메뉴 건너뛰기




Volumn 5, Issue 8, 1998, Pages 721-729

Obligatory steps in protein folding and the conformational diversity of the transition state

Author keywords

[No Author keywords available]

Indexed keywords

FODRIN; MUTANT PROTEIN; PROTEIN TYROSINE KINASE;

EID: 0031825181     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/1418     Document Type: Article
Times cited : (246)

References (57)
  • 1
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
    • Jackson, S.E. & Fersht, A.R. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition. Biochemistry 30, 10428–10435 (1991).
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 2
    • 0026782853 scopus 로고
    • Kinetic analysis of folding and unfolding of the 56 amino acid IgG-binding domain of Streptococcal protein G
    • Alexander, P., Orban, J. & Bryan, P. Kinetic analysis of folding and unfolding of the 56 amino acid IgG-binding domain of Streptococcal protein G. Biochemistry 31, 7243–7248 (1992).
    • (1992) Biochemistry , vol.31 , pp. 7243-7248
    • Alexander, P.1    Orban, J.2    Bryan, P.3
  • 4
    • 0028331876 scopus 로고
    • Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a twostate folding transition
    • Viguera, A.R., Martinez, J.C., Filimonov, V.V., Mateo, P.L. & Serrano, L. Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a twostate folding transition. Biochemistry 33, 2142–2150 (1994).
    • (1994) Biochemistry , vol.33 , pp. 2142-2150
    • Viguera, A.R.1    Martinez, J.C.2    Filimonov, V.V.3    Mateo, P.L.4    Serrano, L.5
  • 6
    • 0029151158 scopus 로고
    • Submillisecond folding of monomeric lrepressor
    • Huang, G.S. & Oas, T.G. Submillisecond folding of monomeric l repressor. Proc. Natl. Acad. Sci. USA 92, 6878–6882 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6878-6882
    • Huang, G.S.1    Oas, T.G.2
  • 7
    • 0028788480 scopus 로고
    • Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2
    • Villegas, V. et al. Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2. Biochemistry 34, 15105–15110 (1995).
    • (1995) Biochemistry , vol.34 , pp. 15105-15110
    • Villegas, V.1
  • 8
    • 0029965111 scopus 로고
    • Fast and one-step folding of closely and distantly related homologous proteins of a four-helix bundle family
    • Kragelund, B.B., Robinson, C.V., Knudesn, J., Dobson, C.M. & Poulsen, F.M. Fast and one-step folding of closely and distantly related homologous proteins of a four-helix bundle family. J. Mol. Biol. 256, 187–200 (1995).
    • (1995) J. Mol. Biol. , vol.256 , pp. 187-200
    • Kragelund, B.B.1    Robinson, C.V.2    Knudesn, J.3    Dobson, C.M.4    Poulsen, F.M.5
  • 9
    • 0032570265 scopus 로고    scopus 로고
    • Structure and stability of the N-terminal domain of the ribosomal protein L9: Evidence for rapid two-state folding
    • Kuhlman, B., Boice, J.A., Fairman, R. & Raleigh, D.P. Structure and stability of the N-terminal domain of the ribosomal protein L9: evidence for rapid two-state folding. Biochemistry 37, 1025–1032 (1998).
    • (1998) Biochemistry , vol.37 , pp. 1025-1032
    • Kuhlman, B.1    Boice, J.A.2    Fairman, R.3    Raleigh, D.P.4
  • 10
    • 0032562182 scopus 로고    scopus 로고
    • The folding kinetics and thermodynamics of the Fyn-SH3 domain
    • Plaxco, K.W. et al. The folding kinetics and thermodynamics of the Fyn-SH3 domain. Biochemistry 37, 2529–2537 (1998).
    • (1998) Biochemistry , vol.37 , pp. 2529-2537
    • Plaxco, K.W.1
  • 11
    • 0029763434 scopus 로고    scopus 로고
    • Rapid refolding of a proline-rich all beta-sheet fibronectin type III module
    • Plaxco, K.W., Spitzfaden, C., Campbell, I.D. & Dobson, C.M. Rapid refolding of a proline-rich all beta-sheet fibronectin type III module. Proc. Natl. Acad. Sci. USA 93, 10703–10706 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10703-10706
    • Plaxco, K.W.1    Spitzfaden, C.2    Campbell, I.D.3    Dobson, C.M.4
  • 12
    • 0028958601 scopus 로고
    • Characterizing transition states in protein folding: An essential step in the puzzle
    • Fersht, A.R. Characterizing transition states in protein folding: an essential step in the puzzle. Curr. Opin. Struct. Biol. 5, 79–84 (1995).
