메뉴 건너뛰기




Volumn 8, Issue 12, 1999, Pages 2773-2783

Synthesis, folding, and structure of the β-turn mimic modified B1 domain of streptococcal protein G

Author keywords

Activity; Dibenzofuran; Domain B1 of protein G; Folding; Protein engineering; Stability; Structure; turn mimic

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; DIBENZOFURAN DERIVATIVE;

EID: 0033433950     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.12.2773     Document Type: Article
Times cited : (28)

References (65)
  • 1
    • 0026764471 scopus 로고
    • Thermodynamic analysis of the folding of the streptucoccal protein G IgG-binding domains B1 and B2: Why small proteins tend to have high denaturation temperatures?
    • Alexander P, Fahnestock S, Lee T, Orban J, Bryan P. 1992a. Thermodynamic analysis of the folding of the streptucoccal protein G IgG-binding domains B1 and B2: Why small proteins tend to have high denaturation temperatures? Biochemistry 31:3597-3603.
    • (1992) Biochemistry , vol.31 , pp. 3597-3603
    • Alexander, P.1    Fahnestock, S.2    Lee, T.3    Orban, J.4    Bryan, P.5
  • 2
    • 0026782853 scopus 로고
    • Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein g
    • Alexander P, Orban J, Bryan P. 1992b. Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein G. Biochemistry 31:7243-7248.
    • (1992) Biochemistry , vol.31 , pp. 7243-7248
    • Alexander, P.1    Orban, J.2    Bryan, P.3
  • 3
    • 0028857598 scopus 로고
    • Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements
    • Altieri AS, Hinton DP, Byrd RA. 1995. Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements. J Am Chem Soc 117:7566-7567.
    • (1995) J Am Chem Soc , vol.117 , pp. 7566-7567
    • Altieri, A.S.1    Hinton, D.P.2    Byrd, R.A.3
  • 4
    • 0027213390 scopus 로고
    • Structural engineering of the HIV-1 protease molecule with a β-turn of fixed geometry
    • Baca M, Alewood PF, Kent SBH. 1993. Structural engineering of the HIV-1 protease molecule with a β-turn of fixed geometry. Protein Sci 2:1085-1091.
    • (1993) Protein Sci , vol.2 , pp. 1085-1091
    • Baca, M.1    Alewood, P.F.2    Kent, S.B.H.3
  • 5
    • 0028301327 scopus 로고
    • NMR solution structure of the isolated fragment of the N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like β-hairpin formation
    • Blanco FJ, Jiménez MA, Pienda A, Rico M, Santoro J, Nicto JL. 1994a. NMR solution structure of the isolated fragment of the N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like β-hairpin formation. Biochemistry 33:6004-6014.
    • (1994) Biochemistry , vol.33 , pp. 6004-6014
    • Blanco, F.J.1    Jiménez, M.A.2    Pienda, A.3    Rico, M.4    Santoro, J.5    Nicto, J.L.6
  • 6
    • 0030623419 scopus 로고    scopus 로고
    • Role of a nonnative interaction in the folding of the protein G B1 domain as inferred from the conformational analysis of the α-helix fragment
    • Blanco FJ, Ortiz AR, Serrano L. 1997. Role of a nonnative interaction in the folding of the protein G B1 domain as inferred from the conformational analysis of the α-helix fragment. Folding Design 2:123-133.
    • (1997) Folding Design , vol.2 , pp. 123-133
    • Blanco, F.J.1    Ortiz, A.R.2    Serrano, L.3
  • 7
    • 0028500779 scopus 로고
    • A short linear peptide that folds into a native stable β-hairpin in aqueous solution
    • Blanco FJ, Rivas G, Serrano L. 1994b. A short linear peptide that folds into a native stable β-hairpin in aqueous solution. Struct Biol 1:584-590.
    • (1994) Struct Biol , vol.1 , pp. 584-590
    • Blanco, F.J.1    Rivas, G.2    Serrano, L.3
  • 8
    • 0029070488 scopus 로고
    • Folding of protein G B1 domain studied by the conformational characterization of fragments comprising its secondary structure elements
    • Blanco FJ, Serrano L. 1995. Folding of protein G B1 domain studied by the conformational characterization of fragments comprising its secondary structure elements. Eur J Biochem 230:634-649.
