메뉴 건너뛰기




Volumn 91, Issue 10, 2006, Pages 3805-3818

Reversible thermal denaturation of a 60-kDa genetically engineered β-sheet polypeptide

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; POLYPEPTIDE; POLYPROLINE 2; PROLINE DERIVATIVE; PROTEIN YEHK21; UNCLASSIFIED DRUG;

EID: 33751213891     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.082792     Document Type: Article
Times cited : (33)

References (96)
  • 2
    • 4344576758 scopus 로고    scopus 로고
    • Fabrication of molecular materials using peptide construction motifs
    • Zhao, X., and S. Zhang. 2004. Fabrication of molecular materials using peptide construction motifs. Trends Biotechnol. 22:470-476.
    • (2004) Trends Biotechnol. , vol.22 , pp. 470-476
    • Zhao, X.1    Zhang, S.2
  • 3
    • 28444485044 scopus 로고    scopus 로고
    • Laminated morphology of nontwisting beta-sheet fibrils constructed via peptide self-assembly
    • Lamm, M. S., K. Rajagopal, J. P. Schneider, and D. J. Pochan. 2005. Laminated morphology of nontwisting beta-sheet fibrils constructed via peptide self-assembly. J. Am. Chem. Soc. 127:16692-16700.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 16692-16700
    • Lamm, M.S.1    Rajagopal, K.2    Schneider, J.P.3    Pochan, D.J.4
  • 4
    • 0345530074 scopus 로고    scopus 로고
    • Self-assembling peptide polyelectrolyte beta-sheet complexes form nematic hydrogels
    • Aggeli, A., M. Bell, N. Boden, L. M. Carrick, and A. E. Strong. 2003. Self-assembling peptide polyelectrolyte beta-sheet complexes form nematic hydrogels. Angew. Chem. Int. Ed. Engl. 42:5603-5606.
    • (2003) Angew. Chem. Int. Ed. Engl. , vol.42 , pp. 5603-5606
    • Aggeli, A.1    Bell, M.2    Boden, N.3    Carrick, L.M.4    Strong, A.E.5
  • 5
    • 23444431592 scopus 로고    scopus 로고
    • Protein engineering approaches to biomaterials design
    • Maskarinec, S. A., and D. A. Tirrell. 2005. Protein engineering approaches to biomaterials design. Curr. Opin. Biotechnol. 16:422-426.
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 422-426
    • Maskarinec, S.A.1    Tirrell, D.A.2
  • 6
    • 1842484779 scopus 로고    scopus 로고
    • Designing materials for biology and medicine
    • Langer, R., and D. A. Tirrell. 2004. Designing materials for biology and medicine. Nature. 428:487-492.
    • (2004) Nature , vol.428 , pp. 487-492
    • Langer, R.1    Tirrell, D.A.2
  • 7
    • 2942568255 scopus 로고    scopus 로고
    • Design and analysis of nanoscale bioassemblies
    • 998-1001
    • Clark, J., E. M. Singer, D. R. Korns, and S. S. Smith. 2004. Design and analysis of nanoscale bioassemblies. Biotechniques. 36:992-996, 998-1001.
    • (2004) Biotechniques , vol.36 , pp. 992-996
    • Clark, J.1    Singer, E.M.2    Korns, D.R.3    Smith, S.S.4
  • 8
    • 0029554952 scopus 로고
    • Designing amino acid sequences to fold with good hydrophobic cores
    • Sun, S., R. Brem, H. S. Chan, and K. A. Dill. 1995. Designing amino acid sequences to fold with good hydrophobic cores. Protein Eng. 8: 1205-1213.
    • (1995) Protein Eng. , vol.8 , pp. 1205-1213
    • Sun, S.1    Brem, R.2    Chan, H.S.3    Dill, K.A.4
  • 9
    • 0028222235 scopus 로고
    • Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions
    • Chakrabartty, A., T. Kortemme, and R. L. Baldwin. 1994. Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions. Protein Sci. 3:843-852.
    • (1994) Protein Sci. , vol.3 , pp. 843-852
    • Chakrabartty, A.1    Kortemme, T.2    Baldwin, R.L.3
  • 11
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of β-hairpin formation
    • Munoz, V., P. A. Thompson, J. Hofrichter, and W. A. Eaton. 1997. Folding dynamics and mechanism of β-hairpin formation. Nature. 390:196-199.
    • (1997) Nature , vol.390 , pp. 196-199
    • Munoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 12
    • 0032917075 scopus 로고    scopus 로고
    • De novo design of a monomeric three-stranded antiparallel β-sheet
    • de Alba, E., J. Santoro, M. Rico, and M. A. Jimenez. 1999. De novo design of a monomeric three-stranded antiparallel β-sheet. Protein Sci. 8:854-865.
