메뉴 건너뛰기




Volumn 4, Issue 10, 1997, Pages 805-809

Functional rapidly folding proteins from simplified amino acid sequences

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN SYNTHESIS; SEQUENCE ANALYSIS;

EID: 0030852463     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb1097-805     Document Type: Article
Times cited : (285)

References (28)
  • 1
    • 0028168562 scopus 로고
    • Design of a minimAl homeodomain: The N-terminal arm modulates DNA binding affinity and stabilizes homeodomain structure
    • Shang, Z. et al. Design of a minimAl homeodomain: the N-terminal arm modulates DNA binding affinity and stabilizes homeodomain structure. Proc. Natl. Acad. Sei. USA 91, 8373-8377 (1994).
    • (1994) Proc. Natl. Acad. Sei. USA , vol.91 , pp. 8373-8377
    • Shang, Z.1
  • 2
    • 0026552361 scopus 로고
    • Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrates the redundancy of information in an amino acid sequence
    • Heinz. D.W., Baase, W.A. & Matthews, B.W. Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrates the redundancy of information in an amino acid sequence. Proc. Natl. Acad. Sei. USA 89, 3751-3755 (1992).
    • (1992) Proc. Natl. Acad. Sei. USA , vol.89 , pp. 3751-3755
    • Heinz, D.W.1    Baase, W.A.2    Matthews, B.W.3
  • 3
    • 0023812695 scopus 로고
    • Charrterization of a helical protein designed from first principles
    • Regan, L & Degrade, W.F. Charrterization of a helical protein designed from first principles. Science 241, 976-978 (1988).
    • (1988) Science , vol.241 , pp. 976-978
    • Regan, L.1    Degrade, W.F.2
  • 4
    • 23444436172 scopus 로고
    • Protein design by binary patterning of polar and nonpolar amino acid sequences
    • Kamteker, S., Schiffer, J.M.. Xiong, H., Babik, J.M. & Hecht, M.H. Protein design by binary patterning of polar and nonpolar amino acid sequences. Science 262, 1680-1685(1993).
    • (1993) Science , vol.262 , pp. 1680-1685
    • Kamteker, S.1    Schiffer, J.M.2    Xiong, H.3    Babik, J.M.4    Hecht, M.H.5
  • 5
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • Scott, J.K. & Smith, G.P. Searching for peptide ligands with an epitope library. Science 249, 386-390 (1990).
    • (1990) Science , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 6
    • 0029004982 scopus 로고
    • A phage display system for studying the sequence determinants of protein folding
    • Gu, H. et al. A phage display system for studying the sequence determinants of protein folding. Prot. Sei. 4, 1108-1117 (1995).
    • (1995) Prot. Sei. , vol.4 , pp. 1108-1117
    • Gu, H.1
  • 7
    • 0027962645 scopus 로고
    • Two binding orientations for peptides to the src SH3 domain: Development of a general model for SH3 ligand interactions
    • Feng, S., Chen, J.K., Yu, H., Simon, J.A. & Schreiber, S.L. Two binding orientations for peptides to the src SH3 domain: development of a general model for SH3 ligand interactions. Science 266, 1241-1247 (1994).
    • (1994) Science , vol.266 , pp. 1241-1247
    • Feng, S.1    Chen, J.K.2    Yu, H.3    Simon, J.A.4    Schreiber, S.L.5
  • 8
  • 9
    • 0028410481 scopus 로고
    • Critical residues in an SH3 domain from Sem-5 suggest a mechanism for proline-rich peptide recognition
    • Lim, W.A. & Richards, P.M. Critical residues in an SH3 domain from Sem-5 suggest a mechanism for proline-rich peptide recognition. Nature Struct. Biol. 1, 221-225 (1994).
    • (1994) Nature Struct. Biol. , vol.1 , pp. 221-225
    • Lim, W.A.1    Richards, P.M.2
  • 10
    • 0027936659 scopus 로고
    • Characterization of the interaction of natural proline-rich peptides with five different SH3 domains
    • Viguera, A.R., Arrondo, J.L.R., Musacchio, A., Saraste. M. & Serrano, L. Characterization of the interaction of natural proline-rich peptides with five different SH3 domains. Biochemistry 33, 10925-10933 (1994).
    • (1994) Biochemistry , vol.33 , pp. 10925-10933
    • Viguera, A.R.1    Arrondo, J.L.R.2    Musacchio, A.3    Saraste, M.4    Serrano, L.5