    • (1995) Eur J Biochem , vol.230 , pp. 634-649
    • Blanco, F.J.1    Serrano, L.2
  • 10
    • 0030986375 scopus 로고    scopus 로고
    • Protein alchemy: Changing β-sheet into α-helix
    • Dalai S, Balasubramanian S, Regan L. 1997. Protein alchemy: Changing β-sheet into α-helix. Nat Struct Biol 4:548-552.
    • (1997) Nat Struct Biol , vol.4 , pp. 548-552
    • Dalai, S.1    Balasubramanian, S.2    Regan, L.3
  • 11
    • 1842403587 scopus 로고    scopus 로고
    • Turn residue sequence determines β-hairpin conformation in design peptides
    • de Alba E, Jiménez MA, Rico M. 1997. Turn residue sequence determines β-hairpin conformation in design 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
  • 12
    • 0030334822 scopus 로고    scopus 로고
    • Conformational investigation of designed short linear peptides able to fold into β-hairpin structures in aqueous solution
    • de Alba E, Jiménez MA, Rica M, Nieto JL. 1996. Conformational investigation of designed short linear peptides able to fold into β-hairpin structures in aqueous solution. Folding Design 1:133-144.
    • (1996) Folding Design , vol.1 , pp. 133-144
    • De Alba, E.1    Jiménez, M.A.2    Rica, M.3    Nieto, J.L.4
  • 13
    • 84936887577 scopus 로고
    • A dibenzofuran-based amino acid designed to nucleate antiparallel β-sheet structure: Evidence for intramolecular hydrogen-bond formation
    • Díaz H, Espina JR, Kelly JW. 1992. A dibenzofuran-based amino acid designed to nucleate antiparallel β-sheet structure: Evidence for intramolecular hydrogen-bond formation. J Am Chem Soc 114:8316-8318.
    • (1992) J Am Chem Soc , vol.114 , pp. 8316-8318
    • Díaz, H.1    Espina, J.R.2    Kelly, J.W.3
  • 14
    • 0026018110 scopus 로고
    • The synthesis of dibenzofuran based diacids and amino acids designed to nucleate parallel and antiparallel β-sheet formation
    • Díaz H, Kelly JW. 1991. The synthesis of dibenzofuran based diacids and amino acids designed to nucleate parallel and antiparallel β-sheet formation. Tetrahedron 32:5725-5728.
    • (1991) Tetrahedron , vol.32 , pp. 5725-5728
    • Díaz, H.1    Kelly, J.W.2
  • 15
    • 0027299230 scopus 로고
    • The design of water soluble β-sheet structure based on a nucleation strategy
    • Díaz H, Tsang KD, Choo D, Kelly JW. 1993a. The design of water soluble β-sheet structure based on a nucleation strategy. Tetrahedron 49:3533-3545.
    • (1993) Tetrahedron , vol.49 , pp. 3533-3545
    • Díaz, H.1    Tsang, K.D.2    Choo, D.3    Kelly, J.W.4
  • 16
    • 0000691139 scopus 로고
    • Design, synthesis, and partial characterization of water-soluble β-sheets stabilized by a dibenzofuran-based amino acid
    • Díaz H, Tsang KY, Choo D, Espina JR, Kelly JW. 1993b. Design, synthesis, and partial characterization of water-soluble β-sheets stabilized by a dibenzofuran-based amino acid. J Am Chem Soc 115:3790-3791.
    • (1993) J Am Chem Soc , vol.115 , pp. 3790-3791
    • Díaz, H.1    Tsang, K.Y.2    Choo, D.3    Espina, J.R.4    Kelly, J.W.5
  • 18
    • 0024278572 scopus 로고
    • Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix
    • Dyson HJ, Rance M, Houghten RA, Wright PE, Lerner RA. 1988. Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix. J Mol Biol 201:201-217.
    • (1988) J Mol Biol , vol.201 , pp. 201-217
    • Dyson, H.J.1    Rance, M.2    Houghten, R.A.3    Wright, P.E.4    Lerner, R.A.5
  • 19
    • 0023682353 scopus 로고
    • Streptococcal protein G has affinity for both Fab- and Fc-fragment of human IgG
    • Erntell M, Myhre EB, Sjöbring U, Björk L. 1988. Streptococcal protein G has affinity for both Fab- and Fc-fragment of human IgG. Mol Immun 25:121-126.
    • (1988) Mol Immun , vol.25 , pp. 121-126
    • Erntell, M.1    Myhre, E.B.2    Sjöbring, U.3    Björk, L.4
  • 20
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • Fink AL. 1998. Protein aggregation: Folding aggregates, inclusion bodies and amyloid. Folding Design 3:9-23.