    • (1999) Protein Sci. , vol.8 , pp. 854-865
    • De Alba, E.1    Santoro, J.2    Rico, M.3    Jimenez, M.A.4
  • 14
    • 0034052404 scopus 로고    scopus 로고
    • Stabilization of a novel β-turn-like motif by nonconventional intramolecular hydrogen-bonding interactions in a model peptide incorporating β-alanine
    • Thakur, A. K., and R. Kishore. 2000. Stabilization of a novel β-turn-like motif by nonconventional intramolecular hydrogen-bonding interactions in a model peptide incorporating β-alanine. Biopolymers. 53:447-454.
    • (2000) Biopolymers , vol.53 , pp. 447-454
    • Thakur, A.K.1    Kishore, R.2
  • 15
    • 0032539561 scopus 로고    scopus 로고
    • Molecular picture of folding of a small α/β protein
    • Sheinerman, F. B., and C. L. Brooks, 3rd. 1998. Molecular picture of folding of a small α/β protein. Proc. Natl .Acad. Sci. USA. 95:1562-1567.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1562-1567
    • Sheinerman, F.B.1    Brooks III, C.L.2
  • 16
    • 0037459022 scopus 로고    scopus 로고
    • Interplay among tertiary contacts, secondary structure formation and side-chain packing in the protein folding mechanism: All-atom representation study of protein L.
    • Clementi, C., A. E. Garcia, and J. N. Onuchic. 2003. Interplay among tertiary contacts, secondary structure formation and side-chain packing in the protein folding mechanism: all-atom representation study of protein L. J. Mol. Biol. 326:933-954.
    • (2003) J. Mol. Biol. , vol.326 , pp. 933-954
    • Clementi, C.1    Garcia, A.E.2    Onuchic, J.N.3
  • 17
    • 3042848873 scopus 로고    scopus 로고
    • Context-dependent contributions of backbone hydrogen bonding to β-sheet folding energetics
    • Deechongkit, S., H. Nguyen, E. T. Powers, P. E. Dawson, M. Gruebele, and J. W. Kelly. 2004. Context-dependent contributions of backbone hydrogen bonding to β-sheet folding energetics. Nature. 430:101-105.
    • (2004) Nature , vol.430 , pp. 101-105
    • Deechongkit, S.1    Nguyen, H.2    Powers, E.T.3    Dawson, P.E.4    Gruebele, M.5    Kelly, J.W.6
  • 18
    • 0029786618 scopus 로고    scopus 로고
    • Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands
    • Uversky, V. N., V. P. Kutyshenko, N. Protasova, V. V. Rogov, K. S. Vassilenko, and A. T. Gudkov. 1996. Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands. Protein Sci. 5:1844-1851.
    • (1996) Protein Sci. , vol.5 , pp. 1844-1851
    • Uversky, V.N.1    Kutyshenko, V.P.2    Protasova, N.3    Rogov, V.V.4    Vassilenko, K.S.5    Gudkov, A.T.6
  • 22
    • 0030963424 scopus 로고    scopus 로고
    • Fast events in protein folding: Relaxation dynamics of secondary and tertiary structure in native apomyoglobin
    • Gilmanshin, R., S. Williams, R. H. Callender, W. H. Woodruff, and R. B. Dyer. 1997. Fast events in protein folding: relaxation dynamics of secondary and tertiary structure in native apomyoglobin. Proc. Natl. Acad. Sci. USA. 94:3709-3713.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3709-3713
    • Gilmanshin, R.1    Williams, S.2    Callender, R.H.3    Woodruff, W.H.4    Dyer, R.B.5
  • 23
    • 0034486196 scopus 로고    scopus 로고
    • Free energy determinants of tertiary structure and the evaluation of protein models
    • Petrey, D., and B. Honig. 2000. Free energy determinants of tertiary structure and the evaluation of protein models. Protein Sci. 9:2181-2191.
    • (2000) Protein Sci. , vol.9 , pp. 2181-2191
    • Petrey, D.1    Honig, B.2
  • 25
    • 23744503388 scopus 로고    scopus 로고
    • UV-resonance Raman thermal unfolding study of Trp-cage shows that it is not a simple two-state miniprotein
    • Ahmed, Z., I. A. Beta, A. V. Mikhonin, and S. A. Asher. 2005. UV-resonance Raman thermal unfolding study of Trp-cage shows that it is not a simple two-state miniprotein. J. Am. Chem. Soc. 127:10943-10950.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 10943-10950
    • Ahmed, Z.1    Beta, I.A.2    Mikhonin, A.V.3    Asher, S.A.4
  • 26
    • 1642414760 scopus 로고    scopus 로고
    • Probing the folding and unfolding dynamics of secondary and tertiary structures in a three-helix bundle protein
    • Vu, D. M., J. K. Myers, T. G. Oas, and R. B. Dyer. 2004. Probing the folding and unfolding dynamics of secondary and tertiary structures in a three-helix bundle protein. Biochemistry. 43:3582-3589.
