메뉴 건너뛰기




Volumn 279, Issue 5, 1998, Pages 1163-1175

Exploring the folding pathways of annexin I, a multidomain protein. I. Non-native structures stabilize the partially folded state of the isolated domain 2 of annexin I

Author keywords

Annexin; NMR; Non native structures; Protein folding; Stability

Indexed keywords

LIPOCORTIN 1;

EID: 0032568860     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1829     Document Type: Article
Times cited : (19)

References (57)
  • 1
    • 0027536094 scopus 로고
    • Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: A two-dimensional NMR study
    • Alexandrescu A.T., Evans P.A., Pitkeathly M., Baum J., Dobson C.M. Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin a two-dimensional NMR study. Biochemistry. 32:1993;1707-1718
    • (1993) Biochemistry , vol.32 , pp. 1707-1718
    • Alexandrescu, A.T.1    Evans, P.A.2    Pitkeathly, M.3    Baum, J.4    Dobson, C.M.5
  • 2
    • 0028274250 scopus 로고
    • Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: A heteronuclear NMR study
    • Alexandrescu A.T., Abeygunawardana C., Shortle D. Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease a heteronuclear NMR study. Biochemistry. 33:1994;1063-1072
    • (1994) Biochemistry , vol.33 , pp. 1063-1072
    • Alexandrescu, A.T.1    Abeygunawardana, C.2    Shortle, D.3
  • 3
    • 0029249945 scopus 로고
    • The nature of protein folding pathways: The classical versus the new view
    • Baldwin R.L. The nature of protein folding pathways the classical versus the new view. J. Biomol. NMR. 5:1995;103-109
    • (1995) J. Biomol. NMR , vol.5 , pp. 103-109
    • Baldwin, R.L.1
  • 4
    • 5144233105 scopus 로고
    • MLEV-17-based two dimensional homonuclear magnetisation transfer spectroscopy
    • Bax A., Davis D.G. MLEV-17-based two dimensional homonuclear magnetisation transfer spectroscopy. J. Mag. Res. 65:1985;355-360
    • (1985) J. Mag. Res. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 5
    • 0000284431 scopus 로고
    • Hetero-TOCSY experiments with WALTZ and DIPSI mixing sequences
    • Brown L.R., Sanctuary B.C. Hetero-TOCSY experiments with WALTZ and DIPSI mixing sequences. J. Mag. Res. 91:1991;413-421
    • (1991) J. Mag. Res. , vol.91 , pp. 413-421
    • Brown, L.R.1    Sanctuary, B.C.2
  • 6
    • 0028899526 scopus 로고
    • A computer program to determine a protein sequence from an amino acid analysis
    • Cordier-Ochsenbein F., Cordier S., Russo-Marie F. A computer program to determine a protein sequence from an amino acid analysis. Bio/Technology. 13:1995;276-278
    • (1995) Bio/Technology , vol.13 , pp. 276-278
    • Cordier-Ochsenbein, F.1    Cordier, S.2    Russo-Marie, F.3
  • 8
    • 0032569033 scopus 로고    scopus 로고
    • Exploring the folding pathways of annexin I, a multidomain protein. II. Hierarchy in domain folding propensities may govern the folding process
    • Cordier-Ochsenbein F., Guerois R., Russo-Marie F., Neumann J.-M., Sanson A. Exploring the folding pathways of annexin I, a multidomain protein. II. Hierarchy in domain folding propensities may govern the folding process. J. Mol. Biol. 279:1998;1177-1185
    • (1998) J. Mol. Biol. , vol.279 , pp. 1177-1185
    • Cordier-Ochsenbein, F.1    Guerois, R.2    Russo-Marie, F.3    Neumann, J.-M.4    Sanson, A.5
  • 9
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill K.A., Chan H.S. From Levinthal to pathways to funnels. Nature Struct. Biol. 4:1997;10-19
    • (1997) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 10
    • 0026768829 scopus 로고
    • Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin
    • Dyson H.J., Merutka G., Waltho J.P., Lerner R.A., Wright P.E. Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin. J. Mol. Biol. 226:1992;795-817
