메뉴 건너뛰기




Volumn 8, Issue 4, 1998, Pages 466-470

Functionalization of designed folded polypeptides

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPEPTIDE; HEME; METAL ION; PEPTIDE; POLYPEPTIDE;

EID: 0032144119     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(98)80124-3     Document Type: Article
Times cited : (33)

References (34)
  • 1
    • 17344363384 scopus 로고    scopus 로고
    • 2D, a native like de novo designed protein
    • of special interest. The first high resolution NMR spectroscopy structure of a designed protein of complexity discloses the key principles that control the packing of the hydrophobic core.
    • 2D, a native like de novo designed protein. of special interest J Am Chem Soc. 120:1998;1138-1145 The first high resolution NMR spectroscopy structure of a designed protein of complexity discloses the key principles that control the packing of the hydrophobic core.
    • (1998) J Am Chem Soc , vol.120 , pp. 1138-1145
    • Hill, R.B.1    Degrado, W.F.2
  • 3
    • 0030885116 scopus 로고    scopus 로고
    • Structure and function of an aromatic ensemble that restricts the dynamics of the hydrophobic core of a designed helix-loop-helix dimer
    • Brive L, Dolphin GT, Baltzer L. Structure and function of an aromatic ensemble that restricts the dynamics of the hydrophobic core of a designed helix-loop-helix dimer. J Am Chem Soc. 119:1997;8596-8607.
    • (1997) J Am Chem Soc , vol.119 , pp. 8596-8607
    • Brive, L.1    Dolphin, G.T.2    Baltzer, L.3
  • 4
    • 0029899119 scopus 로고    scopus 로고
    • Controlling topology and native-like behavior of de novo-designed peptides: Design and characterization of antiparallel four-stranded coiled coils
    • Betz SF, DeGrado WF. Controlling topology and native-like behavior of de novo-designed peptides: design and characterization of antiparallel four-stranded coiled coils. Biochemistry. 35:1996;6955-6962.
    • (1996) Biochemistry , vol.35 , pp. 6955-6962
    • Betz, S.F.1    Degrado, W.F.2
  • 6
    • 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
  • 7
    • 0002543810 scopus 로고    scopus 로고
    • Design and NMR analyses of compact, independently folded BBA motifs
    • Struthers M, Ottesen JJ, Imperiali B. Design and NMR analyses of compact, independently folded BBA motifs. Fold Des. 3:1998;95-103.
    • (1998) Fold des , vol.3 , pp. 95-103
    • Struthers, M.1    Ottesen, J.J.2    Imperiali, B.3
  • 8
    • 0030631493 scopus 로고    scopus 로고
    • The pH-dependent tertiary structure of a designed helix-loop-helix dimer
    • Dolphin GT, Baltzer L. The pH-dependent tertiary structure of a designed helix-loop-helix dimer. Fold Des. 2:1997;319-330.
    • (1997) Fold des , vol.2 , pp. 319-330
    • Dolphin, G.T.1    Baltzer, L.2
  • 9
    • 0029790914 scopus 로고
    • Synthesis of glycopeptides and lipopeptides by chemoselective ligation
    • Cervigni SE, Dumy P, Mutter M. Synthesis of glycopeptides and lipopeptides by chemoselective ligation. Angew Chem Int Ed. 35:1995;1230-1232.
    • (1995) Angew Chem Int Ed , vol.35 , pp. 1230-1232
    • Cervigni, S.E.1    Dumy, P.2    Mutter, M.3
  • 10
    • 0002746714 scopus 로고    scopus 로고
    • Polypeptides with supersecondary structures as templates in rational catalyst design. Catalysis of self functionalization by designed helix-loop-helix motifs
    • Baltzer L, Lundh A-C, Broo K, Olofsson S, Ahlberg P. Polypeptides with supersecondary structures as templates in rational catalyst design. Catalysis of self functionalization by designed helix-loop-helix motifs. J Chem Soc Perkin Trans 2. 1996;1671-1676.
    • (1996) J Chem Soc Perkin Trans 2 , pp. 1671-1676
    • Baltzer, L.1    Lundh A-C2    Broo, K.3    Olofsson, S.4    Ahlberg, P.5
  • 11
    • 0029789894 scopus 로고    scopus 로고
    • The mechanism of self-catalyzed site-selective functionalization of a designed helix-loop-helix motif
    • Broo K, Brive L, Lundh A-C, Ahlberg P, Baltzer L. The mechanism of self-catalyzed site-selective functionalization of a designed helix-loop-helix motif. J Am Chem Soc. 118:1996;8172-8173.
    • (1996) J Am Chem Soc , vol.118 , pp. 8172-8173
    • Broo, K.1    Brive, L.2    Lundh A-C3    Ahlberg, P.4    Baltzer, L.5
  • 12
    • 0027453389 scopus 로고
    • Synthesis, structure and activity of artificial, rationally designed catalytic polypeptides
