribution of hydrophobic interactions to the stability of the globular conformation of proteins
    • Tanford, C. 1962. Contribution of hydrophobic interactions to the stability of the globular conformation of proteins. J. Am. Chem. Soc. 84:4240-4247.
    • (1962) J. Am. Chem. Soc. , vol.84 , pp. 4240-4247
    • Tanford, C.1
  • 40
    • 34247595392 scopus 로고    scopus 로고
    • Experimental measures of amino acid hydrophobicity and the topology of transmembrane and globular proteins
    • DOI 10.1085/jgp.200709743
    • Wolfenden, R. 2007. Experimental measures of amino acid hydrophobicity and the topology of transmembrane and globular proteins. J. Gen. Physiol. 129:357-362. (Pubitemid 46686451)
    • (2007) Journal of General Physiology , vol.129 , Issue.5 , pp. 357-362
    • Wolfenden, R.1
  • 41
    • 0019883174 scopus 로고
    • Affinities of amino acid side chains for solvent water
    • Wolfenden, R., L. Andersson, C. C. Southgate. 1981. Affinities of amino acid side chains for solvent water. Biochemistry. 20:849-855.
    • (1981) Biochemistry , vol.20 , pp. 849-855
    • Wolfenden, R.1    Andersson, L.2    Southgate, C.C.3
  • 42
    • 0043238073 scopus 로고    scopus 로고
    • Effects of confinement in chaperonin assisted protein folding: Rate enhancement by decreasing the roughness of the folding energy landscape
    • DOI 10.1016/S0022-2836(03)00929-X
    • Baumketner, A., A. Jewett, and J. E. Shea. 2003. Effects of confinement in chaperonin assisted protein folding: rate enhancement by decreasing the roughness of the folding energy landscape. J. Mol. Biol. 332: 701-713. (Pubitemid 37075991)
    • (2003) Journal of Molecular Biology , vol.332 , Issue.3 , pp. 701-713
    • Baumketner, A.1    Jewett, A.2    Shea, J.E.3
  • 43
    • 28844454252 scopus 로고    scopus 로고
    • Parallel tempering: Theory, applications, and new perspectives
    • DOI 10.1039/b509983h
    • Earl, D. J., and M. W. Deem. 2005. Parallel tempering: theory, applications, and new perspectives. Phys. Chem. Chem. Phys. 7:3910-3916. (Pubitemid 41771858)
    • (2005) Physical Chemistry Chemical Physics , vol.7 , Issue.23 , pp. 3910-3916
    • Earl, D.J.1    Deem, M.W.2
  • 44
    • 0001616080 scopus 로고    scopus 로고
    • Replica-exchange molecular dynamics method for protein folding
    • PII S0009261499011239
    • Sugita, Y., and Y. Okamoto. 1999. Replica-exchange molecular dynamics method for protein folding. Chem. Phys. Lett. 314:141-151. (Pubitemid 129556751)
    • (1999) Chemical Physics Letters , vol.314 , Issue.1-2 , pp. 141-151
    • Sugita, Y.1    Okamoto, Y.2
  • 45
    • 35949020425 scopus 로고
    • Replica Monte Carlo simulation of spin glasses
    • Swendsen, R. H., and J. S. Wang. 1986. Replica Monte Carlo simulation of spin glasses. Phys. Rev. Lett. 57:2607-2609.
    • (1986) Phys. Rev. Lett. , vol.57 , pp. 2607-2609
    • Swendsen, R.H.1    Wang, J.S.2
  • 46
    • 85031244208 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 47
    • 4243819810 scopus 로고
    • New Monte Carlo technique for studying phase transitions
    • Ferrenberg, A. M., and R. H. Swendsen. 1988. New Monte Carlo technique for studying phase transitions. Phys. Rev. Lett. 61:2635-2638.
    • (1988) Phys. Rev. Lett. , vol.61 , pp. 2635-2638
    • Ferrenberg, A.M.1    Swendsen, R.H.2
  • 48
    • 33646987405 scopus 로고
    • Optimized Monte Carlo data analysis
    • Ferrenberg, A. M., and R. H. Swendsen. 1989. Optimized Monte Carlo data analysis. Phys. Rev. Lett. 63:1195-1198.
    • (1989) Phys. Rev. Lett. , vol.63 , pp. 1195-1198
    • Ferrenberg, A.M.1    Swendsen, R.H.2
  • 49
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules. I. the method
    • Kumar, S., D. Bouzida, J. M. Rosenberg. 1992. The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method. J. Comput. Chem. 13:1011-1021.
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Kumar, S.1    Bouzida, D.2    Rosenberg, J.M.3
  • 50
    • 0007992814 scopus 로고    scopus 로고
    • Protein plasticity to the extreme: Changing the topology of a 4-α- helical bundle with a single amino acid substitution
    • DOI 10.1016/S0969-2126(99)80081-1
    • Glykos, N. M., G. Cesareni, and M. Kokkinidis. 1999. Protein plasticity to the extreme: changing the topology of a 4-α-helical bundle with a single amino acid substitution. Structure. 7:597-603. (Pubitemid 29277413)
    • (1999) Structure , vol.7 , Issue.6 , pp. 597-603
    • Glykos, N.M.1    Cesareni, G.2    Kokkinidis, M.3
  • 52
    • 58149277699 scopus 로고    scopus 로고
    • Factors governing helix formation in peptides confined to carbon nanotubes
    • O'Brien, E. P., G. Stan, .., B. R. Brooks. 2008. Factors governing helix formation in peptides confined to carbon nanotubes. Nano Lett. 8:3702-3708.