    • (1992) J. Mol. Biol. , vol.226 , pp. 795-817
    • Dyson, H.J.1    Merutka, G.2    Waltho, J.P.3    Lerner, R.A.4    Wright, P.E.5
  • 11
    • 0030047497 scopus 로고    scopus 로고
    • The high-resolution crystal structure of human annexin III shows subtle differences with annexin V
    • Favier-Perron B., Lewit-Bentley A., Russo-Marie F. The high-resolution crystal structure of human annexin III shows subtle differences with annexin V. Biochemistry. 35:1996;1740-1744
    • (1996) Biochemistry , vol.35 , pp. 1740-1744
    • Favier-Perron, B.1    Lewit-Bentley, A.2    Russo-Marie, F.3
  • 12
    • 0029157429 scopus 로고
    • Compact intermediate states in protein folding
    • Fink A.L. Compact intermediate states in protein folding. Annu. Rev. Biophys. Biomol. Struct. 24:1995;495-522
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 495-522
    • Fink, A.L.1
  • 13
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implication of simple methods for predicting the secondary structure of globular proteins
    • Garnier J., Osguthorpe D.J., Robson B. Analysis of the accuracy and implication of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 120:1978;97-120
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 14
    • 0024972036 scopus 로고
    • A powerful method of sequential proton resonance assignment in proteins using relayed 15N-1H multiple quantum coherence spectroscopy
    • 93-88
    • Gronenborn A.M., Bax A., Wingfield P.T., Clore G.M. A powerful method of sequential proton resonance assignment in proteins using relayed 15N-1H multiple quantum coherence spectroscopy. FEBS Letters. 243:1989;. 93-88
    • (1989) FEBS Letters , vol.243
    • Gronenborn, A.M.1    Bax, A.2    Wingfield, P.T.3    Clore, G.M.4
  • 15
    • 0027787894 scopus 로고
    • 2O in protein NMR. Application to sensitivity enhancement and NOE measurements
    • 2O in protein NMR. Application to sensitivity enhancement and NOE measurements. J. Am. Chem. Soc. 115:1993;12593-12594
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12593-12594
    • Grzesiek, S.1    Bax, A.2
  • 16
    • 0029740071 scopus 로고    scopus 로고
    • Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein
    • Hamada D., Segawa S., Goto Y. Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein. Nature Struct. Biol. 3:1996;868-873
    • (1996) Nature Struct. Biol. , vol.3 , pp. 868-873
    • Hamada, D.1    Segawa, S.2    Goto, Y.3
  • 17
    • 0028336661 scopus 로고
    • Modeling studies of the change in conformation required for cleavage of limited proteolytic sites
    • Hubbard S.J., Eisenmenger F., Thornton J.M. Modeling studies of the change in conformation required for cleavage of limited proteolytic sites. Protein Sci. 3:1994;757-768
    • (1994) Protein Sci. , vol.3 , pp. 757-768
    • Hubbard, S.J.1    Eisenmenger, F.2    Thornton, J.M.3
  • 18
    • 0026575572 scopus 로고
    • Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins
    • Huber R., Berendes R., Burger A., Schneider M., Karshikov A., Luecke H., Romisch J., Paques E. Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins. J. Mol. Biol. 223:1992;683-704
    • (1992) J. Mol. Biol. , vol.223 , pp. 683-704
    • Huber, R.1    Berendes, R.2    Burger, A.3    Schneider, M.4    Karshikov, A.5    Luecke, H.6    Romisch, J.7    Paques, E.8
  • 19
    • 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. 254:1995;260-288
    • (1995) J. Mol. Biol. , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 20
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings P.A., Wright P.E. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science. 262:1993;892-896
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 21
    • 0027339794 scopus 로고