    • (1998) Folding Design , vol.3 , pp. 9-23
    • Fink, A.L.1
  • 21
    • 0028787226 scopus 로고
    • Structural and dynamic characterisation of the urea denatured state of the immunoglobulin binding domain of streptococcal protein g by multidimensional heteronuclear NMR spectroscopy
    • Frank MK, Glore GM, Gronenborn AM. 1995. Structural and dynamic characterisation of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy. Protein Sci 4:2605-2615.
    • (1995) Protein Sci , vol.4 , pp. 2605-2615
    • Frank, M.K.1    Glore, G.M.2    Gronenborn, A.M.3
  • 23
    • 0028354429 scopus 로고
    • Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR
    • Gallagher T, Alexander P, Bryan P, Gilliland GL. 1994. Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR. Biochemistry 33:4721-4729.
    • (1994) Biochemistry , vol.33 , pp. 4721-4729
    • Gallagher, T.1    Alexander, P.2    Bryan, P.3    Gilliland, G.L.4
  • 24
    • 0026101930 scopus 로고
    • The secondary structure of protein G, a robust molecule
    • Goward CR, Irons LI, Murphy JP, Atkinson T. 1991. The secondary structure of protein G, a robust molecule. Biochem J 274:503-507.
    • (1991) Biochem J , vol.274 , pp. 503-507
    • Goward, C.R.1    Irons, L.I.2    Murphy, J.P.3    Atkinson, T.4
  • 25
    • 0028506408 scopus 로고
    • Amino acids that specify structure through hydrophobic clustering and histidine-aromatic interactions lead to biologically active peptidomimetics
    • Graciani NR, Tsang KY, McCutchen SL, Kelly JW. 1994. Amino acids that specify structure through hydrophobic clustering and histidine-aromatic interactions lead to biologically active peptidomimetics. Bioorg Med Chem 2:999-1006.
    • (1994) Bioorg Med Chem , vol.2 , pp. 999-1006
    • Graciani, N.R.1    Tsang, K.Y.2    McCutchen, S.L.3    Kelly, J.W.4
  • 27
    • 0030566807 scopus 로고    scopus 로고
    • Core mutants of the immunoglobulin binding domain of the streptococcal protein G: Stability and structural integrity
    • Gronenborn AM, Frank K, Clore GM. 1996. Core mutants of the immunoglobulin binding domain of the streptococcal protein G: Stability and structural integrity. FEBS Lett 398:312-316.
    • (1996) FEBS Lett , vol.398 , pp. 312-316
    • Gronenborn, A.M.1    Frank, K.2    Clore, G.M.3
  • 28
    • 0031818010 scopus 로고    scopus 로고
    • Computational protein engineering
    • Hellinga HW. 1998. Computational protein engineering. Nat Struct Biol 5:525-527.
    • (1998) Nat Struct Biol , vol.5 , pp. 525-527
    • Hellinga, H.W.1
  • 29
    • 0029151158 scopus 로고
    • Submillisecond folding of monomeric λ repressor
    • Huang GS, Oas TG. 1995. Submillisecond folding of monomeric λ repressor. Proc Natl Acad Sci USA 92:6878-6882.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6878-6882
    • Huang, G.S.1    Oas, T.G.2
  • 31
    • 0013676199 scopus 로고    scopus 로고
    • Chemical exchange effects on spectra
    • New York: Wiley.
    • Kaplan JI. 1996. Chemical exchange effects on spectra. In: Encyclopedia of nuclear magnetic resonance, vol. 2. New York: Wiley. pp 1247-1256.
    • (1996) Encyclopedia of Nuclear Magnetic Resonance , vol.2 , pp. 1247-1256
    • Kaplan, J.I.1
  • 32
    • 0029062012 scopus 로고
    • A short β-sheet containing proline nucleated by a 2,2′-substituted tolan β-turn mimetic
    • Kemp DS, Li ZQ. 1995. A short β-sheet containing proline nucleated by a 2,2′-substituted tolan β-turn mimetic. Tetrahedron Lett 36:4179-4180.
    • (1995) Tetrahedron Lett , vol.36 , pp. 4179-4180
    • Kemp, D.S.1    Li, Z.Q.2
  • 33
    • 0030922940 scopus 로고    scopus 로고
    • An experimental approach to evaluating the role of backbone interactions in proteins using unnatural amino acid mutagenesis
    • Koh JT, Cornish VW, Schultz PG. 1997. An experimental approach to evaluating the role of backbone interactions in proteins using unnatural amino acid mutagenesis. Biochemistry 36:11314-11322.
