메뉴 건너뛰기




Volumn 255, Issue 3, 1996, Pages 367-372

Ion pairs significantly stabilize coiled-coils in the absence of electrolyte

Author keywords

Coiled coil; Ion pairs; pH effect; Salt effect; Unfolding

Indexed keywords

ELECTROLYTE; GLUTAMIC ACID; ION; SODIUM CHLORIDE;

EID: 0029919676     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0030     Document Type: Editorial
Times cited : (67)

References (27)
  • 2
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C. & von Hippel, P. H. (1989). Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 4
    • 0028076788 scopus 로고
    • Reversed-phase liquid chromatography as a useful probe of hydrophobic interactions involved in protein folding and protein stability
    • Hodges, R. S., Zhu, B. Y., Zhou, N. E. & Mant, C. T. (1994). Reversed-phase liquid chromatography as a useful probe of hydrophobic interactions involved in protein folding and protein stability. J. Chromatog. sect. A, 676, 3-15.
    • (1994) J. Chromatog. Sect. A , vol.676 , pp. 3-15
    • Hodges, R.S.1    Zhu, B.Y.2    Zhou, N.E.3    Mant, C.T.4
  • 6
    • 0028303384 scopus 로고
    • A thermodynamic scale for leucine zipper stability and dimerization specificity: E and g interhelical interactions
    • Krylov, D., Mikhailenko, I. & Vinson, C. (1994). A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions. EMBO J. 13, 2849-2861.
    • (1994) EMBO J. , vol.13 , pp. 2849-2861
    • Krylov, D.1    Mikhailenko, I.2    Vinson, C.3
  • 7
    • 0021719074 scopus 로고
    • Synthesis of a model protein of defined secondary and quaternary structure
    • Lau, S. Y. M., Taneja, A. K. & Hodges, R. S. (1984). Synthesis of a model protein of defined secondary and quaternary structure. J. Biol. Chem. 259, 13253-13261.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13253-13261
    • Lau, S.Y.M.1    Taneja, A.K.2    Hodges, R.S.3
  • 8
    • 0343926429 scopus 로고
    • The stability of tropomyosin at acidic pH is greatly influenced by the binding of anions
    • Lehrer, S. S. & Yuan, A. (1995). The stability of tropomyosin at acidic pH is greatly influenced by the binding of anions. Protein Sci. 4, 72 (suppl. 2).
    • (1995) Protein Sci. , vol.4 , Issue.SUPPL. 2 , pp. 72
    • Lehrer, S.S.1    Yuan, A.2
  • 9
    • 0000820879 scopus 로고
    • Comparative study of the α-helical muscle proteins
    • Lowey S. (1965). Comparative study of the α-helical muscle proteins. J. Biol. Chem. 240, 2421-2427.
    • (1965) J. Biol. Chem. , vol.240 , pp. 2421-2427
    • Lowey, S.1
  • 10
    • 84914430199 scopus 로고
    • A comparative study of the spectrophotometric titration curves of the α-proteins: Myosin, the meromyosins, tropomyosin and paramyosin
    • Gergely J., ed., Little, Brown and Co., Boston, MA
    • Lowey, S. & Kucera, J. (1964). A comparative study of the spectrophotometric titration curves of the α-proteins: myosin, the meromyosins, tropomyosin and paramyosin. In Biochemistry of Muscle Contraction (Gergely J., ed.), pp. 8-18, Little, Brown and Co., Boston, MA.
    • (1964) Biochemistry of Muscle Contraction , pp. 8-18
    • Lowey, S.1    Kucera, J.2
  • 11
    • 0029030233 scopus 로고
    • Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper
    • Lumb, K. J. & Kim, P. S. (1995). Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper. Science, 268, 436-439.
    • (1995) Science , vol.268 , pp. 436-439
    • Lumb, K.J.1    Kim, P.S.2
  • 12
    • 0015274187 scopus 로고
    • On the application of polyelectrolyte "limiting laws" to the helix-coil transitions of DNA. I. Excess univalent cations
    • Manning, G. S. (1972). On the application of polyelectrolyte "limiting laws" to the helix-coil transitions of DNA. I. Excess univalent cations. Biopolymers, 11, 937-949.
    • (1972) Biopolymers , vol.11 , pp. 937-949
    • Manning, G.S.1
  • 13
    • 0017895903 scopus 로고
    • The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides
    • Manning, G. S. (1978). The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides. Quart. Rev. Biophys. 11, 179-246.
    • (1978) Quart. Rev. Biophys. , vol.11 , pp. 179-246
    • Manning, G.S.1
  • 14
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
    • McLachlan, A. D. & Stewart, M. (1975). Tropomyosin coiled-coil interactions: evidence for an unstaggered structure. J. Mol. Biol. 98, 293-304.
    • (1975) J. Mol. Biol. , vol.98 , pp. 293-304
    • McLachlan, A.D.1    Stewart, M.2
  • 15
    • 0028569153 scopus 로고
    • Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions