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 79-84
    • Fersht, A.R.1
  • 13
    • 0002682169 scopus 로고    scopus 로고
    • Local vs non-local interactions in protein folding and stability. An experimentalist point of view
    • Munoz, V. & Serrano, L. Local vs non-local interactions in protein folding and stability. An experimentalist point of view. Folding & Design 1, R71–R77. (1996).
    • (1996) Folding & Design , vol.1
    • Munoz, V.1    Serrano, L.2
  • 14
    • 1842298212 scopus 로고    scopus 로고
    • From levinthal to pathways to funnels
    • Dill, K.A. & Sun Chan, H. From levinthal to pathways to funnels. Nature Struct. Biol. 4, 10–19 (1998).
    • (1998) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Sun Chan, H.2
  • 16
    • 0030334834 scopus 로고    scopus 로고
    • Structure of the transition state for folding of the 129aa protein, CheY, resembles that of a smaller protein, CI-2
    • Lopez-Hernandez, E. & Serrano, L. Structure of the transition state for folding of the 129aa protein, CheY, resembles that of a smaller protein, CI-2. Folding & Design 1, 43–55 (1996).
    • (1996) Folding & Design , vol.1 , pp. 43-55
    • Lopez-Hernandez, E.1    Serrano, L.2
  • 17
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
    • Itzhaki, L.S., Otzen, D.E. & Fersht, A.R. The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding. J. Mol. Biol. 254, 260–288 (1995).
    • (1995) J. Mol. Biol. , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 18
    • 0029760326 scopus 로고    scopus 로고
    • Different folding transition states could result in the some native structure
    • Viguera, A.R. Wilmanns, M. & Serrano, L. Different folding transition states could result in the some native structure. Nature Struct. Biol. 3, 874–880 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 874-880
    • Viguera, A.R.1    Wilmanns, M.2    Serrano, L.3
  • 19
    • 0028024928 scopus 로고
    • Specific nucleus as the transition state for protein folding: Evidence from the lattice model
    • Abkevich, V.I., Gutin, A.M. and Shakhnovich, E.I. Specific nucleus as the transition state for protein folding: evidence from the lattice model. Biochemistry 33, 10026–10036 (1994)
    • (1994) Biochemistry , vol.33 , pp. 10026-10036
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 20
    • 0026437577 scopus 로고
    • M. E. M, Pautit, R. Wierenga, R. & Saraste, M. Crystal structure of a src-homology 3 (SH3) domain
    • Musacchio, A., M. E. M. Noble, M. E. M, Pautit, R. Wierenga, R. & Saraste, M. Crystal structure of a src-homology 3 (SH3) domain. Nature 359, 851–855 (1992).
    • (1992) Nature , vol.359 , pp. 851-855
    • Musacchio, A.1    Noble, M.E.M.2
  • 21
    • 0031160370 scopus 로고    scopus 로고
    • 1H and 15N-NMR assignment and solution structure of the SH3 domain of spectrin. Comparison with the crystal structure
    • Blanco, F.J., Ortiz, A.R. & Serrano, L. 1H and 15N-NMR assignment and solution structure of the SH3 domain of spectrin. Comparison with the crystal structure. J. Biomol. NMR. 9, 347–357 (1997).
    • (1997) J. Biomol. NMR. , vol.9 , pp. 347-357
    • Blanco, F.J.1    Ortiz, A.R.2    Serrano, L.3
  • 22
    • 0028932770 scopus 로고
    • The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics
    • Viguera, A.R., Blanco, F.J. & Serrano, L. The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics. J. Mol. Biol. 247, 670–681 (1995).