    • (2008) Nano Lett. , vol.8 , pp. 3702-3708
    • O'Brien, E.P.1    Stan, G.2    Brooks, B.R.3
  • 53
    • 0002617993 scopus 로고    scopus 로고
    • A simple model of chaperonin-mediated protein folding
    • DOI 10.1002/(SICI)1097-0134(199603)24:3<345::AID-PROT7>3.0.CO;2-F
    • Chan, H. S., and K. A. Dill. 1996. A simple model of chaperonin-mediated protein folding. Proteins. 24:345-351. (Pubitemid 26095966)
    • (1996) Proteins: Structure, Function and Genetics , vol.24 , Issue.3 , pp. 345-351
    • Chan, H.S.1    Dill, K.A.2
  • 54
    • 58149498257 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of protein folding under confinement
    • Mittal, J., and R. B. Best. 2008. Thermodynamics and kinetics of protein folding under confinement. Proc. Natl. Acad. Sci. USA. 105:20233-20238.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 20233-20238
    • Mittal, J.1    Best, R.B.2
  • 57
    • 0035949430 scopus 로고    scopus 로고
    • Stabilization of proteins in confined spaces
    • DOI 10.1021/bi0155504
    • Zhou, H. X., and K. A. Dill. 2001. Stabilization of proteins in confined spaces. Biochemistry. 40:11289-11293. (Pubitemid 32911271)
    • (2001) Biochemistry , vol.40 , Issue.38 , pp. 11289-11293
    • Zhou, H.-X.1    Dill, K.A.2
  • 58
    • 77958171872 scopus 로고    scopus 로고
    • Thermal and structural stability of adsorbed proteins
    • Sharma, S., B. J. Berne, and S. K. Kumar. 2010. Thermal and structural stability of adsorbed proteins. Biophys. J. 99:1157-1165.
    • (2010) Biophys. J. , vol.99 , pp. 1157-1165
    • Sharma, S.1    Berne, B.J.2    Kumar, S.K.3
  • 59
    • 0033515436 scopus 로고    scopus 로고
    • Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity
    • DOI 10.1006/jmbi.1999.2591
    • Betancourt, M. R., and D. Thirumalai. 1999. Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity. J. Mol. Biol. 287:627-644. (Pubitemid 29168438)
    • (1999) Journal of Molecular Biology , vol.287 , Issue.3 , pp. 627-644
    • Betancourt, M.R.1    Thirumalai, D.2
  • 61
    • 33646155113 scopus 로고    scopus 로고
    • Structural transitions of confined model proteins: Molecular dynamics simulation and experimental validation
    • Lu, D., Z. Liu, and J. Wu. 2006. Structural transitions of confined model proteins: molecular dynamics simulation and experimental validation. Biophys. J. 90:3224-3238.
    • (2006) Biophys. J. , vol.90 , pp. 3224-3238
    • Lu, D.1    Liu, Z.2    Wu, J.3
  • 64
    • 0032190497 scopus 로고    scopus 로고
    • Fibrinogen adsorption and host tissue responses to plasma functionalized surfaces
    • DOI 10.1002/(SICI)1097-4636(199810)42:1<156::AID-JBM19>3.0.CO;2-J
    • Tang, L., Y. Wu, and R. B. Timmons. 1998. Fibrinogen adsorption and host tissue responses to plasma functionalized surfaces. J. Biomed. Mater. Res. 42:156-163. (Pubitemid 28413008)
    • (1998) Journal of Biomedical Materials Research , vol.42 , Issue.1 , pp. 156-163
    • Tang, L.1    Wu, Y.2    Timmons, R.B.3
  • 65
    • 0345688752 scopus 로고    scopus 로고
    • Influence of hydrophobic teflon particles on the structure of amyloid β-peptide
    • DOI 10.1021/bm034151g
    • Giacomelli, C. E., and W. Norde. 2003. Influence of hydrophobic Teflon particles on the structure of amyloid β-peptide. Biomacromolecules. 4:1719-1726. (Pubitemid 37455585)
    • (2003) Biomacromolecules , vol.4 , Issue.6 , pp. 1719-1726
    • Giacomelli, C.E.1    Norde, W.2
  • 66
    • 20444488480 scopus 로고    scopus 로고
    • Conformational changes of the amyloid β-peptide (1-40) adsorbed on solid surfaces
    • DOI 10.1002/mabi.200400189
    • Giacomelli, C. E., and W. Norde. 2005. Conformational changes ofthe amyloid β-peptide (1-40) adsorbed on solid surfaces. Macromol. Biosci. 5:401-407. (Pubitemid 40813976)
    • (2005) Macromolecular Bioscience , vol.5 , Issue.5 , pp. 401-407
    • Giacomelli, C.E.1    Norde, W.2


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