    • Monera, O. D., Kay, C. M. & Hodges, R. S. (1994). Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions. Protein Sci. 3, 1984-1991.
    • (1994) Protein Sci. , vol.3 , pp. 1984-1991
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 16
    • 0003328372 scopus 로고
    • The denaturation of paramyosin and tropomyosin by guanidine hydrochloride
    • Gergely J., ed., Little, Brown and Co., Boston, MA
    • Noelken, M. & Holtzer, A. M. (1964). The denaturation of paramyosin and tropomyosin by guanidine hydrochloride. In Biochemistry of Muscle Contraction (Gergely J., ed.), pp. 374-378, Little, Brown and Co., Boston, MA.
    • (1964) Biochemistry of Muscle Contraction , pp. 374-378
    • Noelken, M.1    Holtzer, A.M.2
  • 17
    • 84984086924 scopus 로고
    • A theory on the effect of low molecular salts on the conformation of linear polyions
    • Oosawa, F. (1968). A theory on the effect of low molecular salts on the conformation of linear polyions. Biopolymers, 6, 145-158.
    • (1968) Biopolymers , vol.6 , pp. 145-158
    • Oosawa, F.1
  • 18
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea, E. K., Klemm, J. D., Kim, P. S. & Alber, T. (1991). X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science, 254, 539-544.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 19
    • 0000236570 scopus 로고
    • Peptide 'Velcro*': Design of a heterodimeric coiled coil
    • O'Shea, E. K., Lumb, K. J. & Kim, P. S. (1993). Peptide 'Velcro*': design of a heterodimeric coiled coil. Curr. Biol. 3, 658-667.
    • (1993) Curr. Biol. , vol.3 , pp. 658-667
    • O'Shea, E.K.1    Lumb, K.J.2    Kim, P.S.3
  • 20
    • 84984087761 scopus 로고
    • Determination of stability of the DNA double helix in an aqueous medium
    • Privalov, P. L., Ptitsyn, O. B. & Birshtein, T. M. (1969). Determination of stability of the DNA double helix in an aqueous medium. Biopolymers, 8, 559-571.
    • (1969) Biopolymers , vol.8 , pp. 559-571
    • Privalov, P.L.1    Ptitsyn, O.B.2    Birshtein, T.M.3
  • 21
    • 0005151785 scopus 로고
    • Structural studies of paramyosin. II. Conformational changes
    • Riddiford, L. M. & Scheraga, H. A. (1961). Structural studies of paramyosin. II. Conformational changes. Biochemistry, 1, 108-114.
    • (1961) Biochemistry , vol.1 , pp. 108-114
    • Riddiford, L.M.1    Scheraga, H.A.2
  • 22
    • 0027497118 scopus 로고
    • The enrgetics of ion-pair and hydrogen-bonding interactions in a helical peptide
    • Scholtz, J. M., Qian, H., Robbins, V. H. & Baldwin, R. L. (1993). The enrgetics of ion-pair and hydrogen-bonding interactions in a helical peptide. Biochemistry, 32, 9668-9676.
    • (1993) Biochemistry , vol.32 , pp. 9668-9676
    • Scholtz, J.M.1    Qian, H.2    Robbins, V.H.3    Baldwin, R.L.4
  • 24
    • 0014613497 scopus 로고
    • Studies on the denaturation of tropomyosin and light meromyosin
    • Woods, E. F. (1969). Studies on the denaturation of tropomyosin and light meromyosin. Int. J. Protein Res. 1, 29-43.
    • (1969) Int. J. Protein Res. , vol.1 , pp. 29-43
    • Woods, E.F.1
  • 25
    • 0030014013 scopus 로고    scopus 로고
    • Investigation of electrostatic interactions in two-stranded coiled-coils through residue shuffling
    • In the press
    • Yu, Y., Monera, O. D., Hodges, R. S. & Privalov, P. L. (1996). Investigation of electrostatic interactions in two-stranded coiled-coils through residue shuffling. Biophys. Chem. In the press.
    • (1996) Biophys. Chem.
    • Yu, Y.1    Monera, O.D.2    Hodges, R.S.3    Privalov, P.L.4
  • 26
    • 0028036221 scopus 로고
    • Alpha helix capping in synthetic model peptides by reciprocal side chain-main chain interactions: Evidence for an N terminal "capping box"
    • Zhou, H. X., Lyu, P., Wemmer, D. E. & Kallenbach, N. R. (1994). Alpha helix capping in synthetic model peptides by reciprocal side chain-main chain interactions: evidence for an N terminal "capping box". Proteins: Struct. Funct. Genet. 18, 1-7.
    • (1994) Proteins: Struct. Funct. Genet. , vol.18 , pp. 1-7
    • Zhou, H.X.1    Lyu, P.2    Wemmer, D.E.3    Kallenbach, N.R.4
  • 27
    • 0027949381 scopus 로고
    • The net energetic contribution of interhelical electrostatic attractions to coiled-coil stability
    • Zhou, N. E., Kay C. M. & Hodges, R. S. (1994). The net energetic contribution of interhelical electrostatic attractions to coiled-coil stability. Protein Eng. 7, 1365-1372.
    • (1994) Protein Eng. , vol.7 , pp. 1365-1372
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.