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Volumn 1, Issue 2, 1996, Pages

Protein folding from a combinatorial perspective

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOPHAGE LAMBDA REPRESSOR PROTEIN; DNA BINDING PROTEIN; PHAGE REPRESSOR PROTEINS; PROTEIN; REPRESSOR PROTEIN; VIRUS PROTEIN;

EID: 0002983608     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(96)00015-6     Document Type: Article
Times cited : (37)

References (31)
  • 1
    • 0023949179 scopus 로고
    • Combinatorial cassette mutagenesis as a probe of the informational content of protein sequences
    • Reidhaar-Olson, J.F. & Sauer, R.T. (1988). Combinatorial cassette mutagenesis as a probe of the informational content of protein sequences. Science 241, 53-57.
    • (1988) Science , vol.241 , pp. 53-57
    • Reidhaar-Olson, J.F.1    Sauer, R.T.2
  • 2
    • 0001586362 scopus 로고
    • Identifying determinants of folding and activity for a protein of unknown structure
    • Bowie, J.U. & Sauer, R.T. (1989). Identifying determinants of folding and activity for a protein of unknown structure. Proc. Natl. Acad. Sci. USA 86, 2152-2156.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2152-2156
    • Bowie, J.U.1    Sauer, R.T.2
  • 3
    • 0024507791 scopus 로고
    • Alternative packing arrangements in the hydrophobic core of λ repressor
    • Lim, W.A. & Sauer, R.T. (1989). Alternative packing arrangements in the hydrophobic core of λ repressor. Nature 339, 31-36.
    • (1989) Nature , vol.339 , pp. 31-36
    • Lim, W.A.1    Sauer, R.T.2
  • 4
    • 0024307543 scopus 로고
    • Mutational analysis of the fine specificity of binding of monoclonal antibody 51F to λ repressor
    • Breyer, R.M. & Sauer, R.T. (1989). Mutational analysis of the fine specificity of binding of monoclonal antibody 51F to λ repressor. J. Biol. Chem. 264, 13355-13360.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13355-13360
    • Breyer, R.M.1    Sauer, R.T.2
  • 5
    • 23444436172 scopus 로고
    • Protein design by binary patterning of polar and nonpolar amino acids
    • Kamtekar, S., Schiffer, J.M., Xiong, H., Babik, J.M. & Hecht, M.H. (1993). Protein design by binary patterning of polar and nonpolar amino acids. Science 262, 1680-1685.
    • (1993) Science , vol.262 , pp. 1680-1685
    • Kamtekar, S.1    Schiffer, J.M.2    Xiong, H.3    Babik, J.M.4    Hecht, M.H.5
  • 6
    • 0027211894 scopus 로고
    • Additivity of mutant effects assessed by binomial mutagenesis
    • Gregoret, L. & Sauer, R.T. (1993). Additivity of mutant effects assessed by binomial mutagenesis. Proc. Natl. Acad. Sci. USA 90, 4246-4250.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4246-4250
    • Gregoret, L.1    Sauer, R.T.2
  • 7
    • 0027180729 scopus 로고
    • Probing the roles of residues at the e and g positions of the GCN4 leucine zipper by combinatorial mutagenesis
    • Hu, J.C., Newell, N.E., Tidor, B. & Sauer, R.T. (1993). Probing the roles of residues at the e and g positions of the GCN4 leucine zipper by combinatorial mutagenesis. Protein Sci. 2,1072-1084.
    • (1993) Protein Sci. , vol.2 , pp. 1072-1084
    • Hu, J.C.1    Newell, N.E.2    Tidor, B.3    Sauer, R.T.4
  • 8
    • 0025370163 scopus 로고
    • Functionally acceptable substitutions in two α-helical regions of λ repressor
    • Reidhaar-Olson, J.F. & Sauer, R.T. (1990). Functionally acceptable substitutions in two α-helical regions of λ repressor. Proteins 7, 306-316.
    • (1990) Proteins , vol.7 , pp. 306-316
    • Reidhaar-Olson, J.F.1    Sauer, R.T.2
  • 9
    • 0025363984 scopus 로고
    • Deciphering the message in protein sequences: Tolerance to amino acid substitutions
    • Bowie, J.U., Reidhaar-Olson, J.F., Lim, W.A. & Sauer, R.T. (1990). Deciphering the message in protein sequences: tolerance to amino acid substitutions. Science 247, 1306-1310.
