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Volumn 260, Issue 2, 1996, Pages 126-134

A thermostable 35-residue subdomain within villin headpiece

Author keywords

NMR; Protein folding; Subdomain; Thermostability; Villin

Indexed keywords

ACTIN BINDING PROTEIN; CYSTEINE; VILLIN;

EID: 0008501653     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0387     Document Type: Editorial
Times cited : (205)

References (43)
  • 4
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen, G. & Ruben, D. J. (1980). Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Letters, 69, 185-189.
    • (1980) Chem. Phys. Letters , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 5
    • 0344975376 scopus 로고
    • Villin: The major microfilament-associated protein of the intestinal microvillus
    • Bretscher, A. & Weber, K. (1979). Villin: the major microfilament-associated protein of the intestinal microvillus. Proc. Natl Acad. Sci. USA, 76, 2321-2325.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 2321-2325
    • Bretscher, A.1    Weber, K.2
  • 6
    • 84985733652 scopus 로고
    • 1H-NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH
    • 1H-NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH. Biopolymers, 18, 285-297.
    • (1979) Biopolymers , vol.18 , pp. 285-297
    • Bundi, A.1    Wüthrich, K.2
  • 8
    • 0016169865 scopus 로고
    • Determination of the helix and B form of proteins in aqueous solution by circular dichroism
    • Chen, Y.-H., Yang, J. T. & Chau, K. H. (1974). Determination of the helix and B form of proteins in aqueous solution by circular dichroism. Biochemistry, 13, 3350-3359.
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.-H.1    Yang, J.T.2    Chau, K.H.3
  • 10
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. (1967). Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry, 6, 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 11
    • 0026554080 scopus 로고
    • In vivo analysis of functional domains from villin and gelsolin
    • Finidori, J., Friederich, E., Kwiatkowski, D. J. & Louvard, D. (1992). In vivo analysis of functional domains from villin and gelsolin. J. Cell Biol. 116, 1145-1155.
    • (1992) J. Cell Biol. , vol.116 , pp. 1145-1155
    • Finidori, J.1    Friederich, E.2    Kwiatkowski, D.J.3    Louvard, D.4
  • 12
    • 0026773096 scopus 로고
    • An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin
    • Friederich, E., Vancompernolle, K., Huet, C., Goethals, M., Finidori, J., Vandekerckhove, J. & Louvard, D. (1992). An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin. Cell, 70, 81-92.
    • (1992) Cell , vol.70 , pp. 81-92
    • Friederich, E.1    Vancompernolle, K.2    Huet, C.3    Goethals, M.4    Finidori, J.5    Vandekerckhove, J.6    Louvard, D.7
  • 13
    • 0019821604 scopus 로고
    • Demonstration of at least two different actin-binding sites in villin, a calcium-regulated modulator of f-actin organization
    • Glenny, J. R. J., Geisler, N., Kaulfus, P. & Weber, K. (1981). Demonstration of at least two different actin-binding sites in villin, a calcium-regulated modulator of f-actin organization. J. Biol. Chem. 256, 8156-8161.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8156-8161
    • Glenny, J.R.J.1    Geisler, N.2    Kaulfus, P.3    Weber, K.4
  • 16
    • 0027404572 scopus 로고
    • The high-resolution structure of the peripheral subunit-binding domain of dihydrolipoamide acetyltransferase from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus
    • Kalia, Y. N., Brocklehurst, S. M., Hipps, D. S., Appella, E., Sakaguchi, K. & Perham, R. N. (1993). The high-resolution structure of the peripheral subunit-binding domain of dihydrolipoamide acetyltransferase from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. J. Mol. Biol. 230, 323-341.