    • Johnsson K, Allemann RK, Widmer H, Benner SA. Synthesis, structure and activity of artificial, rationally designed catalytic polypeptides. Nature. 365:1993;530-532.
    • (1993) Nature , vol.365 , pp. 530-532
    • Johnsson, K.1    Allemann, R.K.2    Widmer, H.3    Benner, S.A.4
  • 13
    • 0030700484 scopus 로고    scopus 로고
    • A synthetic peptide ligase
    • of special interest. A new principle in catalyst design is successfully explored and the design, synthesis and function of a novel catalyst is presented. Specificity is introduced in a rational way.
    • Severin K, Lee DH, Kennan AJ, Ghadiri MR. A synthetic peptide ligase. of special interest Nature. 389:1997;706-709 A new principle in catalyst design is successfully explored and the design, synthesis and function of a novel catalyst is presented. Specificity is introduced in a rational way.
    • (1997) Nature , vol.389 , pp. 706-709
    • Severin, K.1    Lee, D.H.2    Kennan, A.J.3    Ghadiri, M.R.4
  • 15
    • 0031587461 scopus 로고    scopus 로고
    • Catalysis of hydrolysis and transesterification reactions of p-nitrophenyl esters by a designed helix-loop-helix dimer
    • of special interest. Histidine-based catalysts are introduced into the field of catalyst design. The structure and function of a catalytic four-helix bundle motif is presented.
    • Broo KS, Brive L, Ahlberg P, Baltzer L. Catalysis of hydrolysis and transesterification reactions of p-nitrophenyl esters by a designed helix-loop-helix dimer. of special interest J Am Chem Soc. 119:1997;11362-11372 Histidine-based catalysts are introduced into the field of catalyst design. The structure and function of a catalytic four-helix bundle motif is presented.
    • (1997) J Am Chem Soc , vol.119 , pp. 11362-11372
    • Broo, K.S.1    Brive, L.2    Ahlberg, P.3    Baltzer, L.4
  • 17
    • 0031442682 scopus 로고    scopus 로고
    • Emergence of symbiosis in peptide self-replication through a hypercyclic
    • Lee DH, Severin K, Yokobayashi Y, Ghadiri MR. Emergence of symbiosis in peptide self-replication through a hypercyclic. Nature. 390:1997;591-594.
    • (1997) Nature , vol.390 , pp. 591-594
    • Lee, D.H.1    Severin, K.2    Yokobayashi, Y.3    Ghadiri, M.R.4
  • 20
    • 0032490082 scopus 로고    scopus 로고
    • +-His pair and arginine transition state binding in catalysis of ester hydrolysis reactions by designed helix-loop-helix motifs
    • +-His pair and arginine transition state binding in catalysis of ester hydrolysis reactions by designed helix-loop-helix motifs. J Am Chem Soc. 120:1998;4063-4068.
    • (1998) J Am Chem Soc , vol.120 , pp. 4063-4068
    • Broo, K.S.1    Nilsson, H.2    Nilssor, J.3    Flodberg, A.4    Baltzer, L.5
  • 21
    • 0032517335 scopus 로고    scopus 로고
    • Substrate recognition and saturation kinetics in de novo designed histidine-based four-helix bundle catalysts
    • of special interest
    • Broo KS, Nilsson H, Nilsson J, Baltzer L. Substrate recognition and saturation kinetics in de novo designed histidine-based four-helix bundle catalysts. of special interest J Am Chem Soc. 1998; The authors present the rational design of a catalyst that is capable of substrate recognition, leading to substrate binding and saturation kinetics, and the recognition of charged and hydrophobic residues.
    • (1998) J Am Chem Soc
    • Broo, K.S.1    Nilsson, H.2    Nilsson, J.3    Baltzer, L.4
  • 22
    • 0031867874 scopus 로고    scopus 로고
    • Site-selective control of the reactivity of surface exposed histidine residues in designed four-helix bundle catalysts
    • Broo KS, Brive L, Sott RS, Baltzer L. Site-selective control of the reactivity of surface exposed histidine residues in designed four-helix bundle catalysts. Fold Des. 3:1998;303-312.
    • (1998) Fold des , vol.3 , pp. 303-312
    • Broo, K.S.1    Brive, L.2    Sott, R.S.3    Baltzer, L.4
  • 23
    • 0030874443 scopus 로고    scopus 로고
    • De novo design of mercury-binding two- and three-helical bundles
    • of special interest. The first demonstration of the control of metal-ion coordination by folded polypeptides suggests that the binding energy obtained in peptide folding can be exploited for the engineering of novel and unusual properties in designed metalloproteins.