    • (1990) Science , vol.247 , pp. 1306-1310
    • Bowie, J.U.1    Reidhaar-Olson, J.F.2    Lim, W.A.3    Sauer, R.T.4
  • 11
    • 0027815614 scopus 로고
    • An analysis of packing in the protein folding problem
    • Richards, F.M. & Lim, W. (1993). An analysis of packing in the protein folding problem. Q. Rev. Biophys. 26, 423-498.
    • (1993) Q. Rev. Biophys. , vol.26 , pp. 423-498
    • Richards, F.M.1    Lim, W.2
  • 12
    • 0025908265 scopus 로고
    • The role of internal packing interactions in determining the structure and stability of a protein
    • Lim, W.A. & Sauer, R.T. (1991). The role of internal packing interactions in determining the structure and stability of a protein. J. Mol. Biol. 219, 359-376.
    • (1991) J. Mol. Biol. , vol.219 , pp. 359-376
    • Lim, W.A.1    Sauer, R.T.2
  • 13
    • 0026766573 scopus 로고
    • The structural and energetic consequences of disruptive mutations in a protein core
    • Lim, W.A., Farruggio, D.C. & Sauer, R.T. (1992). The structural and energetic consequences of disruptive mutations in a protein core. Biochemistry 31, 4324-4333.
    • (1992) Biochemistry , vol.31 , pp. 4324-4333
    • Lim, W.A.1    Farruggio, D.C.2    Sauer, R.T.3
  • 15
    • 0025598302 scopus 로고
    • Sequence requirements for coiled-coil interactions: Analysis using X repressor-GCN4 leucine zipper fusions
    • Hu, J.C., O'Shea, E.K., Kim, P.S. & Sauer, R.T. (1990). Sequence requirements for coiled-coil interactions: analysis using X repressor-GCN4 leucine zipper fusions. Science 250, 1400-1403.
    • (1990) Science , vol.250 , pp. 1400-1403
    • Hu, J.C.1    O'Shea, E.K.2    Kim, P.S.3    Sauer, R.T.4
  • 16
    • 0027450286 scopus 로고
    • Exploring the interface between the N- and C-terminal helices of cytochrome c by random mutagenesis within the C-terminal helix
    • Fredericks, Z.L. & Pielak, G.J. (1993). Exploring the interface between the N- and C-terminal helices of cytochrome c by random mutagenesis within the C-terminal helix. Biochemistry 32, 929-936.
    • (1993) Biochemistry , vol.32 , pp. 929-936
    • Fredericks, Z.L.1    Pielak, G.J.2
  • 17
    • 0027716138 scopus 로고
    • The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme
    • Baldwin, E.P., Hajiseyedjavadi, O., Baase, W.A. & Matthews, B.W. (1993). The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. Science 262, 1715-1718.
    • (1993) Science , vol.262 , pp. 1715-1718
    • Baldwin, E.P.1    Hajiseyedjavadi, O.2    Baase, W.A.3    Matthews, B.W.4
  • 18
    • 0028608066 scopus 로고
    • Redesigning the hydrophobic core of a four-helix-bundle protein
    • Munson, M., O'Brien, R., Sturtevant, J.M. & Regan, L. (1994). Redesigning the hydrophobic core of a four-helix-bundle protein. Protein Sci. 3, 2015-2022.
    • (1994) Protein Sci. , vol.3 , pp. 2015-2022
    • Munson, M.1    O'Brien, R.2    Sturtevant, J.M.3    Regan, L.4
  • 19
    • 0028858499 scopus 로고
    • De novo design of the hydrophobic cores of proteins
    • Desjarlais, J.R. & Handel, T.M. (1995). De novo design of the hydrophobic cores of proteins. Protein Sci. 4, 2006-2018.
