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Volumn 9, Issue 4, 1998, Pages 350-353

Helical protein design

Author keywords

[No Author keywords available]

Indexed keywords

PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SHORT SURVEY;

EID: 0032146407     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(98)80006-2     Document Type: Article
Times cited : (17)

References (38)
  • 1
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill KA, Chan HS. From Levinthal to pathways to funnels. Nat Struct Biol. 4:1997;10-19.
    • (1997) Nat Struct Biol , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 2
    • 0030593029 scopus 로고    scopus 로고
    • Design of a monomeric 23-residue polypeptide with defined tertiary structure
    • Struthers MD, Cheng RP, Imperiali B. Design of a monomeric 23-residue polypeptide with defined tertiary structure. Science. 271:1996;342-345.
    • (1996) Science , vol.271 , pp. 342-345
    • Struthers, M.D.1    Cheng, R.P.2    Imperiali, B.3
  • 3
    • 0029157648 scopus 로고
    • A de novo designed protein mimics the native state of natural proteins
    • Raleigh DP, Betz SF, DeGrado WF. A de novo designed protein mimics the native state of natural proteins. J Am Chem Soc. 117:1995;7558-7559.
    • (1995) J Am Chem Soc , vol.117 , pp. 7558-7559
    • Raleigh, D.P.1    Betz, S.F.2    DeGrado, W.F.3
  • 5
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection [see comments]
    • Dahiyat BI, Mayo SL. De novo protein design: fully automated sequence selection [see comments]. Science. 278:1997;82-87.
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 6
    • 0016352763 scopus 로고
    • Hydrophobic bonding and accessible surface area in proteins
    • Chothia C. Hydrophobic bonding and accessible surface area in proteins. Nature. 248:1974;338-339.
    • (1974) Nature , vol.248 , pp. 338-339
    • Chothia, C.1
  • 7
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA. Dominant forces in protein folding. Biochemistry. 29:1990;7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 9
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occuring amino acids
    • O'Neil KT, DeGrado WF. A thermodynamic scale for the helix-forming tendencies of the commonly occuring amino acids. Science. 250:1990;646-650.
    • (1990) Science , vol.250 , pp. 646-650
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 10
    • 0001079105 scopus 로고
    • On the use of sequence homologies to predict protein structure: Identical pentapeptides can have completely different conformations
    • Kabsch W, Sander C. On the use of sequence homologies to predict protein structure: identical pentapeptides can have completely different conformations. Proc Natl Acad Sci USA. 81:1984;1075-1078.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 1075-1078
    • Kabsch, W.1    Sander, C.2
  • 11
    • 0023193211 scopus 로고
    • Analysis of sequence-similar pentapeptides in unrelated protein tertiary structures
    • Argos P. Analysis of sequence-similar pentapeptides in unrelated protein tertiary structures. J Mol Biol. 197:1987;331-348.
    • (1987) J Mol Biol , vol.197 , pp. 331-348
    • Argos, P.1
  • 12
    • 0027448801 scopus 로고
    • Origins of structural diversity within sequentially identical hexapeptides
    • Cohen BI, Presnell SR, Cohen FE. Origins of structural diversity within sequentially identical hexapeptides. Protein Sci. 2:1993;2134-2145.
    • (1993) Protein Sci , vol.2 , pp. 2134-2145
    • Cohen, B.I.1    Presnell, S.R.2    Cohen, F.E.3
  • 13
    • 0029865623 scopus 로고    scopus 로고
    • Context-dependent secondary structure formation of a designed protein sequence