    • Dieckmann GR, McRorie DK, Tierney DL, Utschig LM, Singer CP, O'Halloran TV, Penner-Hahn JE, DeGrado WF, Pecoraro VL. De novo design of mercury-binding two- and three-helical bundles. of special interest J Am Chem Soc. 119:1997;6195-6196 The first demonstration of the control of metal-ion coordination by folded polypeptides suggests that the binding energy obtained in peptide folding can be exploited for the engineering of novel and unusual properties in designed metalloproteins.
    • (1997) J Am Chem Soc , vol.119 , pp. 6195-6196
    • Dieckmann, G.R.1    McRorie, D.K.2    Tierney, D.L.3    Utschig, L.M.4    Singer, C.P.5    O'Halloran, T.V.6    Penner-Hahn, J.E.7    Degrado, W.F.8    Pecoraro, V.L.9
  • 24
    • 0032542575 scopus 로고    scopus 로고
    • Metal ion induced folding of a de novo designed coiled-coil peptide
    • Kohn WD, Kay CM, Sykes BD, Hodges RS. Metal ion induced folding of a de novo designed coiled-coil peptide. J Am Chem Soc. 120:1998;1124-1132.
    • (1998) J Am Chem Soc , vol.120 , pp. 1124-1132
    • Kohn, W.D.1    Kay, C.M.2    Sykes, B.D.3    Hodges, R.S.4
  • 25
    • 0032584314 scopus 로고    scopus 로고
    • Effect of four helix bundle topology on heme binding and redox properties
    • of special interest. The authors describe a highly complex designed protein that binds four hemes and induces different redox properties in each one. Based on a designed apo-protein with a well-defined tertiary structure, this model system promises to allow a thorough investigation of structure and function.
    • Gibney BR, Rabanal F, Reddy KS, Dutton PL. Effect of four helix bundle topology on heme binding and redox properties. of special interest Biochemistry. 37:1998;4635-4643 The authors describe a highly complex designed protein that binds four hemes and induces different redox properties in each one. Based on a designed apo-protein with a well-defined tertiary structure, this model system promises to allow a thorough investigation of structure and function.
    • (1998) Biochemistry , vol.37 , pp. 4635-4643
    • Gibney, B.R.1    Rabanal, F.2    Reddy, K.S.3    Dutton, P.L.4
  • 26
    • 0030961554 scopus 로고    scopus 로고
    • Hemoprotein models based on a covalent helix-heme-helix sandwich 1. Design, synthesis and characterisation
    • Nastri F, Lombardi A, Morelli G, Maglio O, D'Auria G, Pedone C, Pavone V. Hemoprotein models based on a covalent helix-heme-helix sandwich 1. Design, synthesis and characterisation. Chemistry Eur J. 3:1997;340-349.
    • (1997) Chemistry Eur J , vol.3 , pp. 340-349
    • Nastri, F.1    Lombardi, A.2    Morelli, G.3    Maglio, O.4    D'Auria, G.5    Pedone, C.6    Pavone, V.7
  • 29
    • 0032573867 scopus 로고    scopus 로고
    • Design, synthesis and properties of a novel cytochrome b model
    • Rau HK, Haehnel W. Design, synthesis and properties of a novel cytochrome b model. J Am Chem Soc. 120:1998;468-476.
    • (1998) J Am Chem Soc , vol.120 , pp. 468-476
    • Rau, H.K.1    Haehnel, W.2
  • 32
    • 0002806726 scopus 로고    scopus 로고
    • Non-covalent control of site-selective incorporation of the pyridoxal phosphate cofactor into a folded polypeptide motif - mimicking a key step in enzymatic transamination
    • Allert M, Kjellstrand M, Broo K, Nilsson A, Baltzer L. Non-covalent control of site-selective incorporation of the pyridoxal phosphate cofactor into a folded polypeptide motif - mimicking a key step in enzymatic transamination. Chem Commun. 1998;1547-1548.
    • (1998) Chem Commun , pp. 1547-1548
    • Allert, M.1    Kjellstrand, M.2    Broo, K.3    Nilsson, A.4    Baltzer, L.5
  • 33
    • 0032192431 scopus 로고    scopus 로고
    • Chemo- and stereoselective glycosylation of hydroxylamine derivatives: A versatile approach to glycoconjugates
    • in press
    • Peri F, Dumy P, Mutter M. Chemo- and stereoselective glycosylation of hydroxylamine derivatives: a versatile approach to glycoconjugates. Tetrahedron. 1998;. in press.
    • (1998) Tetrahedron
    • Peri, F.1    Dumy, P.2    Mutter, M.3
  • 34
    • 0003305648 scopus 로고    scopus 로고
    • The site-selective glycosylation of a designed helix-loop-helix polypeptide motif
    • Andersson L, Stenhagen G, Baltzer L. The site-selective glycosylation of a designed helix-loop-helix polypeptide motif. J Org Chem. 63:1998;1366-1367.
    • (1998) J Org Chem , vol.63 , pp. 1366-1367
    • Andersson, L.1    Stenhagen, G.2    Baltzer, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.