    • CD and 1H-NMR studies on the conformational properties of peptide fragments from the C-terminal domain of thermolysin
    • Jimenez M.A., Bruix M., Gonzalez C., Blanco F.J., Nieto J.L., Herranz J., Rico M. CD and 1H-NMR studies on the conformational properties of peptide fragments from the C-terminal domain of thermolysin. Eur. J. Biochem. 211:1993;569-581
    • (1993) Eur. J. Biochem. , vol.211 , pp. 569-581
    • Jimenez, M.A.1    Bruix, M.2    Gonzalez, C.3    Blanco, F.J.4    Nieto, J.L.5    Herranz, J.6    Rico, M.7
  • 22
    • 0028327236 scopus 로고
    • Protein folding dynamics: The diffusion-collision model and experimental data
    • Karplus M., Weaver D.L. Protein folding dynamics the diffusion-collision model and experimental data. Protein Sci. 3:1994;650-668
    • (1994) Protein Sci. , vol.3 , pp. 650-668
    • Karplus, M.1    Weaver, D.L.2
  • 23
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 24
    • 0002532387 scopus 로고
    • Sensitivity enhanced two dimensional heteronuclear relayed coherence transfer NMR spectroscopy
    • Lerner L., Bax A. Sensitivity enhanced two dimensional heteronuclear relayed coherence transfer NMR spectroscopy. J. Magn. Reson. 69:1986;375-385
    • (1986) J. Magn. Reson. , vol.69 , pp. 375-385
    • Lerner, L.1    Bax, A.2
  • 25
    • 0031588693 scopus 로고    scopus 로고
    • Folding kinetics of Che Y mutants with enhanced native alpha-helix propensities
    • Lopez-Hernandez E., Cronet P., Serrano L., Munoz V. Folding kinetics of Che Y mutants with enhanced native alpha-helix propensities. J. Mol. Biol. 266:1997;610-620
    • (1997) J. Mol. Biol. , vol.266 , pp. 610-620
    • Lopez-Hernandez, E.1    Cronet, P.2    Serrano, L.3    Munoz, V.4
  • 26
    • 0024329563 scopus 로고
    • Two-dimensional nuclear magnetic resonance spectroscopy of proteins: An overview
    • Markley J.L. Two-dimensional nuclear magnetic resonance spectroscopy of proteins an overview. Methods Enzymol. 176:1989;12-64
    • (1989) Methods Enzymol. , vol.176 , pp. 12-64
    • Markley, J.L.1
  • 27
    • 0026524680 scopus 로고
    • 2H exchange-nuclear magnetic resonance studies on the folding pathway of barnase: Complementarity to and agreement with protein engineering studies
    • 2H exchange-nuclear magnetic resonance studies on the folding pathway of barnase complementarity to and agreement with protein engineering studies. J. Mol. Biol. 224:1992;837-845
    • (1992) J. Mol. Biol. , vol.224 , pp. 837-845
    • Matouschek, A.1    Serrano, L.2    Meiering, E.M.3    Bycroft, M.4    Fersht, A.R.5
  • 28
    • 20744456789 scopus 로고
    • Solid phase synthesis. I. the synthesis of a tetrapeptide
    • Merrifield R.B. Solid phase synthesis. I. The synthesis of a tetrapeptide. J. Am. Chem. Soc. 85:1963;2149-2154
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 2149-2154
    • Merrifield, R.B.1
  • 29
    • 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. 5:1995;14-24
    • (1995) J. Biomol. NMR , vol.5 , pp. 14-24
    • Merutka, G.1    Dyson, H.J.2    Wright, P.E.3
  • 30
    • 0027770910 scopus 로고
    • Detection of transient protein folding populations by mass spectrometry
    • Miranker A., Robinson C.V., Radford S.E., Aplin R.T., Dobson C.M. Detection of transient protein folding populations by mass spectrometry. Science. 262:1993;896-900
    • (1993) Science , vol.262 , pp. 896-900
    • Miranker, A.1    Robinson, C.V.2    Radford, S.E.3    Aplin, R.T.4    Dobson, C.M.5
  • 31
    • 0028820642 scopus 로고
    • Molecular phylogeny of annexins and identification of a primitive homologue in Giardia lamblia
    • Morgan R.O., Fernandez M.P. Molecular phylogeny of annexins and identification of a primitive homologue in Giardia lamblia. Mol. Biol. Evol. 12:1995;967-979
    • (1995) Mol. Biol. Evol. , vol.12 , pp. 967-979