    • (1997) Biochemistry , vol.36 , pp. 11314-11322
    • Koh, J.T.1    Cornish, V.W.2    Schultz, P.G.3
  • 34
    • 2642670311 scopus 로고    scopus 로고
    • Design of a 20-amino acid three-stranded β-sheet protein
    • Kortemme T, Ramirez-Alvarado M, Serrano L. 1998. Design of a 20-amino acid three-stranded β-sheet protein. Science 281:253-256.
    • (1998) Science , vol.281 , pp. 253-256
    • Kortemme, T.1    Ramirez-Alvarado, M.2    Serrano, L.3
  • 35
    • 0028578686 scopus 로고
    • Fast folding of a prototypic polypeptide: The immunoglobulin binding domain of streptococcal protein G
    • Kuszewski J, Clore GM, Gronenborn AM. 1994. Fast folding of a prototypic polypeptide: The immunoglobulin binding domain of streptococcal protein G. Protein Sci 3:1945-1952.
    • (1994) Protein Sci , vol.3 , pp. 1945-1952
    • Kuszewski, J.1    Clore, G.M.2    Gronenborn, A.M.3
  • 36
    • 0031779918 scopus 로고    scopus 로고
    • Design, structure and stability of a hyperthermophilic protein variant
    • Malakauskas SM, Mayo SL. 1998. Design, structure and stability of a hyperthermophilic protein variant. Nat Struct Biol 5:470-475.
    • (1998) Nat Struct Biol , vol.5 , pp. 470-475
    • Malakauskas, S.M.1    Mayo, S.L.2
  • 38
    • 0343869257 scopus 로고    scopus 로고
    • Incorporation of a β-turn mimic in the N-terminal fragment of the B1 domain of streptococcal protein G
    • Melnyk O, Boutillon C, Draffan L, Odaert B, Jean F, Lippens G, Tartar A. 1998. Incorporation of a β-turn mimic in the N-terminal fragment of the B1 domain of streptococcal protein G. Lett Pept Sci 5:147-150.
    • (1998) Lett Pept Sci , vol.5 , pp. 147-150
    • Melnyk, O.1    Boutillon, C.2    Draffan, L.3    Odaert, B.4    Jean, F.5    Lippens, G.6    Tartar, A.7
  • 39
    • 0022699646 scopus 로고
    • Solid phase peptide synthesis
    • Merrifield B. 1986. Solid phase peptide synthesis. Science 232:341-347.
    • (1986) Science , vol.232 , pp. 341-347
    • Merrifield, B.1
  • 40
    • 0028176595 scopus 로고
    • Measurement of the β-sheet-forming propensities of amino acids
    • Minor DL, Kim PS. 1994a. Measurement of the β-sheet-forming propensities of amino acids. Nature 367:660-663.
    • (1994) Nature , vol.367 , pp. 660-663
    • Minor, D.L.1    Kim, P.S.2
  • 41
    • 0027998757 scopus 로고
    • Context is a major determinant of β-sheet propensity
    • Minor DL, Kim PS. 1994b. Context is a major determinant of β-sheet propensity. Nature 371:264-267.
    • (1994) Nature , vol.371 , pp. 264-267
    • Minor, D.L.1    Kim, P.S.2
  • 42
    • 0032499752 scopus 로고    scopus 로고
    • Expressed protein ligation: A general method for protein engineering
    • Muir TW, Sondhi D, Cole PA. 1998. Expressed protein ligation: A general method for protein engineering. Proc Natl Acad Sci USA 95:6705-6710.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6705-6710
    • Muir, T.W.1    Sondhi, D.2    Cole, P.A.3
  • 44
    • 0028447768 scopus 로고
    • Elucidating the folding problem of α-helical peptides using empirical parameters
    • Muñoz V, Serrano L. 1994a. Elucidating the folding problem of α-helical peptides using empirical parameters. Nat Struct Biol 1:399-409.
    • (1994) Nat Struct Biol , vol.1 , pp. 399-409
    • Muñoz, V.1    Serrano, L.2
  • 45
    • 0028873081 scopus 로고
    • Elucidating the folding problem of α-helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides
    • Muñoz V, Serrano L. 1994b. Elucidating the folding problem of α-helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides. J Mol Biol 245:215-296.