    • (2004) Biochemistry , vol.43 , pp. 3582-3589
    • Vu, D.M.1    Myers, J.K.2    Oas, T.G.3    Dyer, R.B.4
  • 27
    • 0345133287 scopus 로고    scopus 로고
    • Folding a protein in a computer: An atomic description of the folding/unfolding of protein A
    • Garcia, A. E., and J. N. Onuchic. 2003. Folding a protein in a computer: an atomic description of the folding/unfolding of protein A. Proc. Natl. Acad. Sci. USA. 100:13898-13903.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13898-13903
    • Garcia, A.E.1    Onuchic, J.N.2
  • 28
    • 0034602807 scopus 로고    scopus 로고
    • Staphylococcal protein A: Unfolding pathways, unfolded states, and differences between the B and E domains
    • Alonso, D. O., and V. Daggett. 2000. Staphylococcal protein A: unfolding pathways, unfolded states, and differences between the B and E domains. Proc. Natl. Acad. Sci. USA. 97:133-138.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 133-138
    • Alonso, D.O.1    Daggett, V.2
  • 29
    • 3943113660 scopus 로고    scopus 로고
    • Using protein folding rates to test protein folding theories
    • Gillespie, B., and K. W. Plaxco. 2004. Using protein folding rates to test protein folding theories. Annu. Rev. Biochem. 73:837-859.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 837-859
    • Gillespie, B.1    Plaxco, K.W.2
  • 30
    • 0033117927 scopus 로고    scopus 로고
    • Deciphering the timescales and mechanisms of protein folding using minimal off-lattice models
    • Thirumalai, D., and D. K. Klimov. 1999. Deciphering the timescales and mechanisms of protein folding using minimal off-lattice models. Curr. Opin. Struct. Biol. 9:197-207.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 197-207
    • Thirumalai, D.1    Klimov, D.K.2
  • 32
    • 1842298212 scopus 로고    scopus 로고
    • From evinthal to pathways to funnels
    • Dill, K. A., and H. S. Chan. 1997. From evinthal to pathways to funnels. Nat. Struct. Biol. 4:10-19.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 33
    • 1342324030 scopus 로고    scopus 로고
    • Exploring folding free energy landscapes using computational protein design
    • Kuhlman, B., and D. Baker. 2004. Exploring folding free energy landscapes using computational protein design. Curr. Opin. Struct. Biol. 14:89-95.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 89-95
    • Kuhlman, B.1    Baker, D.2
  • 34
    • 0036280693 scopus 로고    scopus 로고
    • Protein and peptide folding explored with molecular simulations
    • Brooks, C. L., 3rd. 2002. Protein and peptide folding explored with molecular simulations. Acc. Chem. Res. 35:447-454.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 447-454
    • Brooks III, C.L.1
  • 35
    • 0344407048 scopus 로고    scopus 로고
    • Kinetics of cytochrome C folding: Atomically detailed simulations
    • Cardenas, A. E., and R. Elber. 2003. Kinetics of cytochrome C folding: atomically detailed simulations. Proteins. 51:245-257.
    • (2003) Proteins , vol.51 , pp. 245-257
    • Cardenas, A.E.1    Elber, R.2
  • 36
    • 0842299585 scopus 로고    scopus 로고
    • Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of α-helical content and compactness
    • Uzawa, T., S. Akiyama, T. Kimura, S. Takahashi, K. Ishimori, I. Morishima, and T. Fujisawa. 2004. Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of α-helical content and compactness. Proc. Natl. Acad. Sci. USA. 101: 1171-1176.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1171-1176
    • Uzawa, T.1    Akiyama, S.2    Kimura, T.3    Takahashi, S.4    Ishimori, K.5    Morishima, I.6    Fujisawa, T.7
  • 39
    • 0037058992 scopus 로고    scopus 로고
    • Probing the folding free energy landscape of the Src-SH3 protein domain
    • Shea, J. E., J. N. Onuchic, and C. L. Brooks, 3rd. 2002. Probing the folding free energy landscape of the Src-SH3 protein domain. Proc. Natl. Acad. Sci. USA. 99:16064-16068.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16064-16068
    • Shea, J.E.1    Onuchic, J.N.2    Brooks III, C.L.3
  • 41
    • 30144436601 scopus 로고    scopus 로고
    • Intermediacy of poly(L-proline) II and β-strand conformations in poly(L-lysine) β-sheet formation probed by temperature-jump/UV resonance Raman spectroscopy
    • Jiji, R. D., G. Balakrishnan, Y. Hu, and T. G. Spiro. 2006. Intermediacy of poly(L-proline) II and β-strand conformations in poly(L-lysine) β-sheet formation probed by temperature-jump/UV resonance Raman spectroscopy. Biochemistry. 45:34-41.
