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Volumn 13, Issue 7, 2004, Pages 1918-1926

Facile chemical synthesis and equilibrium unfolding properties of CopG

Author keywords

Protein design; Protein folding unfolding; Total chemical synthesis

Indexed keywords

GUANIDINE; PROTEIN COPG; REPRESSOR PROTEIN; UNCLASSIFIED DRUG;

EID: 3042630863     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04671804     Document Type: Article
Times cited : (7)

References (19)
  • 1
    • 3543005326 scopus 로고    scopus 로고
    • Structural features of the plasmid pMV158-encoded transcriptional repressor CopG, a protein sharing similarities with both helix-turn-helix and β-sheet DNA binding proteins
    • Acebo, P., Garcia de Lacoba, M., Rivas, G., Andreu, J.M., Espinosa, M., and del Solar, G. 1998. Structural features of the plasmid pMV158-encoded transcriptional repressor CopG, a protein sharing similarities with both helix-turn-helix and β-sheet DNA binding proteins. Proteins 32: 248-261.
    • (1998) Proteins , vol.32 , pp. 248-261
    • Acebo, P.1    Garcia De Lacoba, M.2    Rivas, G.3    Andreu, J.M.4    Espinosa, M.5    Del Solar, G.6
  • 2
    • 0034645614 scopus 로고    scopus 로고
    • Design, synthesis, and characterization of 4-ester C12, a model for backbone hydrogen bonding in protein α-helices
    • Beligere, G.S. and Dawson, P.E. 2000. Design, synthesis, and characterization of 4-ester C12, a model for backbone hydrogen bonding in protein α-helices. J. Am. Chem. Soc. 122: 12079-12082.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12079-12082
    • Beligere, G.S.1    Dawson, P.E.2
  • 3
    • 85004754595 scopus 로고
    • Side chain reactions in peptide synthesis
    • Bodansky, M. and Martinez, J. 1981. Side chain reactions in peptide synthesis. Synthesis (Stuttgart) 5: 333-356.
    • (1981) Synthesis (Stuttgart) , vol.5 , pp. 333-356
    • Bodansky, M.1    Martinez, J.2
  • 4
    • 0024962376 scopus 로고
    • Equilibrium dissociation and unfolding of the Arc repressor dimer
    • Bowie, J.U. and Sauer, R.T. 1989. Equilibrium dissociation and unfolding of the Arc repressor dimer. Biochemistry 28: 7139-7143.
    • (1989) Biochemistry , vol.28 , pp. 7139-7143
    • Bowie, J.U.1    Sauer, R.T.2
  • 5
    • 0016169865 scopus 로고
    • Determination of the helix and β form of proteins in aqueous solution by circular dichroism
    • Chen, Y.H., Yang, J.T., and Chau, K.H. 1974. Determination of the helix and β 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
  • 6
    • 0035816213 scopus 로고    scopus 로고
    • Plasmid transcriptional repressor CopG oligomerises to render helical superstructures unbound and in complexes with oligonucleotides
    • Costa, M., Sola, M., del Solar, G., Eritja, R., Hernandez-Arriaga, A.M., Espinosa, M., Gomis-Rüth, F.X., and Coll, M. 2001. Plasmid transcriptional repressor CopG oligomerises to render helical superstructures unbound and in complexes with oligonucleotides. J. Mol. Biol. 310: 403-417.
    • (2001) J. Mol. Biol. , vol.310 , pp. 403-417
    • Costa, M.1    Sola, M.2    Del Solar, G.3    Eritja, R.4    Hernandez-Arriaga, A.M.5    Espinosa, M.6    Gomis-Rüth, F.X.7    Coll, M.8
  • 7
    • 0026502191 scopus 로고
    • The copy number plasmid of pLSI is regulated by two trans-acting plasmid products: The antisense RNA II and the repressor protein RepA
    • del Solar, G. and Espinosa, M. 1992. The copy number plasmid of pLSI is regulated by two trans-acting plasmid products: the antisense RNA II and the repressor protein RepA. Mol. Microbiol. 6: 83-94.
    • (1992) Mol. Microbiol. , vol.6 , pp. 83-94
    • Del Solar, G.1    Espinosa, M.2
  • 8
    • 0028236013 scopus 로고
    • Chemical synthesis of a fully active transcriptional repressor protein