    • (1993) J. Mol. Biol. , vol.230 , pp. 323-341
    • Kalia, Y.N.1    Brocklehurst, S.M.2    Hipps, D.S.3    Appella, E.4    Sakaguchi, K.5    Perham, R.N.6
  • 17
    • 0017178548 scopus 로고
    • Three-state denaturation of α-lactalbumin by guanidine hydrochloride
    • Kuwajima, K., Nitta, K., Yoneyama, M. & Sugai, S. (1976). Three-state denaturation of α-lactalbumin by guanidine hydrochloride. J. Mol. Biol. 106, 359-373.
    • (1976) J. Mol. Biol. , vol.106 , pp. 359-373
    • Kuwajima, K.1    Nitta, K.2    Yoneyama, M.3    Sugai, S.4
  • 18
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • Harding, S. E., Rowe, A. J. & Horton, J. C., eds, The Royal Society of Chemistry, Cambridge, UK
    • Laue, T. M., Shah, B. D., Ridgeway, T. M. & Pelletier, S. L. (1992). Computer-aided interpretation of analytical sedimentation data for proteins. In Analytical Ultracentrifugation in Biochemistry and Polymer Science (Harding, S. E., Rowe, A. J. & Horton, J. C., eds), pp. 90-125, The Royal Society of Chemistry, Cambridge, UK.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 19
    • 0027384196 scopus 로고
    • Hydrogen exchange in unligated and ligated staphylococcal nuclease
    • Loh, S. N., Prehoda, K. E., Jinfeng, W. & Markely, J. L. (1993). Hydrogen exchange in unligated and ligated staphylococcal nuclease. Biochemistry, 32, 11022-11028.
    • (1993) Biochemistry , vol.32 , pp. 11022-11028
    • Loh, S.N.1    Prehoda, K.E.2    Jinfeng, W.3    Markely, J.L.4
  • 20
    • 0029008590 scopus 로고
    • A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil
    • Lumb, K. J. & Kim, P. S. (1995). A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil. Biochemistry, 34, 8642-8648.
    • (1995) Biochemistry , vol.34 , pp. 8642-8648
    • Lumb, K.J.1    Kim, P.S.2
  • 22
    • 0027495048 scopus 로고
    • Amide proton exchange rates of oxidized and reduced Saccharomyces cerevisiae iso-1-cytochrome c
    • Marmorino, J. L., Auld, D. S., Betz, S. F., Doyle, D. F., Young, G. B. & Pielak, G. J. (1993). Amide proton exchange rates of oxidized and reduced Saccharomyces cerevisiae iso-1-cytochrome c. Protein Sci. 2, 1966-1974.
    • (1993) Protein Sci. , vol.2 , pp. 1966-1974
    • Marmorino, J.L.1    Auld, D.S.2    Betz, S.F.3    Doyle, D.F.4    Young, G.B.5    Pielak, G.J.6
  • 23
    • 0024707204 scopus 로고
    • Unusually stable helix formation in short alanine-based peptides
    • Marqusee, S., Robbins, V. H. & Baldwin, R. L. (1989). Unusually stable helix formation in short alanine-based peptides. Proc. Natl Acad. Sci. USA, 86, 5286-5290.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 5286-5290
    • Marqusee, S.1    Robbins, V.H.2    Baldwin, R.L.3
  • 24
    • 0027730340 scopus 로고
    • Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A
    • Mayo, S. L. & Baldwin, R. L. (1993). Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A. Science, 262, 873-876.
    • (1993) Science , vol.262 , pp. 873-876
    • Mayo, S.L.1    Baldwin, R.L.2
  • 25
    • 0024836418 scopus 로고
    • Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance
    • Muchmore, D. C., McIntosh, L. P., Russell, C. B., Anderson, D. E, & Dahlquist, F. W. (1989). Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance. Methods Enzymol. 177, 44-73.
    • (1989) Methods Enzymol. , vol.177 , pp. 44-73
    • Muchmore, D.C.1    McIntosh, L.P.2    Russell, C.B.3    Anderson, D.E.4    Dahlquist, F.W.5
  • 26
    • 0023692599 scopus 로고
    • A peptide model of a protein folding intermediate
    • Oas, T. G. & Kim, P. S. (1988). A peptide model of a protein folding intermediate. Nature, 336, 42-48.
    • (1988) Nature , vol.336 , pp. 42-48