    • (2006) Biochemistry , vol.45 , pp. 34-41
    • Jiji, R.D.1    Balakrishnan, G.2    Hu, Y.3    Spiro, T.G.4
  • 43
    • 0030845525 scopus 로고    scopus 로고
    • Effects of amino acid side-chain volume on chain packing in genetically engineered periodic polypeptides
    • Cantor, E. J., E. D. Atkins, S. J. Cooper, M. J. Fournier, T. L. Mason, and D. A. Tirrell. 1997. Effects of amino acid side-chain volume on chain packing in genetically engineered periodic polypeptides. J. Biochem. (Tokyo). 122:217-225.
    • (1997) J. Biochem. (Tokyo) , vol.122 , pp. 217-225
    • Cantor, E.J.1    Atkins, E.D.2    Cooper, S.J.3    Fournier, M.J.4    Mason, T.L.5    Tirrell, D.A.6
  • 44
    • 0035834113 scopus 로고    scopus 로고
    • Hierarchical self-assembly of chiral rod-like molecules as a model for peptide β-sheet tapes, ribbons, fibrils, and fibers
    • Aggeli, A., I. A. Nyrkova, M. Bell, R. Harding, L. Carrick, T. C. McLeish, A. N. Semenov, and N. Boden. 2001. Hierarchical self-assembly of chiral rod-like molecules as a model for peptide β-sheet tapes, ribbons, fibrils, and fibers. Proc. Natl. Acad. Sci. USA. 98: 11857-11862.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11857-11862
    • Aggeli, A.1    Nyrkova, I.A.2    Bell, M.3    Harding, R.4    Carrick, L.5    McLeish, T.C.6    Semenov, A.N.7    Boden, N.8
  • 47
    • 13844254633 scopus 로고    scopus 로고
    • Deep-UV Raman spectrometer tunable between 193 and 205 nm for structural characterization of proteins
    • Lednev, I. K., V. V. Ermolenkov, W. He, and M. Xu. 2005. Deep-UV Raman spectrometer tunable between 193 and 205 nm for structural characterization of proteins. Anal. Bioanal. Chem. 381:431-437.
    • (2005) Anal. Bioanal. Chem. , vol.381 , pp. 431-437
    • Lednev, I.K.1    Ermolenkov, V.V.2    He, W.3    Xu, M.4
  • 48
    • 0032478198 scopus 로고    scopus 로고
    • UV resonance Raman-selective amide vibrational enhancement: Quantitative methodology for determining protein secondary structure
    • Chi, Z., X. G. Chen, J. S. Holtz, and S. A. Asher. 1998. UV resonance Raman-selective amide vibrational enhancement: quantitative methodology for determining protein secondary structure. Biochemistry. 37:2854-2864.
    • (1998) Biochemistry , vol.37 , pp. 2854-2864
    • Chi, Z.1    Chen, X.G.2    Holtz, J.S.3    Asher, S.A.4
  • 49
    • 0035965724 scopus 로고    scopus 로고
    • Dihedral psi angle dependence of the amide III vibration: A uniquely sensitive UV resonance Raman secondary structural probe
    • Asher, S. A., A. Ianoul, G. Mix, M. N. Boyden, A. Karnoup, M. Diem, and R. Schweitzer-Stenner. 2001. Dihedral psi angle dependence of the amide III vibration: a uniquely sensitive UV resonance Raman secondary structural probe. J. Am. Chem. Soc. 123:11775-11781.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11775-11781
    • Asher, S.A.1    Ianoul, A.2    Mix, G.3    Boyden, M.N.4    Karnoup, A.5    Diem, M.6    Schweitzer-Stenner, R.7
  • 50
    • 0036845354 scopus 로고    scopus 로고
    • The behavior of polyamino acids reveals an inverse side chain effect in amyloid structure formation
    • Fandrich, M., and C. M. Dobson. 2002. The behavior of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J. 21:5682-5690.
    • (2002) EMBO J. , vol.21 , pp. 5682-5690
    • Fandrich, M.1    Dobson, C.M.2
  • 51
    • 0036186024 scopus 로고    scopus 로고
    • UV Raman monitoring of histidine protonation and H-(2)H exchange in plastocyanin
    • Wu, Q., F. Li, W. Wang, M. H. Hecht, and T. G. Spiro. 2002. UV Raman monitoring of histidine protonation and H-(2)H exchange in plastocyanin. J. Inorg. Biochem. 88:381-387.
