메뉴 건너뛰기




Volumn 3, Issue 4, 1997, Pages 299-313

Structural comparison in solution of a native and retro peptide derived from the third helix of Staphylococcus aureus protein A, domain B: Retro peptides, a useful tool for the discrimination of helix stabilization factors dependent on the peptide chain orientation

Author keywords

Helix; Macrodipole; NMR; Protein A; Retro enantio

Indexed keywords

STAPHYLOCOCCUS AUREUS;

EID: 0031181577     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1099-1387(199707)3:4<299::aid-psc121>3.0.co;2-b     Document Type: Review
Times cited : (14)

References (39)
  • 2
    • 0007247909 scopus 로고
    • Cycloenantiomerie und cyclodiastereomerie
    • V. Prelog and V. Gerlach (1964). Cycloenantiomerie und cyclodiastereomerie. Helv. Chim. Acta 47, 2288-2302.
    • (1964) Helv. Chim. Acta , vol.47 , pp. 2288-2302
    • Prelog, V.1    Gerlach, V.2
  • 3
    • 0028875452 scopus 로고
    • Recent developments in retro peptides and proteins-an ongoing topochemical exploration
    • M. Chorev and M. Goodman (1995). Recent developments in retro peptides and proteins-an ongoing topochemical exploration. Trends Biotchnol. 13, 438-445.
    • (1995) Trends Biotchnol. , vol.13 , pp. 438-445
    • Chorev, M.1    Goodman, M.2
  • 7
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic model of a human Fc fragment and its complex with fragment B of protein A from Staphyloooccus aureus at 2.9 and 2.8Å resolution
    • J. Deisenhofer (1981). Crystallographic refinement and atomic model of a human Fc fragment and its complex with fragment B of protein A from Staphyloooccus aureus at 2.9 and 2.8Å resolution. Biochemistry 20, 2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 8
    • 0026801084 scopus 로고
    • Three dimensional solution structure of the B domain of Staphyloccocus aureus protein A: Comparison of the solution and crystal structure
    • H. Gouda, H. Torigoe, A. Saito, M. Sato, Y. Arata and I. Shimana (1992). Three dimensional solution structure of the B domain of Staphyloccocus aureus protein A: Comparison of the solution and crystal structure. Biochemistry 31, 9665-9672.
    • (1992) Biochemistry , vol.31 , pp. 9665-9672
    • Gouda, H.1    Torigoe, H.2    Saito, A.3    Sato, M.4    Arata, Y.5    Shimana, I.6
  • 11
    • 5144233105 scopus 로고
    • MLEV-17 based two dimensional homonuclear magnetic transfer spectroscopy
    • A. Bax and D. G. Davis (1985). MLEV-17 based two dimensional homonuclear magnetic transfer spectroscopy. J. Magn. Res. 65, 355-360.
    • (1985) J. Magn. Res. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 12
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • J. Jeener, B. H. Meier, P. Bachman and R. R. Ernst (1979). Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71, 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachman, P.3    Ernst, R.R.4
  • 13
    • 0019327003 scopus 로고
    • A two dimensional nuclear overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross relaxation
    • A. Kumar, R. R. Ernst and K. Wüthrich (1980). A two dimensional nuclear overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross relaxation. Biochem. Biophys. Res. Commun. 95, 1-6.
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 14
    • 0011491177 scopus 로고
    • Structure determination of a tetrasaccharide: Transient nuclear Overhauser effects in the rotating frame
    • A. A. Brother-Ny, R. L. Stephens, J. M. Lee, C. D. Warren and R. W. Jeanloz (1984). Structure determination of a tetrasaccharide: transient nuclear Overhauser effects in the rotating frame. J. Am. Chem. Soc. 106, 811-613.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 811-1613
    • Brother-Ny, A.A.1    Stephens, R.L.2    Lee, J.M.3    Warren, C.D.4    Jeanloz, R.W.5
  • 15
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • M. Piorro, V. Saudek and V. Sklenár (1992). Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMRJ 2, 661-665.
    • (1992) J. Biomol. NMRJ , vol.2 , pp. 661-665
    • Piorro, M.1    Saudek, V.2    Sklenár, V.3
  • 17
    • 0026726004 scopus 로고