    • Morgan, R.O.1    Fernandez, M.P.2
  • 33
    • 0028447768 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters
    • Munoz V., Serrano L. Elucidating the folding problem of helical peptides using empirical parameters. Nature Struct. Biol. 1:1994;399-409
    • (1994) Nature Struct. Biol. , vol.1 , pp. 399-409
    • Munoz, V.1    Serrano, L.2
  • 34
    • 0028873081 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides
    • Munoz V., Serrano L. Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides. J. Mol. Biol. 245:1995;275-296
    • (1995) J. Mol. Biol. , vol.245 , pp. 275-296
    • Munoz, V.1    Serrano, L.2
  • 35
    • 0028834210 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence
    • Munoz V., Serrano L. Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence. J. Mol. Biol. 245:1995;297-308
    • (1995) J. Mol. Biol. , vol.245 , pp. 297-308
    • Munoz, V.1    Serrano, L.2
  • 36
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms
    • Munoz V., Serrano L. Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation comparison with Zimm-Bragg and Lifson-Roig formalisms. Biopolymers. 41:1997;495-509
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Munoz, V.1    Serrano, L.2
  • 37
    • 0028871617 scopus 로고
    • Nonnative capping structure initiates helix folding in an annexin I fragment. a H-1 NMR conformational study
    • Odaert B., Baleux F., Huynhdinh T., Neumann J.M., Sanson A. Nonnative capping structure initiates helix folding in an annexin I fragment. A H-1 NMR conformational study. Biochemistry. 34:1995;12820-12829
    • (1995) Biochemistry , vol.34 , pp. 12820-12829
    • Odaert, B.1    Baleux, F.2    Huynhdinh, T.3    Neumann, J.M.4    Sanson, A.5
  • 38
    • 0028805413 scopus 로고
    • Extensive nonrandom structure in reduced and unfolded bovine pancreatic trypsin inhibitor
    • Pan H., Barbar E., Barany G., Woodward C. Extensive nonrandom structure in reduced and unfolded bovine pancreatic trypsin inhibitor. Biochemistry. 34:1995;13974-13981
    • (1995) Biochemistry , vol.34 , pp. 13974-13981
    • Pan, H.1    Barbar, E.2    Barany, G.3    Woodward, C.4
  • 39
    • 0027981501 scopus 로고
    • Conformational properties of four peptides corresponding to alpha-helical regions of Rhodospirillum cytochrome c2 and bovine calcium binding protein
    • Pintar A., Chollet A., Bradshaw C., Chaffotte A., Cadieux C., Rooman M.J., Hallenga K., Knowles J., Goldberg M., Wodak S.J. Conformational properties of four peptides corresponding to alpha-helical regions of Rhodospirillum cytochrome c2 and bovine calcium binding protein. Biochemistry. 33:1994;11158-11173
    • (1994) Biochemistry , vol.33 , pp. 11158-11173
    • Pintar, A.1    Chollet, A.2    Bradshaw, C.3    Chaffotte, A.4    Cadieux, C.5    Rooman, M.J.6    Hallenga, K.7    Knowles, J.8    Goldberg, M.9    Wodak, S.J.10
  • 40
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M., Saudek V., Sklenar V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR. 2:1992;661-665
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 41
    • 33845555707 scopus 로고
    • Exchangeable proton NMR without base-line distortion, using new strong-pulse sequence
    • Plateau P., Guéron M. Exchangeable proton NMR without base-line distortion, using new strong-pulse sequence. J. Am. Chem. Soc. 104:1982;7310-7311
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 7310-7311
    • Plateau, P.1    Guéron, M.2
  • 42
    • 0028917296 scopus 로고
    • Structures of folding intermediates
    • Ptitsyn O.B. Structures of folding intermediates. Curr. Opin. Struct. Biol. 5:1995;74-78
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 74-78
    • Ptitsyn, O.B.1
  • 43
    • 0028324464 scopus 로고