    • (2002) J. Inorg. Biochem. , vol.88 , pp. 381-387
    • Wu, Q.1    Li, F.2    Wang, W.3    Hecht, M.H.4    Spiro, T.G.5
  • 52
    • 1342296786 scopus 로고    scopus 로고
    • Ultraviolet Raman spectrometry
    • John Wiley & Sons, New York
    • Asher, S. A. 2001. Ultraviolet Raman spectrometry. In Handbook of Vibrational Spectroscopy. John Wiley & Sons, New York. 557-571.
    • (2001) Handbook of Vibrational Spectroscopy , pp. 557-571
    • Asher, S.A.1
  • 53
    • 0023661664 scopus 로고
    • Secondary structure determination in proteins from deep (192-223-nm) ultraviolet Raman spectroscopy
    • Copeland, R. A., and T. G. Spiro. 1987. Secondary structure determination in proteins from deep (192-223-nm) ultraviolet Raman spectroscopy. Biochemistry. 26:2134-2139.
    • (1987) Biochemistry , vol.26 , pp. 2134-2139
    • Copeland, R.A.1    Spiro, T.G.2
  • 54
    • 0022437688 scopus 로고
    • Ultraviolet resonance Raman spectroscopy of biopolymers
    • Hudson, B., and L. Mayne. 1986. Ultraviolet resonance Raman spectroscopy of biopolymers. Methods Enzymol. 130:331-350.
    • (1986) Methods Enzymol. , vol.130 , pp. 331-350
    • Hudson, B.1    Mayne, L.2
  • 55
    • 0034023387 scopus 로고    scopus 로고
    • Conformational transitions in model silk peptides
    • Wilson, D., R. Valluzzi, and D. Kaplan. 2000. Conformational transitions in model silk peptides. Biophys. J. 78:2690-2701.
    • (2000) Biophys. J. , vol.78 , pp. 2690-2701
    • Wilson, D.1    Valluzzi, R.2    Kaplan, D.3
  • 56
    • 26844488077 scopus 로고    scopus 로고
    • Lysozyme fibrillation: Deep UV Raman spectroscopic characterization of protein structural transformation
    • Xu, M., V. V. Ermolenkov, W. He, V. N. Uversky, L. Fredriksen, and I. K. Lednev. 2005. Lysozyme fibrillation: deep UV Raman spectroscopic characterization of protein structural transformation. Biopolymers. 79:58-61.
    • (2005) Biopolymers , vol.79 , pp. 58-61
    • Xu, M.1    Ermolenkov, V.V.2    He, W.3    Uversky, V.N.4    Fredriksen, L.5    Lednev, I.K.6
  • 57
    • 19744362700 scopus 로고    scopus 로고
    • UV resonance Raman determination of polyproline II, extended 2.5(1)-helix, and β-sheet psi angle energy landscape in poly-L-lysine and poly-L-glutamic acid
    • Mikhonin, A. V., N. S. Myshakina, S. V. Bykov, and S. A. Asher. 2005. UV resonance Raman determination of polyproline II, extended 2.5(1)-helix, and β-sheet psi angle energy landscape in poly-L-lysine and poly-L-glutamic acid. J. Am. Chem. Soc. 127:7712-7720.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 7712-7720
    • Mikhonin, A.V.1    Myshakina, N.S.2    Bykov, S.V.3    Asher, S.A.4
  • 58
    • 0033536452 scopus 로고    scopus 로고
    • Alpha-helix peptide folding and unfolding activation barriers: A nano-second UV resonance Raman study
    • Lednev, I. K., A. S. Karnoup, M. C. Sparrow, and S. A. Asher. 1999. Alpha-helix peptide folding and unfolding activation barriers: a nano-second UV resonance Raman study. J. Am. Chem. Soc. 121:8074-8086.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 8074-8086
    • Lednev, I.K.1    Karnoup, A.S.2    Sparrow, M.C.3    Asher, S.A.4
  • 59
    • 3142754280 scopus 로고    scopus 로고
    • UV Raman demonstrates that α-helical polyalanine peptides melt to polyproline II conformations
    • Asher, S. A., A. V. Mikhonin, and S. Bykov. 2004. UV Raman demonstrates that α-helical polyalanine peptides melt to polyproline II conformations. J. Am. Chem. Soc. 126:8433-8440.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8433-8440
    • Asher, S.A.1    Mikhonin, A.V.2    Bykov, S.3
  • 60
    • 1342324027 scopus 로고    scopus 로고
    • Progress toward a molecular-level structural understanding of amyloid fibrils
    • Tycko, R. 2004. Progress toward a molecular-level structural understanding of amyloid fibrils. Curr. Opin. Struct. Biol. 14:96-103.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 96-103
    • Tycko, R.1
  • 61
    • 1642297346 scopus 로고    scopus 로고
    • Core structure of amyloid fibril proposed from IR-microscope linear dichroism
    • Hiramatsu, H., Y. Goto, H. Naiki, and T. Kitagawa. 2004. Core structure of amyloid fibril proposed from IR-microscope linear dichroism. J. Am. Chem. Soc. 126:3008-3009.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3008-3009
    • Hiramatsu, H.1    Goto, Y.2    Naiki, H.3    Kitagawa, T.4
  • 62
    • 0037174998 scopus 로고    scopus 로고
    • Structural and dynamic features of Alzheimer's Aβ peptide in amyloid fibrils studied by site-directed spin labeling
    • Torok, M., S. Milton, R. Kayed, P. Wu, T. McIntire, C. G. Glabe, and R. Langen. 2002. Structural and dynamic features of Alzheimer's Aβ peptide in amyloid fibrils studied by site-directed spin labeling. J. Biol. Chem. 277:40810-40815.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40810-40815
    • Torok, M.1    Milton, S.2    Kayed, R.3    Wu, P.4    McIntire, T.5    Glabe, C.G.6    Langen, R.7
  • 63
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein
    • Harper, J. D., C. M. Lieber, and P. T. Lansbury, Jr. 1997. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein. Chem. Biol. 4:951-959.