    • Effect of trifluoroethanol on protein secondary structure: An nmr and cd study using a synthetic actin peptide
    • F. D. Sönnichsen, J. E. V. Eyk, R. S. Hodges and B. D. Sykes (1992). Effect of trifluoroethanol on protein secondary structure: an nmr and cd study using a synthetic actin peptide. Biochemistry 31, 8790-8798.
    • (1992) Biochemistry , vol.31 , pp. 8790-8798
    • Sönnichsen, F.D.1    Eyk, J.E.V.2    Hodges, R.S.3    Sykes, B.D.4
  • 18
    • 0030567341 scopus 로고    scopus 로고
    • Mechanism of stabilization of helical conformations of polypeptides by water containing trifluoroethanol
    • A. Cammers-Goodwin, T. J. Allen, S. L. Oslick, K. F. McClure, J. H. Lee and D. S. Kemp (1996). Mechanism of stabilization of helical conformations of polypeptides by water containing trifluoroethanol. J. Am. Chem. Soc. 188, 3082-3090.
    • (1996) J. Am. Chem. Soc. , vol.188 , pp. 3082-3090
    • Cammers-Goodwin, A.1    Allen, T.J.2    Oslick, S.L.3    McClure, K.F.4    Lee, J.H.5    Kemp, D.S.6
  • 19
    • 0023785593 scopus 로고
    • Secondary structure of proteins through circular dichroism spectroscopy
    • W. C. Johnson (1988). Secondary structure of proteins through circular dichroism spectroscopy. Ann. Rev. Biophys. 17, 145-166.
    • (1988) Ann. Rev. Biophys. , vol.17 , pp. 145-166
    • Johnson, W.C.1
  • 20
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • J. T. Yand, C. -S. C. Wu and H. M. Martínez (1986). Calculation of protein conformation from circular dichroism. Methods Enzymol. 130, 208-269.
    • (1986) Methods Enzymol. , vol.130 , pp. 208-269
    • Yand, J.T.1    Wu, C.-S.C.2    Martínez, H.M.3
  • 21
    • 0024293204 scopus 로고
    • Conformation of peptide fragments of proteins in aqueous solution: Implications for initiation of protein folding
    • P. E. Wright, H. J. Dyson and R. A. Lernet (1988). Conformation of peptide fragments of proteins in aqueous solution: Implications for initiation of protein folding. Biochemistry 27, 7167-7175.
    • (1988) Biochemistry , vol.27 , pp. 7167-7175
    • Wright, P.E.1    Dyson, H.J.2    Lernet, R.A.3
  • 23
    • 0024278572 scopus 로고
    • Folding of immunogenic peptide fragments of proteins in water solution II: The nascent helix
    • H. J. Dyson, M. Rance, R. A. Houghten, R. A. Lerner and P. E. Wright (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    Lerner, R.A.4    Wright, P.E.5
  • 24
    • 0027180807 scopus 로고
    • Conformatlonal behaviour of Escherichia coli OmpA signal peptides in membrane mimetic environments
    • J. Rizo, F. J. Blanco, B. Kobe, M. Bruch and L. M. Gierasch (1993). Conformatlonal behaviour of Escherichia coli OmpA signal peptides in membrane mimetic environments. Biochemistry 32, 4881-4894.
    • (1993) Biochemistry , vol.32 , pp. 4881-4894
    • Rizo, J.1    Blanco, F.J.2    Kobe, B.3    Bruch, M.4    Gierasch, L.M.5
  • 25
    • 0028673594 scopus 로고
    • Chemical shifts as a tool for structure determination
    • D. S. Wishart and B. D. Sykes (1994). Chemical shifts as a tool for structure determination. Methods Enzymol. 239, 363-392.
    • (1994) Methods Enzymol. , vol.239 , pp. 363-392
    • Wishart, D.S.1    Sykes, B.D.2
  • 26
    • 0024278597 scopus 로고
    • Folding of immunogenic peptide fragments of proteins in water solution I. Sequence requirements for the formation of a reverse turn
    • H. J. Dyson, M. Rance, R. A. Houghton and P. E. Wright (1988). Folding of immunogenic peptide fragments of proteins in water solution I. Sequence requirements for the formation of a reverse turn. J. Mol. Biol. 226, 161-200.
    • (1988) J. Mol. Biol. , vol.226 , pp. 161-200
    • Dyson, H.J.1    Rance, M.2    Houghton, R.A.3    Wright, P.E.4
  • 27
    • 84985653913 scopus 로고
    • 1H-NMR titration shifts for studies of polypeptide conformation
    • 1H-NMR titration shifts for studies of polypeptide conformation. Biopolymers 18, 299-311.
    • (1979) Biopolymers , vol.18 , pp. 299-311
    • Buni, A.1    Wüthrich, K.2
  • 28
    • 33947300095 scopus 로고
    • Conformation of cyclic peptides III. Cyclopentaglycyltyrosyl and related compounds