    • (1994) J Mol Biol , vol.245 , pp. 215-296
    • Muñoz, V.1    Serrano, L.2
  • 46
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of β-hairpin formation
    • Muñoz V, Thomson PA, Hofrichter J, Eaton WA. 1997. Folding dynamics and mechanism of β-hairpin formation. Nature 390:196-199.
    • (1997) Nature , vol.390 , pp. 196-199
    • Muñoz, V.1    Thomson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 47
    • 0030342726 scopus 로고    scopus 로고
    • An NMR study on the β-hairpin region of barnase
    • Neira JL, Fersht AR. 1996. An NMR study on the β-hairpin region of barnase. Folding Design 1:231-241.
    • (1996) Folding Design , vol.1 , pp. 231-241
    • Neira, J.L.1    Fersht, A.R.2
  • 48
    • 0030014956 scopus 로고    scopus 로고
    • Progress towards understanding β-sheet structure
    • Nesloney CL, Kelly JW. 1996a. Progress towards understanding β-sheet structure. Bioorg Med Chem 4:739-766.
    • (1996) Bioorg Med Chem , vol.4 , pp. 739-766
    • Nesloney, C.L.1    Kelly, J.W.2
  • 49
    • 0000375517 scopus 로고    scopus 로고
    • Synthesis and hydrogen bonding capabilities of hiphenyl-based amino acids designed to nucleate β-sheet structure
    • Nesloney CL, Kelly JW. 1996b. Synthesis and hydrogen bonding capabilities of hiphenyl-based amino acids designed to nucleate β-sheet structure. J Org Chem 61:3127-3137.
    • (1996) J Org Chem , vol.61 , pp. 3127-3137
    • Nesloney, C.L.1    Kelly, J.W.2
  • 50
    • 0028821194 scopus 로고
    • Thermodynamic genetics of the folding of the B1 immunoglobulin-binding domain from streptococcal protein G
    • O'Neil KT, Hoess RH, Raleigh DP, DeGrado WF. 1995. Thermodynamic genetics of the folding of the B1 immunoglobulin-binding domain from streptococcal protein G. Proteins Struct Funct Genet 21:11-21.
    • (1995) Proteins Struct Funct Genet , vol.21 , pp. 11-21
    • O'Neil, K.T.1    Hoess, R.H.2    Raleigh, D.P.3    Degrado, W.F.4
  • 51
    • 0028236501 scopus 로고
    • Hydrogen-deuterium exchange in the free and immunoglobulin G-bound protein G B-domain
    • Orban J, Alexander P, Bryan P. 1994. Hydrogen-deuterium exchange in the free and immunoglobulin G-bound protein G B-domain. Biochemistry 33:5702-5710.
    • (1994) Biochemistry , vol.33 , pp. 5702-5710
    • Orban, J.1    Alexander, P.2    Bryan, P.3
  • 52
    • 0028810974 scopus 로고
    • Assessment of stability differences in the protein G B1 and B2 domains from hydrogen-deuterium exchange: Comparison with calorimetric data
    • Orban J, Alexander P, Bryan P, Khare D. 1995. Assessment of stability differences in the protein G B1 and B2 domains from hydrogen-deuterium exchange: Comparison with calorimetric data. Biochemistry 34:15291-15300.
    • (1995) Biochemistry , vol.34 , pp. 15291-15300
    • Orban, J.1    Alexander, P.2    Bryan, P.3    Khare, D.4
  • 53
    • 0030664958 scopus 로고    scopus 로고
    • An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core
    • Park S, O'Neil KT, Roder H. 1997. An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like Core. Biochemistry 36:14277-14283.
    • (1997) Biochemistry , vol.36 , pp. 14277-14283
    • Park, S.1    O'Neil, K.T.2    Roder, H.3
  • 54
    • 0031574916 scopus 로고    scopus 로고
    • Non-native local interactions in protein folding and stability: Introducing a helical tendency in the all β-sheet α-spectrin SH3 domain
    • Prieto J, Wilmans M, Jiménez MA, Rico M, Serrano L. 1997. Non-native local interactions in protein folding and stability: Introducing a helical tendency in the all β-sheet α-spectrin SH3 domain. J Mol Biol 268:760-778.