    • Minor DL Jr, Kim PS. Context-dependent secondary structure formation of a designed protein sequence. Nature. 380:1996;730-734.
    • (1996) Nature , vol.380 , pp. 730-734
    • Minor D.L., Jr.1    Kim, P.S.2
  • 15
    • 0023812695 scopus 로고
    • Characterization of a helical protein designed from first principles
    • Regan L, DeGrado WF. Characterization of a helical protein designed from first principles. Science. 241:1988;976-978.
    • (1988) Science , vol.241 , pp. 976-978
    • Regan, L.1    DeGrado, W.F.2
  • 17
    • 0027177971 scopus 로고
    • Metal ion-dependent modulation of the dynamics of a designed protein
    • Handel TM, Williams SA, DeGrado WF. Metal ion-dependent modulation of the dynamics of a designed protein. Science. 261:1993;879-885.
    • (1993) Science , vol.261 , pp. 879-885
    • Handel, T.M.1    Williams, S.A.2    DeGrado, W.F.3
  • 18
    • 0025040232 scopus 로고
    • De novo design expression and characterization of Felix: A four-helix bundle protein of native-like sequence
    • Hecht MH, Richardson JS, Richardson DC, Ogden RC. De novo design expression and characterization of Felix: a four-helix bundle protein of native-like sequence. Science. 249:1990;884-891.
    • (1990) Science , vol.249 , pp. 884-891
    • Hecht, M.H.1    Richardson, J.S.2    Richardson, D.C.3    Ogden, R.C.4
  • 19
    • 23444436172 scopus 로고
    • Protein design by binary patterning of polar and nonpolar amino acids [see comments]
    • Kamtekar S, Schiffer JM, Xiong H, Babik JM, Hecht MH. Protein design by binary patterning of polar and nonpolar amino acids [see comments]. Science. 262:1993;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
  • 20
    • 0030878180 scopus 로고    scopus 로고
    • A protein designed by binary patterning of polar and nonpolar amino acids displays native-like properties
    • Roy S, Ratnaswamy G, Boice JA, Fairman R, McLendon G, Hecht MH. A protein designed by binary patterning of polar and nonpolar amino acids displays native-like properties. J Am Chem Soc. 119:1997;5302-5306.
    • (1997) J Am Chem Soc , vol.119 , pp. 5302-5306
    • Roy, S.1    Ratnaswamy, G.2    Boice, J.A.3    Fairman, R.4    McLendon, G.5    Hecht, M.H.6
  • 21
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled-coils
    • Crick FHC. The packing of α-helices: simple coiled-coils. Acta Crystallogr. 6:1953;689.
    • (1953) Acta Crystallogr , vol.6 , pp. 689
    • Crick, F.H.C.1
  • 22
    • 0027686674 scopus 로고
    • Structure at 2.5 Å of a designed peptide that maintains solubility of membrane proteins
    • Schafmeister CE, Miercke LJ, Stroud RM. Structure at 2.5 Å of a designed peptide that maintains solubility of membrane proteins. Science. 262:1993;734-738.
    • (1993) Science , vol.262 , pp. 734-738
    • Schafmeister, C.E.1    Miercke, L.J.2    Stroud, R.M.3
  • 23
    • 0027756896 scopus 로고
    • A switch between two-, three- and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury PB, Zhang T, Kim PS, Alber T. A switch between two-, three- and four-stranded coiled coils in GCN4 leucine zipper mutants. Science. 262:1993;1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 24
    • 0028858499 scopus 로고
    • De novo design of the hydrophobic cores of proteins
    • Desjarlais JR, Handel TM. De novo design of the hydrophobic cores of proteins. Protein Sci. 4:1995;2006-2018.
    • (1995) Protein Sci , vol.4 , pp. 2006-2018
    • Desjarlais, J.R.1    Handel, T.M.2
  • 25
    • 0030992890 scopus 로고    scopus 로고
    • De novo design of the hydrophobic core of ubiquitin