    • K. D. Kopple, M. Ohnishi and A. Go (1969). Conformation of cyclic peptides III. Cyclopentaglycyltyrosyl and related compounds. J. Am. Chem. Soc. 91, 4264-4272.
    • (1969) J. Am. Chem. Soc. , vol.91 , pp. 4264-4272
    • Kopple, K.D.1    Ohnishi, M.2    Go, A.3
  • 29
    • 0014688629 scopus 로고
    • Temperature dependence of amide proton chemical shift: The secondary structures of gramicidin S and Valinomycln
    • M. Ohnishi and D. W. Urry (1969). Temperature dependence of amide proton chemical shift: The secondary structures of gramicidin S and Valinomycln. Biochem. Biophys. Res. Commun. 36, 194-202.
    • (1969) Biochem. Biophys. Res. Commun. , vol.36 , pp. 194-202
    • Ohnishi, M.1    Urry, D.W.2
  • 30
    • 33646746207 scopus 로고
    • Scalar coupling constants-their analysis and their application for the elucidation of structures
    • M. Eberstadt, G. Gemmecker, D. F. Mierke and H. Kessler (1995). Scalar coupling constants-their analysis and their application for the elucidation of structures. Angew. Chem. Int. Ed. Engl. 34, 1671-1695.
    • (1995) Angew. Chem. Int. Ed. Engl. , vol.34 , pp. 1671-1695
    • Eberstadt, M.1    Gemmecker, G.2    Mierke, D.F.3    Kessler, H.4
  • 31
    • 0028672867 scopus 로고
    • Use of chemical shifts and coupling constants in nuclear and magnetic resonance structural studies on peptides and proteins
    • D. A. Case, J. Dyson and P. E. Wright (1994). Use of chemical shifts and coupling constants in nuclear and magnetic resonance structural studies on peptides and proteins. Methods Enzymol. 239, 392-416.
    • (1994) Methods Enzymol. , vol.239 , pp. 392-416
    • Case, D.A.1    Dyson, J.2    Wright, P.E.3
  • 32
    • 0029207339 scopus 로고
    • 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG
    • 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG. J. Biomol. NMR 5, 14-24.
    • (1995) J. Biomol. NMR , vol.5 , pp. 14-24
    • Merutka, G.1    Dyson, H.J.2    Wright, P.E.3
  • 33
    • 0028871617 scopus 로고
    • Nonnative capping structure 0 initiates helix folding in an Annexin-I fragment - A H-1-NMR conformational study
    • B. Odaert, F. Baleux, T. Huynhdinh, J. M. Neumann and A. Sanson (1995). Nonnative capping structure 0 initiates helix folding in an Annexin-I fragment - a H-1-NMR conformational study. Biochemistry 34, 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
  • 34
    • 0028447768 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters
    • V. Munoz and L. Serrano (1994). Elucidating the folding problem of helical peptides using empirical parameters. Nature Struct. Biol. 1, 399-409.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 399-409
    • Munoz, V.1    Serrano, L.2
  • 35
    • 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
    • V. Munoz and L. Serrano (1995). 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, 275-296.
    • (1995) J. Mol. Biol. , vol.245 , pp. 275-296
    • Munoz, V.1    Serrano, L.2
  • 36
    • 0028834210 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters: III. Temperature and pH dependence
    • V. Munoz and L. Serrano (1995). Elucidating the folding problem of helical peptides using empirical parameters: III. Temperature and pH dependence. J. Mol. Biol. 245, 297-308.
    • (1995) J. Mol. Biol. , vol.245 , pp. 297-308
    • Munoz, V.1    Serrano, L.2
  • 38
    • 0015217634 scopus 로고
    • The solubility of amino acids and two glycine peptdes in aqueous ethanol and dioxane solutions
    • Nozakl and Tanford (1971). The solubility of amino acids and two glycine peptdes in aqueous ethanol and dioxane solutions. J. Biol. Chem. 246, 2211-2217.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2211-2217
    • Nozakl1    Tanford2
  • 39
    • 0000092491 scopus 로고
    • Promotion of helix formation in peptides dissolved in alcohol and water-alcohol mixtures
    • Brooks and Nielsen (1993). Promotion of helix formation in peptides dissolved in alcohol and water-alcohol mixtures. J. Am. Chem. Soc. 115, 11034-11035.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 11034-11035
    • Brooks1    Nielsen2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.