    • del Solar, G., Albericio, F., Eritja, R., and Espinosa, M. 1994. Chemical synthesis of a fully active transcriptional repressor protein. Proc. Natl. Acad. Sci. 91: 5178-5182.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 5178-5182
    • Del Solar, G.1    Albericio, F.2    Eritja, R.3    Espinosa, M.4
  • 11
    • 0001414449 scopus 로고    scopus 로고
    • Probing intermolecular main chain hydrogen bonding in serine protinase-protein inhibitor complexes: Chemical synthesis of backbone-engineered turkey ovomucoid third domain
    • Lu, W.Y., Qasim, M.A., Laskowski Jr., M., and Kent, S.B.H. 1997. Probing intermolecular main chain hydrogen bonding in serine protinase-protein inhibitor complexes: Chemical synthesis of backbone-engineered turkey ovomucoid third domain. Biochemistry 36: 673-679.
    • (1997) Biochemistry , vol.36 , pp. 673-679
    • Lu, W.Y.1    Qasim, M.A.2    Laskowski Jr., M.3    Kent, S.B.H.4
  • 12
    • 0028325298 scopus 로고
    • Arc repressor: Folding kinetics for a single-domain, dimeric protein
    • Milla, M.E. and Sauer, R.T. 1994. Arc repressor: Folding kinetics for a single-domain, dimeric protein. Biochemistry 33: 1125-1133.
    • (1994) Biochemistry , vol.33 , pp. 1125-1133
    • Milla, M.E.1    Sauer, R.T.2
  • 13
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers, J.K., Pace, C.N., and Scholtz, J.M. 1995. Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4: 2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 14
    • 0034734353 scopus 로고    scopus 로고
    • Identification of an essential backbone amide bond in the folding and stability of a multimeric enzyme
    • Nakhle, B.M., Silinski, P., and Fitzgerald, M.C. 2000. Identification of an essential backbone amide bond in the folding and stability of a multimeric enzyme. J. Am. Chem. Soc. 122: 8105-8111.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8105-8111
    • Nakhle, B.M.1    Silinski, P.2    Fitzgerald, M.C.3
  • 15
    • 0026486811 scopus 로고
    • In situ neutralization in Boc-chemistry solid phase peptide synthesis: Rapid, high yield assembly of difficult sequences
    • Schnölzer, M., Alewood, P., Jones, A., Alewood, D., and Kent, S.B.H. 1992. In situ neutralization in Boc-chemistry solid phase peptide synthesis: Rapid, high yield assembly of difficult sequences. Int. J. Peptide Protein Res. 40: 180-193.
    • (1992) Int. J. Peptide Protein Res. , vol.40 , pp. 180-193
    • Schnölzer, M.1    Alewood, P.2    Jones, A.3    Alewood, D.4    Kent, S.B.H.5
  • 16
    • 0001479670 scopus 로고
    • A simple ultraviolet spectrophotometric method for the determination of protein
    • Waddell, W.J. 1956. A simple ultraviolet spectrophotometric method for the determination of protein. J. Lab. Clin. Med. 48: 311-314.
    • (1956) J. Lab. Clin. Med. , vol.48 , pp. 311-314
    • Waddell, W.J.1
  • 17
    • 0034794583 scopus 로고    scopus 로고
    • The energetic contribution of backbone-backbone hydrogen bonds to the thermodynamic stability of a hyperstable P22 Arc repressor mutant
    • Wales, T.E. and Fitzgerald, M.C. 2001. The energetic contribution of backbone-backbone hydrogen bonds to the thermodynamic stability of a hyperstable P22 Arc repressor mutant. J. Am. Chem. Soc. 123: 7709-7710.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7709-7710
    • Wales, T.E.1    Fitzgerald, M.C.2
  • 19
    • 0000325019 scopus 로고    scopus 로고
    • Thermodynamic and structural effects of a single backbone hydrogen bond deletion in a metal-assembled helical bundle protein
    • Zhou, J., Case, M., Wishart, J.F., and McLendon, G.L. 1998. Thermodynamic and structural effects of a single backbone hydrogen bond deletion in a metal-assembled helical bundle protein. J. Phys. Chem. B 102: 9975-9980.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 9975-9980
    • Zhou, J.1    Case, M.2    Wishart, J.F.3    McLendon, G.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.