    • (1997) Chem. Biol. , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury Jr., P.T.3
  • 65
    • 24644510813 scopus 로고    scopus 로고
    • Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure
    • Sambashivan, S., Y. Liu, M. R. Sawaya, M. Gingery, and D. Eisenberg. 2005. Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure. Nature. 437:266-269.
    • (2005) Nature , vol.437 , pp. 266-269
    • Sambashivan, S.1    Liu, Y.2    Sawaya, M.R.3    Gingery, M.4    Eisenberg, D.5
  • 67
    • 0037014715 scopus 로고    scopus 로고
    • Hydrogen bonding to Trp b37 is the first step in a compound pathway for hemoglobin allostery
    • Goldbeck, R. A., R. M. Esquerra, and D. S. Kliger. 2002. Hydrogen bonding to Trp b37 is the first step in a compound pathway for hemoglobin allostery. J. Am. Chem. Soc. 124:7646-7647.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 7646-7647
    • Goldbeck, R.A.1    Esquerra, R.M.2    Kliger, D.S.3
  • 68
    • 0344990168 scopus 로고    scopus 로고
    • Dynamics of protein and chromophore structural changes in the photocycle of photoactive yellow protein monitored by time-resolved optical rotatory dispersion
    • Chen, E., T. Gensch, A. B. Gross, J. Hendriks, K. J. Hellingwerf, and D. S. Kliger. 2003. Dynamics of protein and chromophore structural changes in the photocycle of photoactive yellow protein monitored by time-resolved optical rotatory dispersion. Biochemistry. 42:2062-2071.
    • (2003) Biochemistry , vol.42 , pp. 2062-2071
    • Chen, E.1    Gensch, T.2    Gross, A.B.3    Hendriks, J.4    Hellingwerf, K.J.5    Kliger, D.S.6
  • 69
    • 0003546549 scopus 로고
    • Nakanishi, K., N. Berova, and R. W. Woody, editors. VCH, New York
    • Nakanishi, K., N. Berova, and R. W. Woody, editors. 1994. Circular Dichroism: Principles and Applications. VCH, New York.
    • (1994) Circular Dichroism: Principles and Applications
  • 70
    • 14544292864 scopus 로고    scopus 로고
    • Uncoupled peptide bond vibrations in α-helical and polyproline II conformations of polyalanine peptides
    • Mikhonin, A. V., and S. A. Asher. 2005. Uncoupled peptide bond vibrations in α-helical and polyproline II conformations of polyalanine peptides. J. Phys. Chem. B. 109:3047-3052.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 3047-3052
    • Mikhonin, A.V.1    Asher, S.A.2
  • 71
    • 0034692360 scopus 로고    scopus 로고
    • Uncoupled adjacent amide vibrations in small peptides
    • Mix, G., R. Schweitzer-Stenner, and S. A. Asher. 2000. Uncoupled adjacent amide vibrations in small peptides. J. Am. Chem. Soc. 122:9028 -9029.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 9028-9029
    • Mix, G.1    Schweitzer-Stenner, R.2    Asher, S.A.3
  • 72
    • 0037065773 scopus 로고    scopus 로고
    • Comparison between UV Raman and circular dichroism detection of short α helices in Bombolitin III
    • Ozdemir, A., I. K. Lednev, and S. A. Asher. 2002. Comparison between UV Raman and circular dichroism detection of short α helices in Bombolitin III. Biochemistry. 41:1893-1896.
    • (2002) Biochemistry , vol.41 , pp. 1893-1896
    • Ozdemir, A.1    Lednev, I.K.2    Asher, S.A.3
  • 73
    • 0033363464 scopus 로고    scopus 로고
    • Solid-state tunable kHz ultraviolet laser for Raman applications
    • Zhao, X., R. Chen, C. Tengroth, and T. G. Spiro. 1999. Solid-state tunable kHz ultraviolet laser for Raman applications. Appl. Spectrosc. 53:1200-1205.