    • Oas, T.G.1    Kim, P.S.2
  • 27
    • 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
  • 28
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C. N. (1986). Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131, 266-280.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 29
    • 0028058169 scopus 로고
    • Characterization of the F-actin binding domains of villin: Classification of F-actin binding proteins into two groups according to their binding sites on actin
    • Pope, B., Way, M., Matsudaira, P. T. & Weeds, A. (1994). Characterization of the F-actin binding domains of villin: classification of F-actin binding proteins into two groups according to their binding sites on actin. FEBS Letters, 338, 58-62.
    • (1994) FEBS Letters , vol.338 , pp. 58-62
    • Pope, B.1    Way, M.2    Matsudaira, P.T.3    Weeds, A.4
  • 30
    • 0002940127 scopus 로고
    • The molten globule state
    • Creighton, T. E., ed., W. H. Freeman and Co., New York
    • Ptitsyn, O. B. (1992). The molten globule state. In Protein Folding (Creighton, T. E., ed.), pp. 243-300, W. H. Freeman and Co., New York.
    • (1992) Protein Folding , pp. 243-300
    • Ptitsyn, O.B.1
  • 32
    • 0002345583 scopus 로고
    • Study and applications of the effects of detergents and chaotropes on enzymatic proteolysis
    • Villafranca, J. J., ed., Academic Press Inc., San Diego
    • Riviere, L. R., Fleming, M., Elicone, C. & Tempst, P. (1991). Study and applications of the effects of detergents and chaotropes on enzymatic proteolysis. In Techniques in Protein Chemistry II (Villafranca, J. J., ed.), pp. 171-180, Academic Press Inc., San Diego.
    • (1991) Techniques in Protein Chemistry , vol.2 , pp. 171-180
    • Riviere, L.R.1    Fleming, M.2    Elicone, C.3    Tempst, P.4
  • 33
    • 0024331090 scopus 로고
    • Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange
    • Roder, H. (1989). Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange. Methods Enzymol. 176, 446-473.
    • (1989) Methods Enzymol. , vol.176 , pp. 446-473
    • Roder, H.1
  • 34
    • 0018782641 scopus 로고
    • Hierarchic organization of domains in globular proteins
    • Rose, G. D. (1979). Hierarchic organization of domains in globular proteins. J. Mol. Biol. 134, 447-470.
    • (1979) J. Mol. Biol. , vol.134 , pp. 447-470
    • Rose, G.D.1
  • 37
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different deaturants
    • Santoro, M. M. & Bolen, D. W. (1988). Unfolding free energy changes determined by the linear extrapolation method 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different deaturants. Biochemistry, 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 38
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H. & von Jagow, G. (1987). Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem. 166, 368-379.
    • (1987) Anal Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 39
    • 0030593029 scopus 로고    scopus 로고
    • Design of a monomeric 23-residue polypeptide with defined tertiary structure
    • Struthers, M. D., Cheng, R. P. & Imperiali, B. (1996). Design of a monomeric 23-residue polypeptide with defined tertiary structure. Science, 271, 342-345.
    • (1996) Science , vol.271 , pp. 342-345
    • Struthers, M.D.1    Cheng, R.P.2    Imperiali, B.3
  • 43
    • 0000018782 scopus 로고
    • A proton-detected heteronuclear chemical-shift correlation experiment with improved resolution and sensitivity
    • Zuiderweg, E. P. R. (1990). A proton-detected heteronuclear chemical-shift correlation experiment with improved resolution and sensitivity. J. Magn. Reson. 86, 346-357.
    • (1990) J. Magn. Reson. , vol.86 , pp. 346-357
    • Zuiderweg, E.P.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.