    • (1995) J. Mol. Biol. , vol.247 , pp. 670-681
    • Viguera, A.R.1    Blanco, F.J.2    Serrano, L.3
  • 23
    • 0030663205 scopus 로고    scopus 로고
    • Loop length, intramolecular diffusion and protein folding
    • Viguera, A.R. & Serrano, L. Loop length, intramolecular diffusion and protein folding. Nature Struct. Biol. 4, 939–946 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 939-946
    • Viguera, A.R.1    Serrano, L.2
  • 24
    • 0031890195 scopus 로고    scopus 로고
    • Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins
    • Perl, D. et al. Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nature Struct. Biol. 5, 229–235 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 229-235
    • Perl, D.1
  • 25
    • 0031558811 scopus 로고    scopus 로고
    • Role of b-turns residues in ß-hairpin formation and stability in designed peptides
    • Ramirez-Alvarado, M., Blanco, F.J., Niemann, H. & Serrano, L. Role of b-turns residues in ß-hairpin formation and stability in designed peptides. J. Mol. Biol. 273, 898–912 (1997).
    • (1997) J. Mol. Biol. , vol.273 , pp. 898-912
    • Ramirez-Alvarado, M.1    Blanco, F.J.2    Niemann, H.3    Serrano, L.4
  • 26
    • 0027265713 scopus 로고
    • The role of turns in the structure of an a-helical protein
    • Brunet, A.P. et al. The role of turns in the structure of an a-helical protein. Nature 363, 355–358 (1993).
    • (1993) Nature , vol.363 , pp. 355-358
    • Brunet, A.P.1
  • 27
    • 0028284549 scopus 로고
    • Linking an easily detectable phenotype to the folding of a common structural motif. Selection of rare mutations that prevent the folding of Rop
    • Castagnoli, L., Vetriani, C. & Cesareni, C. Linking an easily detectable phenotype to the folding of a common structural motif. Selection of rare mutations that prevent the folding of Rop. J. Mol. Biol. 234, 378–387 (1994).
    • (1994) J. Mol. Biol. , vol.234 , pp. 378-387
    • Castagnoli, L.1    Vetriani, C.2    Cesareni, C.3
  • 28
    • 0029877554 scopus 로고    scopus 로고
    • Sequence replacements in the central b-turn of plastocyanin
    • Ybe, J.A. & Hecht, M.H. Sequence replacements in the central b-turn of plastocyanin. Prot. Sci. 5, 814–824 (1996).
    • (1996) Prot. Sci. , vol.5 , pp. 814-824
    • Ybe, J.A.1    Hecht, M.H.2
  • 29
    • 0028174179 scopus 로고
    • Engineering alternative b-turn types in Staphylococcal nuclease
    • Hynes, T.R., Hodel, A. & Fox, R.O. Engineering alternative b-turn types in Staphylococcal nuclease. Biochemistry 33, 5021–5030 (1994).
    • (1994) Biochemistry , vol.33 , pp. 5021-5030
    • Hynes, T.R.1    Hodel, A.2    Fox, R.O.3
  • 30
    • 0030062459 scopus 로고    scopus 로고
    • Amino acid substitutions in a surface turn modulate protein stability
    • Predki, P.F., Agrawal, V., Brunger, A.T. & Regan, L. Amino acid substitutions in a surface turn modulate protein stability. Nature Struct. Biol. 3, 54–58 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 54-58
    • Predki, P.F.1    Agrawal, V.2    Brunger, A.T.3    Regan, L.4
  • 31
    • 0029926618 scopus 로고    scopus 로고
    • In vitro evolution of thermodynamically stable turns
    • Zhou, H.X., Hoess, R.H. & deGrado, W.F. In vitro evolution of thermodynamically stable turns. Nature Struct. Biol. 3, 446–451 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 446-451
    • Zhou, H.X.1    Hoess, R.H.2    Degrado, W.F.3
  • 32
    • 0031022599 scopus 로고    scopus 로고
    • ß-turn propensities as paradigms for the analysis of structural motifs to engineer protein stability
    • Ohage, E.C., Grami, W., Walter, M.M., Steinbacher, S. & Steipe, B. ß-turn propensities as paradigms for the analysis of structural motifs to engineer protein stability. Prot. Sci. 6, 233–241 (1997).