    • (1999) Appl. Spectrosc. , vol.53 , pp. 1200-1205
    • Zhao, X.1    Chen, R.2    Tengroth, C.3    Spiro, T.G.4
  • 74
    • 0030282280 scopus 로고    scopus 로고
    • Applications of a new 206 5-nm continuous-wave laser source: UV Raman determination of protein secondary structure and CVD diamond material properties
    • Holtz, J. S. W., R. W. Bormett, Z. Chi, N. Cho, X. G. Chen, V. Pajcini, S. A. Asher, L. Spinelli, P. Owen, and M. Arrigoni. 1996. Applications of a new 206 5-nm continuous-wave laser source: UV Raman determination of protein secondary structure and CVD diamond material properties. Appl. Spectrosc. 50:1459.
    • (1996) Appl. Spectrosc. , vol.50 , pp. 1459
    • Holtz, J.S.W.1    Bormett, R.W.2    Chi, Z.3    Cho, N.4    Chen, X.G.5    Pajcini, V.6    Asher, S.A.7    Spinelli, L.8    Owen, P.9    Arrigoni, M.10
  • 75
    • 0032477947 scopus 로고    scopus 로고
    • UV resonance Raman determination of protein acid denaturation: Selective unfolding of helical segments of horse myoglobin
    • Chi, Z., and S. A. Asher. 1998. UV resonance Raman determination of protein acid denaturation: selective unfolding of helical segments of horse myoglobin. Biochemistry. 37:2865-2872.
    • (1998) Biochemistry , vol.37 , pp. 2865-2872
    • Chi, Z.1    Asher, S.A.2
  • 76
    • 0033614784 scopus 로고    scopus 로고
    • Ultraviolet resonance Raman examination of horse apomyoglobin acid unfolding intermediates
    • Chi, Z., and S. A. Asher. 1999. Ultraviolet resonance Raman examination of horse apomyoglobin acid unfolding intermediates. Biochemistry. 38:8196-8203.
    • (1999) Biochemistry , vol.38 , pp. 8196-8203
    • Chi, Z.1    Asher, S.A.2
  • 77
    • 0027515699 scopus 로고
    • Protein structure from ultraviolet resonance Raman spectroscopy
    • Austin, J. C., K. R. Rodgers, and T. G. Spiro. 1993. Protein structure from ultraviolet resonance Raman spectroscopy. Methods Enzymol. 226:374-396.
    • (1993) Methods Enzymol. , vol.226 , pp. 374-396
    • Austin, J.C.1    Rodgers, K.R.2    Spiro, T.G.3
  • 78
    • 0002832320 scopus 로고    scopus 로고
    • UV lasers revolutionize Raman spectroscopy
    • Asher, S. A., C. H. Munro, and Z. Chi. 1997. UV lasers revolutionize Raman spectroscopy. Laser Focus World. 33:99-109.
    • (1997) Laser Focus World , vol.33 , pp. 99-109
    • Asher, S.A.1    Munro, C.H.2    Chi, Z.3
  • 79
    • 1842403587 scopus 로고    scopus 로고
    • Turn residue sequence determines β-hairpin conformation in designed peptides
    • de Alba, E., M. A. Jiménez, and M. Rico. 1997. Turn residue sequence determines β-hairpin conformation in designed peptides. J. Am. Chem. Soc. 119:175-183.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 175-183
    • De Alba, E.1    Jiménez, M.A.2    Rico, M.3
  • 80
    • 0024391832 scopus 로고
    • Conformation of β-hairpins in protein structures. A systematic classification with applications to modeling by homology, electron density fitting and protein engineering
    • Sibanda, B. L., T. L. Blundell, and J. M. Thornton. 1989. Conformation of β-hairpins in protein structures. A systematic classification with applications to modeling by homology, electron density fitting and protein engineering. J. Mol. Biol. 206:759-777.
    • (1989) J. Mol. Biol. , vol.206 , pp. 759-777
    • Sibanda, B.L.1    Blundell, T.L.2    Thornton, J.M.3
  • 81
    • 0032212855 scopus 로고    scopus 로고
    • Effect of local sequence inversions on the crystalline antiparallel β-sheet lamellar structures of periodic polypeptides: Implications for chain-folding
    • Parkhe, A. D., S. J. Cooper, E. D. Atkins, M. J. Fournier, T. L. Mason, and D. A. Tirrell. 1998. Effect of local sequence inversions on the crystalline antiparallel β-sheet lamellar structures of periodic polypeptides: implications for chain-folding. Int. J. Biol. Macromol. 23: 251-258.