    • (1997) J Mol Biol , vol.268 , pp. 760-778
    • Prieto, J.1    Wilmans, M.2    Jiménez, M.A.3    Rico, M.4    Serrano, L.5
  • 55
    • 0033617266 scopus 로고    scopus 로고
    • From computer simulations to human disease: Emerging themes in protein
    • Radford SE, Dobson CM. 1999. From computer simulations to human disease: Emerging themes in protein. Cell 97:291-298.
    • (1999) Cell , vol.97 , pp. 291-298
    • Radford, S.E.1    Dobson, C.M.2
  • 56
    • 0031558811 scopus 로고    scopus 로고
    • Role of β-turn residues in β-hairpin formation and stability in designed peptides
    • Ramírez-Alvarado M, Blanco FJ, Niemann, H, Serrano L. 1997. Role of β-turn residues in β-hairpin formation and stability in designed peptides. J Mol Biol 273:898-912.
    • (1997) J Mol Biol , vol.273 , pp. 898-912
    • Ramírez-Alvarado, M.1    Blanco, F.J.2    Niemann, H.3    Serrano, L.4
  • 57
    • 0031181666 scopus 로고    scopus 로고
    • Protein folding and the paracelsus challenge
    • Rose GD. 1997. Protein folding and the Paracelsus challenge. Nat Struct Biol 4:512-514.
    • (1997) Nat Struct Biol , vol.4 , pp. 512-514
    • Rose, G.D.1
  • 58
    • 0043122630 scopus 로고    scopus 로고
    • Use of a designed triple-stranded antiparallel β-sheet to probe β-sheet cooperativety in aqueous solution
    • Schenck HL, Gellman SH. 1998. Use of a designed triple-stranded antiparallel β-sheet to probe β-sheet cooperativety in aqueous solution. J Am Chem Soc 120:4869-4870.
    • (1998) J Am Chem Soc , vol.120 , pp. 4869-4870
    • Schenck, H.L.1    Gellman, S.H.2
  • 59
    • 0032568924 scopus 로고    scopus 로고
    • Expressed protein ligation, a novel method for studying protein-protein interactions in transcription
    • Severinov K, Muir TW. 1998. Expressed protein ligation, a novel method for studying protein-protein interactions in transcription. J Biol Chem 273:16205-16209.
    • (1998) J Biol Chem , vol.273 , pp. 16205-16209
    • Severinov, K.1    Muir, T.W.2
  • 60
    • 0030982583 scopus 로고    scopus 로고
    • A molecular dynamics simulation study of segment B1 of protein G
    • Sheinerman FB, Brooks CL III. 1997. A molecular dynamics simulation study of segment B1 of protein G. Proteins Struct Funct Genet 29:193-202.
    • (1997) Proteins Struct Funct Genet , vol.29 , pp. 193-202
    • Sheinerman, F.B.1    Brooks C.L. III2
  • 61
    • 0032539561 scopus 로고    scopus 로고
    • Molecular picture of folding of a small α/β protein
    • Sheinerman FB, Brooks CL III. 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 C.L. III2
  • 62
    • 0011034289 scopus 로고
    • Hydrophobic cluster formation is necessary for dibenzofuran-based amino acids to function as β-sheeet nucleators
    • Tsang KY, Diaz H, Graciani N, Kelly JW. 1994. Hydrophobic cluster formation is necessary for dibenzofuran-based amino acids to function as β-sheeet nucleators. J Am Chem Soc 116:3988-4005.
    • (1994) J Am Chem Soc , vol.116 , pp. 3988-4005
    • Tsang, K.Y.1    Diaz, H.2    Graciani, N.3    Kelly, J.W.4
  • 63
    • 0030623698 scopus 로고    scopus 로고
    • Favourable native-like helical local interactions can accelerate protein folding
    • Viguera AR, Villegas V, Avilés FX, Serrano L. 1996. Favourable native-like helical local interactions can accelerate protein folding. Folding Design 2:23-33.
    • (1996) Folding Design , vol.2 , pp. 23-33
    • Viguera, A.R.1    Villegas, V.2    Avilés, F.X.3    Serrano, L.4
  • 64
    • 0030334742 scopus 로고
    • Stabilization of proteins by rational design of α-helix stability using helix/coil transition theory
    • Villegas V, Viguera AR, Avilés FX, Serrano L. 1995. Stabilization of proteins by rational design of α-helix stability using helix/coil transition theory. Folding Design 1:29-34.
    • (1995) Folding Design , vol.1 , pp. 29-34
    • Villegas, V.1    Viguera, A.R.2    Avilés, F.X.3    Serrano, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.