    • Annexins: The problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins
    • Raynal P., Pollard H.B. Annexins the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins. Biochim. Biophys. Acta. 1197:1994;63-93
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 44
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • Roder H., Colon W. Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol. 7:1997;15-28
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 15-28
    • Roder, H.1    Colon, W.2
  • 45
    • 0025326950 scopus 로고
    • Relations between protein sequence and structure and their significance
    • Rooman M.J., Rodriguez J., Wodak S.J. Relations between protein sequence and structure and their significance. J. Mol. Biol. 213:1990;337-350
    • (1990) J. Mol. Biol. , vol.213 , pp. 337-350
    • Rooman, M.J.1    Rodriguez, J.2    Wodak, S.J.3
  • 46
    • 0026009212 scopus 로고
    • Prediction of protein backbone conformation based on seven structure assignments. Influence of local interactions
    • Rooman M.J., Kocher J.P., Wodak S.J. Prediction of protein backbone conformation based on seven structure assignments. Influence of local interactions. J. Mol. Biol. 221:1991;961-979
    • (1991) J. Mol. Biol. , vol.221 , pp. 961-979
    • Rooman, M.J.1    Kocher, J.P.2    Wodak, S.J.3
  • 47
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost B., Sander C. Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232:1993;584-599
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 48
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost B., Sander C. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins: Struct. Funct. Genet. 19:1994;55-72
    • (1994) Proteins: Struct. Funct. Genet. , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 49
    • 0030759665 scopus 로고    scopus 로고
    • Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea
    • Schwalbe H., Fiebig K.M., Buck M., Jones J.A., Grimshaw S.B., Spencer A., Glaser S.J., Smith L.J., Dobson C.M. Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea. Biochemistry. 36:1997;8977-8991
    • (1997) Biochemistry , vol.36 , pp. 8977-8991
    • Schwalbe, H.1    Fiebig, K.M.2    Buck, M.3    Jones, J.A.4    Grimshaw, S.B.5    Spencer, A.6    Glaser, S.J.7    Smith, L.J.8    Dobson, C.M.9
  • 50
    • 0029961647 scopus 로고    scopus 로고
    • Structural analysis of non native states of proteins by NMR methods
    • Shortle D.R. Structural analysis of non native states of proteins by NMR methods. Curr. Opin. Struct. Biol. 6:1996;24-30
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 24-30
    • Shortle, D.R.1
  • 51
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase
    • Smith D.B., Johnson K.S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase. Gene. 67:1988;31-40
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 52
    • 0030320442 scopus 로고    scopus 로고
    • The concept of a random coil. Residual structure in peptides and denatured proteins
    • Smith L.J., Fiebig K.M., Schwalbe H., Dobson C.M. The concept of a random coil. Residual structure in peptides and denatured proteins. Fold. Des. 1:1996;R95-R106
    • (1996) Fold. Des. , vol.1
    • Smith, L.J.1    Fiebig, K.M.2    Schwalbe, H.3    Dobson, C.M.4
  • 53
    • 13344276445 scopus 로고
    • SN2 deprotection of synthetic peptides with a low concentration of HF in dimethylsulfoxide: Evidence and application in peptide synthesis
    • Tam J.P., Heath W.F. SN2 deprotection of synthetic peptides with a low concentration of HF in dimethylsulfoxide evidence and application in peptide synthesis. J. Am. Chem. Soc. 105:1983;6442-6447
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 6442-6447
    • Tam, J.P.1    Heath, W.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.