    • (1998) Int. J. Biol. Macromol. , vol.23 , pp. 251-258
    • Parkhe, A.D.1    Cooper, S.J.2    Atkins, E.D.3    Fournier, M.J.4    Mason, T.L.5    Tirrell, D.A.6
  • 82
    • 32544446167 scopus 로고    scopus 로고
    • Peptide secondary structure folding reaction coordinate: Correlation between UV Raman amide III frequency, Psi Ramachandran angle, and hydrogen bonding
    • Mikhonin, A. V., S. V. Bykov, N. S. Myshakina, and S. A. Asher. 2006. Peptide secondary structure folding reaction coordinate: correlation between UV Raman amide III frequency, Psi Ramachandran angle, and hydrogen bonding. .J Phys. Chem. B. 110:1928-1943.
    • (2006) J. Phys. Chem. B. , vol.110 , pp. 1928-1943
    • Mikhonin, A.V.1    Bykov, S.V.2    Myshakina, N.S.3    Asher, S.A.4
  • 83
    • 0038281274 scopus 로고    scopus 로고
    • Vibrational spectroscopic detection of β- and γ-turns in synthetic and natural peptides and proteins
    • Vass, E., M. Hollosi, F. Besson, and R. Buchet. 2003. Vibrational spectroscopic detection of β- and γ-turns in synthetic and natural peptides and proteins. Chem. Rev. 103:1917-1954.
    • (2003) Chem. Rev. , vol.103 , pp. 1917-1954
    • Vass, E.1    Hollosi, M.2    Besson, F.3    Buchet, R.4
  • 84
    • 0037061998 scopus 로고    scopus 로고
    • UV resonance Raman study of the spatial dependence of α-helix unfolding
    • Ianoul, A., A. Mikhonin, I. K. Lednev, and S. A. Asher. 2002. UV resonance Raman study of the spatial dependence of α-helix unfolding. J. Phys. Chem. A. 106:3621-3624.
    • (2002) J. Phys. Chem. A , vol.106 , pp. 3621-3624
    • Ianoul, A.1    Mikhonin, A.2    Lednev, I.K.3    Asher, S.A.4
  • 85
    • 85030592029 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 86
    • 0027489832 scopus 로고
    • Thermodynamics of unfolding for turkey ovomucoid third domain: Thermal and chemical denaturation
    • Swint, L., and A. D. Robertson. 1993. Thermodynamics of unfolding for turkey ovomucoid third domain: thermal and chemical denaturation. Protein Sci. 2:2037-2049.
    • (1993) Protein Sci. , vol.2 , pp. 2037-2049
    • Swint, L.1    Robertson, A.D.2
  • 87
    • 12944309313 scopus 로고    scopus 로고
    • Scaling of folding times with protein size
    • Naganathan, A. N., and V. Munoz. 2005. Scaling of folding times with protein size. J. Am. Chem. Soc. 127:480-481.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 480-481
    • Naganathan, A.N.1    Munoz, V.2
  • 88
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco, K. W., K. T. Simons, and D. Baker. 1998. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277:985-994.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 89
    • 2942689229 scopus 로고    scopus 로고
    • Prediction of protein folding rates from the amino acid sequence-predicted secondary structure
    • Ivankov, D. N., and A. V. Finkelstein. 2004. Prediction of protein folding rates from the amino acid sequence-predicted secondary structure. Proc. Natl. Acad. Sci. USA. 101:8942-8944.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8942-8944
    • Ivankov, D.N.1    Finkelstein, A.V.2
  • 90
    • 0000050196 scopus 로고
    • From minimal models to real proteins: Time scales for protein folding kinetics
    • Thirumalai, D. 1995. From minimal models to real proteins: Time scales for protein folding kinetics. Journal de Physique I. 5:1457-1467.
    • (1995) Journal de Physique I , vol.5 , pp. 1457-1467
    • Thirumalai, D.1
  • 91
    • 0034984144 scopus 로고    scopus 로고
    • Protein folding theory: From lattice to all-atom models
    • Mirny, L., and E. Shakhnovich. 2001. Protein folding theory: from lattice to all-atom models. Annu. Rev. Biophys. Biomol. Struct. 30:361-396.
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 361-396
    • Mirny, L.1    Shakhnovich, E.2
  • 95
    • 4544301224 scopus 로고    scopus 로고
    • Amyloidogenic hexapeptide fragment of medin: Homology to functional islet amyloid polypeptide fragments
    • Reches, M., and E. Gazit. 2004. Amyloidogenic hexapeptide fragment of medin: homology to functional islet amyloid polypeptide fragments. Amyloid. 11:81-89.
    • (2004) Amyloid , vol.11 , pp. 81-89
    • Reches, M.1    Gazit, E.2
  • 96
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett, J. T., and P. T. Lansbury, Jr. 1993. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell. 73:1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.