    • (1997) Prot. Sci. , vol.6 , pp. 233-241
    • Ohage, E.C.1    Grami, W.2    Walter, M.M.3    Steinbacher, S.4    Steipe, B.5
  • 33
    • 0031048642 scopus 로고    scopus 로고
    • Intestinal fatty acid binding protein: A specific residue in one turn appears to stabilize the native structure and be responsible for slow folding
    • Kim, K., Ramanathan, R. & Frieden, C. Intestinal fatty acid binding protein: a specific residue in one turn appears to stabilize the native structure and be responsible for slow folding. Prot. Sci. 6, 364–372 (1997).
    • (1997) Prot. Sci. , vol.6 , pp. 364-372
    • Kim, K.1    Ramanathan, R.2    Frieden, C.3
  • 34
    • 0031565981 scopus 로고    scopus 로고
    • Contrasting roles for symmetrically disposed beta-turns in the folding of a small protein
    • Gu H, Kim D, Baker D. Contrasting roles for symmetrically disposed beta-turns in the folding of a small protein. J. Mol. Biol. 274, 588–596 (1997).
    • (1997) J. Mol. Biol. , vol.274 , pp. 588-596
    • Gu, H.1    Kim, D.2    Baker, D.3
  • 35
    • 0031574916 scopus 로고    scopus 로고
    • Non-native interactions in protein folding and stability: Introducing a helical tendency in the all b-sheeta-spectrin SH3 domain
    • Prieto, J., Wilmanns, M., Jimenez, M.A., Rico, M. & Serrano, L. Non-native interactions in protein folding and stability: Introducing a helical tendency in the all b-sheet a-spectrin SH3 domain. J. Mol. Biol. 268, 760–778 (1997).
    • (1997) J. Mol. Biol. , vol.268 , pp. 760-778
    • Prieto, J.1    Wilmanns, M.2    Jimenez, M.A.3    Rico, M.4    Serrano, L.5
  • 36
    • 0028882589 scopus 로고
    • P22 Arc repressor: Transition state properties inferred from mutational effects on the rates of protein unfolding and efolding
    • Milla, M.E., Brown, B.M., Waldburger, C.D. & Sauer, R.T. P22 Arc repressor: transition state properties inferred from mutational effects on the rates of protein unfolding and efolding. Biochemistry 34, 13914–13919 (1995).
    • (1995) Biochemistry , vol.34 , pp. 13914-13919
    • Milla, M.E.1    Brown, B.M.2    Waldburger, C.D.3    Sauer, R.T.4
  • 37
    • 0028037217 scopus 로고
    • Single versus parallel pathways of protein folding and fractional formation of structure in the transition state
    • Fersht, A.R., Itzhaki, L.S., elMasry, N., Matthews, J.M. & Otzen, D.E. Single versus parallel pathways of protein folding and fractional formation of structure in the transition state. Proc. Natl. Acad. Sci. USA 91, 10426–10429 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10426-10429
    • Fersht, A.R.1    Itzhaki, L.S.2    Elmasry, N.3    Matthews, J.M.4    Otzen, D.E.5
  • 38
    • 0031853167 scopus 로고    scopus 로고
    • Important role of hydrogen bonds in the structurally polarized transition sate for folding of the src SH3 domain
    • Grantcharova, V.P., Riddle, D.S., Santiago, J.V. & Baker, D. Important role of hydrogen bonds in the structurally polarized transition sate for folding of the src SH3 domain. Nature Struct. Biol. 5, 714–720 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 714-720
    • Grantcharova, V.P.1    Riddle, D.S.2    Santiago, J.V.3    Baker, D.4
  • 40
    • 0029670994 scopus 로고    scopus 로고
    • Conserved residues and the mechanism of protein folding
    • Shakhnovich, E., Abkevich, V. & Ptitsyn, O. Conserved residues and the mechanism of protein folding. Nature 379, 96–98 (1996).
    • (1996) Nature , vol.379 , pp. 96-98
    • Shakhnovich, E.1    Abkevich, V.2    Ptitsyn, O.3
  • 41
    • 0032562182 scopus 로고    scopus 로고
    • The folding kinetics and thermodynamics of the Fyn-SH3 domain
    • Plaxco, K.W. et al. The folding kinetics and thermodynamics of the Fyn-SH3 domain. Biochemistry 37, 2529–2537 (1998).