    • Lazar GA, Desjarlais JR, Handel TM. De novo design of the hydrophobic core of ubiquitin. Protein Sci. 6:1997;1167-1178.
    • (1997) Protein Sci , vol.6 , pp. 1167-1178
    • Lazar, G.A.1    Desjarlais, J.R.2    Handel, T.M.3
  • 26
    • 0031558762 scopus 로고    scopus 로고
    • De novo protein design: Towards fully automated sequence selection
    • Dahiyat BI, Sarisky CA, Mayo SL. De novo protein design: towards fully automated sequence selection. J Mol Biol. 273:1997;789-796.
    • (1997) J Mol Biol , vol.273 , pp. 789-796
    • Dahiyat, B.I.1    Sarisky, C.A.2    Mayo, S.L.3
  • 27
    • 0030987610 scopus 로고    scopus 로고
    • Probing the role of packing specificity in protein design
    • Dahiyat BI, Mayo SL. Probing the role of packing specificity in protein design. Proc Natl Acad Sci USA. 94:1997;10172-10177.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10172-10177
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 28
    • 0343742614 scopus 로고    scopus 로고
    • Automated design of the surface positions of protein helices
    • Dahiyat BI, Gordon DB, Mayo SL. Automated design of the surface positions of protein helices. Protein Sci. 6:1997;1333-1337.
    • (1997) Protein Sci , vol.6 , pp. 1333-1337
    • Dahiyat, B.I.1    Gordon, D.B.2    Mayo, S.L.3
  • 29
    • 0029920337 scopus 로고    scopus 로고
    • Protein design automation
    • Dahiyat BI, Mayo SL. Protein design automation. Protein Sci. 5:1996;895-903.
    • (1996) Protein Sci , vol.5 , pp. 895-903
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 30
    • 0026589733 scopus 로고
    • The dead-end elimination theorem and its use in protein side-chain positioning
    • Desmet J, Demaeyer M, Hazes B, Lasters I. The dead-end elimination theorem and its use in protein side-chain positioning. Nature. 356:1992;539-542.
    • (1992) Nature , vol.356 , pp. 539-542
    • Desmet, J.1    Demaeyer, M.2    Hazes, B.3    Lasters, I.4
  • 32
    • 0031892699 scopus 로고    scopus 로고
    • Exploring sequence constraints on an interhelical turn using in vivo selection for catalytic activity
    • MacBeath G, Kast P, Hilvert D. Exploring sequence constraints on an interhelical turn using in vivo selection for catalytic activity. Protein Sci. 7:1998;325-335.
    • (1998) Protein Sci , vol.7 , pp. 325-335
    • MacBeath, G.1    Kast, P.2    Hilvert, D.3
  • 33
    • 0032549781 scopus 로고    scopus 로고
    • Redesigning enzyme topology by directed evolution
    • MacBeath G, Kast P, Hilvert D. Redesigning enzyme topology by directed evolution. Science. 279:1998;1958-1961.
    • (1998) Science , vol.279 , pp. 1958-1961
    • MacBeath, G.1    Kast, P.2    Hilvert, D.3
  • 34
    • 0030623398 scopus 로고    scopus 로고
    • An inverse correlation between loop length and stability in a four-helix-bundle protein
    • Nagi AD, Regan L. An inverse correlation between loop length and stability in a four-helix-bundle protein. Fold Des. 2:1997;67-75.
    • (1997) Fold Des , vol.2 , pp. 67-75
    • Nagi, A.D.1    Regan, L.2
  • 35
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of (alpha) helices
    • Richardson JS, Richardson DC. Amino acid preferences for specific locations at the ends of (alpha) helices. Science. 240:1988;1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 38
    • 0043224256 scopus 로고    scopus 로고
    • Engineering cyclophilin into a proline-specific endopeptidase
    • Quéméneur E, Moutiez M, Charbonnier J-B, Ménez A. Engineering cyclophilin into a proline-specific endopeptidase. Nature. 391:1998;301-304.
    • (1998) Nature , vol.391 , pp. 301-304
    • Quéméneur, E.1    Moutiez, M.2    Charbonnier, J.-B.3    Ménez, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.