    • (1995) Protein Sci. , vol.4 , pp. 2006-2018
    • Desjarlais, J.R.1    Handel, T.M.2
  • 20
    • 0029980972 scopus 로고    scopus 로고
    • Active barnase variants with completely random hydrophobic cores
    • in press
    • Axe, D.D., Foster, N.W. & Fersht, A. (1996). Active barnase variants with completely random hydrophobic cores. Proc. Natl. Acad. Sci. USA in press.
    • (1996) Proc. Natl. Acad. Sci. USA
    • Axe, D.D.1    Foster, N.W.2    Fersht, A.3
  • 21
    • 0028940706 scopus 로고
    • Critical side-chain interactions at a subunit interface in the Arc represser dimer
    • Milla, M.E. & Sauer, R.T. (1995). Critical side-chain interactions at a subunit interface in the Arc represser dimer. Biochemistry 34, 3344-3351.
    • (1995) Biochemistry , vol.34 , pp. 3344-3351
    • Milla, M.E.1    Sauer, R.T.2
  • 22
    • 0028147533 scopus 로고
    • The crystal structure of a mutant protein with altered but improved hydrophobic core packing
    • Lim, W.A., Hodel, A., Sauer, R.T. & Richards, P.M. (1994). The crystal structure of a mutant protein with altered but improved hydrophobic core packing. Proc. Natl. Acad. Sci. USA 91, 423-427.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 423-427
    • Lim, W.A.1    Hodel, A.2    Sauer, R.T.3    Richards, P.M.4
  • 23
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? a continuum electrostatic analysis
    • Hendsch, Z.S. & Tidor, B. (1994). Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci. 3, 211-226.
    • (1994) Protein Sci. , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 24
    • 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
  • 25
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity
    • Waldburger, C.D., Schildbach, J.F. & Sauer, R.T. (1995). Are buried salt bridges important for protein stability and conformational specificity. Nature Struct. Biol. 2, 122-128.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach, J.F.2    Sauer, R.T.3
  • 26
    • 0029966342 scopus 로고    scopus 로고
    • Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure
    • in press
    • Waldburger, C.D., Jonsson, T. & Sauer, R.T. (1996). Barriers to protein folding: formation of buried polar interactions is a slow step in acquisition of structure. Proc. Natl. Acad. Sci. USA in press.
    • (1996) Proc. Natl. Acad. Sci. USA
    • Waldburger, C.D.1    Jonsson, T.2    Sauer, R.T.3
  • 27
    • 0028882589 scopus 로고
    • P22 Arc repressor: Transition state properties inferred from mutational effects on the rates of protein unfolding and refolding
    • Milla, M.E., Brown, B.M., Waldburger, C.D. & Sauer, R.T. (1995). P22 Arc repressor: transition state properties inferred from mutational effects on the rates of protein unfolding and refolding. Biochemistry 34, 13914-13919.
    • (1995) Biochemistry , vol.34 , pp. 13914-13919
    • Milla, M.E.1    Brown, B.M.2    Waldburger, C.D.3    Sauer, R.T.4
  • 29
    • 0029868589 scopus 로고    scopus 로고
    • Nonlinear free energy relationships in Arc repressor unfolding imply existence of unstable, native-like folding intermediates
    • in press
    • Jonsson, T., Waldburger, C.D. & Sauer, R.T. (1996). Nonlinear free energy relationships in Arc repressor unfolding imply existence of unstable, native-like folding intermediates. Biochemistry in press.
    • (1996) Biochemistry
    • Jonsson, T.1    Waldburger, C.D.2    Sauer, R.T.3
  • 30
    • 0028218304 scopus 로고
    • Folded proteins occur frequently in libraries of random amino acid sequences
    • Davidson, A.R. & Sauer, R.T. (1994). Folded proteins occur frequently in libraries of random amino acid sequences. Proc. Natl. Acad. Sci. USA 91, 2146-2150.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2146-2150
    • Davidson, A.R.1    Sauer, R.T.2
  • 31
    • 0029120253 scopus 로고
    • Cooperatively folded proteins in random sequence libraries
    • Davidson, A.R., Lumb, K.J. & Sauer, R.T. (1995). Cooperatively folded proteins in random sequence libraries. Nature Struct. Biol. 2, 856-863.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 856-863
    • Davidson, A.R.1    Lumb, K.J.2    Sauer, R.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.