    • (1998) Biochemistry , vol.37 , pp. 2529-2537
    • Plaxco, K.W.1
  • 43
    • 2642699794 scopus 로고
    • Rapid and efficient site-directed mutagenesis without phenotypic selection
    • Kunkel, T.A. Rapid and efficient site-directed mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82, 488–492 (1985).
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 44
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C. & von Hippel, P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319–326 (1989).
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 45
    • 84984758190 scopus 로고    scopus 로고
    • The HKL program suite. Unpublished programs
    • Otwinowski, Z. & Minor, W. The HKL program suite. Unpublished programs.
    • Otwinowski, Z.1    Minor, W.2
  • 46
    • 84920325457 scopus 로고
    • AMORE: An automated package for molecular replacement
    • Navaza, J. AMORE: An automated package for molecular replacement. Acta Crystallogr. A50, 157–163 (1994).
    • (1994) Acta Crystallogr , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 47
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110–119 (1991).
    • (1991) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 48
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brunger, A.T., Kuriyan, J. & Karplus, M. Crystallographic R factor refinement by molecular dynamics. Science 235, 458–460 (1987).
    • (1987) Science , vol.235 , pp. 458-460
    • Brunger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 49
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin, V.S. & Wilson, K.S. Automated refinement of protein models. Acta Crystallogr. A49, 129–147 (1993).
    • (1993) Acta Crystallogr , vol.A49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 50
    • 0021114895 scopus 로고
    • Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurement of proton-proton spin-spin coupling constants
    • Marion, D. & Wüthrich, K. Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurement of proton-proton spin-spin coupling constants. Biochem. Biophys. Res. Comm. 113, 967–974 (1983).
    • (1983) Biochem. Biophys. Res. Comm. , vol.113 , pp. 967-974
    • Marion, D.1    Wüthrich, K.2
  • 51
    • 0006393051 scopus 로고
    • Two dimensional spectroscopy. Application to nuclear magnetic resonance
    • Aue, W.P., Bartholdi, E. & Ernst, R.R. Two dimensional spectroscopy. Application to nuclear magnetic resonance. J. Chem. Phys. 64, 2229–2246 (1976).
    • (1976) J. Chem. Phys. , vol.64 , pp. 2229-2246
    • Aue, W.P.1    Bartholdi, E.2    Ernst, R.R.3
  • 52
    • 0005963761 scopus 로고
    • Multiple quantum filters for elucidating NMR coupling networks
    • Piantini, U., Sørensen, O. W., Ernst, R. R. Multiple quantum filters for elucidating NMR coupling networks. J. Amer. Chem. Soc. 104, 6800–6801 (1982).
    • (1982) J. Amer. Chem. Soc. , vol.104 , pp. 6800-6801
    • Piantini, U.1    Sørensen, O.W.2    Ernst, R.R.3
  • 53
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete protonproton cross-relaxation networks in biological macromolecules
    • Kumar, A., Ernst, R.R. & Wüthrich, K. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete protonproton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Comm. 95, 1–6 (1980)
    • (1980) Biochem. Biophys. Res. Comm. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 54
    • 5144233105 scopus 로고
    • MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A., & Davis, D. G. MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65, 355–360. (1985).
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 56
    • 0029061516 scopus 로고
    • Protein stability as a function of denaturant concentration: The thermal stability of barnase in the presence of urea
    • Johnson, C.M. & Fersht, A.R. Protein stability as a function of denaturant concentration: The thermal stability of barnase in the presence of urea. Biochemistry 34, 6795–6804 (1995).
    • (1995) Biochemistry , vol.34 , pp. 6795-6804
    • Johnson, C.M.1    Fersht, A.R.2
  • 57
    • 0029207339 scopus 로고
    • Random coil 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG
    • Merutka, G., Dyson, H.J. & Wright, P.E. Random coil 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG. J. Biomol. NMR 5, 14–24 (1995).
    • (1995) J. Biomol. NMR , vol.5 , pp. 14-24
    • Merutka, G.1    Dyson, H.J.2    Wright, P.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.