  • 11
    • 0028286471 scopus 로고
    • Kinetics versus thermodynamics in protein folding
    • Baker, D. & Agard, D.A. Kinetics versus thermodynamics in protein folding. Biochemistry 33, 7505-7509 (1994).
    • (1994) Biochemistry , vol.33 , pp. 7505-7509
    • Baker, D.1    Agard, D.A.2
  • 12
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal, O Are there pathways for protein folding? J. Chim. Phys. 65, 44-45 (1968).
    • (1968) J. Chim. Phys. , vol.65 , pp. 44-45
    • Levinthal, O.1
  • 13
    • 0026605509 scopus 로고
    • A protein-folding reaction under kinetic control
    • Baker, D., Sohl, I.L.& Agard, D.A. A protein-folding reaction under kinetic control. Nature 356. 263-265 (1992).
    • (1992) Nature , vol.356 , pp. 263-265
    • Baker, D.1    Sohl, I.L.2    Agard, D.A.3
  • 15
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K.A. & Chan, H.S. From Levinthal to pathways to funnels. Nature Struct. Biol. 4, 10-19(1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 16
    • 0027177971 scopus 로고
    • Met al ion-dependent modulation of the dynamics of a designed protein
    • Handel, T.M., Williams, S.A. & DeGrado, W.F. Met al ion-dependent modulation of the dynamics of a designed protein. Sc/ence 261, 879-885 (1993).
    • (1993) Sc/ence , vol.261 , pp. 879-885
    • Handel, T.M.1    Williams, S.A.2    DeGrado, W.F.3
  • 18
    • 0014378880 scopus 로고
    • The origin of the genetic code. 1
    • Crick, F.H.C The origin of the genetic code. 1. Mol. Biol. 38, 367-379 (1958).
    • (1958) Mol. Biol. , vol.38 , pp. 367-379
    • Crick, F.H.C.1
  • 19
    • 0001155613 scopus 로고
    • A co-evolution theory of the genetic code
    • Wong, J.T. A co-evolution theory of the genetic code. Proc. Wat. Acad. Sei. USA 72, 1909-1912(1975).
    • (1975) Proc. Wat. Acad. Sei. USA , vol.72 , pp. 1909-1912
    • Wong, J.T.1
  • 20
    • 0026345258 scopus 로고
    • Random mutagenesis of protein sequences using oligonucleotide cassettes
    • Reidhaar-Olsen, J.F. ef al. Random mutagenesis of protein sequences using oligonucleotide cassettes. Methods Enzymol. 208, 564-586 (1991).
    • (1991) Methods Enzymol. , vol.208 , pp. 564-586
    • Reidhaar-Olsen, J.F.1
  • 22
    • 0030900533 scopus 로고    scopus 로고
    • Kinetics of folding of the IgG binding domain of peptostreptoccocal protein L
    • Scalley, M.L et al. Kinetics of folding of the IgG binding domain of peptostreptoccocal protein L Biochemistry 36, 3373-3382 (1997).
    • (1997) Biochemistry , vol.36 , pp. 3373-3382
    • Scalley, M.L.1
  • 23
    • 0027892193 scopus 로고
    • Biased combinatorial libraries: Novel ligands for the SH3 domain of phosphatidylinositol 3-kinase
    • Chen, J.K., Lane, W.S., Brauer, A., Tanaka. A. 8 Schreiber, S.L. Biased combinatorial libraries: novel ligands for the SH3 domain of phosphatidylinositol 3-kinase. I. Am. Chem. Soc. 115, 12591-12592 (1993).
    • (1993) I. Am. Chem. Soc. , vol.115 , pp. 12591-12592
    • Chen, J.K.1    Lane, W.S.2    Brauer, A.3    Tanaka, A.4    Schreiber, S.L.5
  • 25
    • 0027340025 scopus 로고
    • Structure of the PI3K SH3 domain and analysis of the SH3 family
    • Koyama, S. et al. Structure of the PI3K SH3 domain and analysis of the SH3 family. CeW 72, 945-952 (1993).
    • (1993) CeW , vol.72 , pp. 945-952
    • Koyama, S.1
  • 26
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 27
    • 0000913086 scopus 로고
    • A fast algorithm for rendering space-filling molecule pictures
    • Bacon. D. & Andersen, W.F. A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graphics 6, 219-220 (1988).
    • (1988) J. Mol. Graphics , vol.6 , pp. 219-220
    • Bacon, D.1    Andersen, W.F.2
  • 28
    • 0028057108 scopus 로고
    • Raster 3D Version 2.0 a program for photorealistic molecular graphics
    • Merritt, E.A. & Murphy, M.E. Raster 3D Version 2.0 A program for photorealistic molecular graphics. Atta Crystallogr. D50, 869-873 (1994).
    • (1994) Atta Crystallogr. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.