메뉴 건너뛰기




Volumn 3, Issue 5, 1996, Pages 446-451

In vitro evolution of thermodynamically stable turns

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; BETA CHAIN; EVOLUTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; REVIEW; THERMODYNAMICS;

EID: 0029926618     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0596-446     Document Type: Review
Times cited : (80)

References (15)
  • 2
    • 0024556397 scopus 로고
    • Transfer of a β-turn structure to a new protein context
    • Hynes, T.R., Kautz, R.A., Goodman, M.A., Gill, J.F. & Fox, R.O. Transfer of a β-turn structure to a new protein context. Nature 339, 73-76 (1989).
    • (1989) Nature , vol.339 , pp. 73-76
    • Hynes, T.R.1    Kautz, R.A.2    Goodman, M.A.3    Gill, J.F.4    Fox, R.O.5
  • 3
    • 0030062459 scopus 로고    scopus 로고
    • Amino-acid substitutions in a surface turn modulate protein stability
    • Predki, P.F., Agrawal V., Trunger, A.T. & Regan, L. Amino-acid substitutions in a surface turn modulate protein stability. Nature Struct. Biol. 3, 54-58 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 54-58
    • Predki, P.F.1    Agrawal, V.2    Trunger, A.T.3    Regan, L.4
  • 4
    • 0024293204 scopus 로고
    • Conformation of peptide fragments of proteins in aqueous solution: Implications for initiation of protein folding
    • Wright, P.E., Dyson, J.H. & Lerner, R.A. Conformation of peptide fragments of proteins in aqueous solution: Implications for initiation of protein folding. Biochemistry 27, 7167-7175 (1988).
    • (1988) Biochemistry , vol.27 , pp. 7167-7175
    • Wright, P.E.1    Dyson, J.H.2    Lerner, R.A.3
  • 5
    • 0001610538 scopus 로고
    • Chain reversals in model peptides: Studies of cystine-containing cyclic peptides I. Conformational free energies of cyclizationof hexapeptides of sequence Ac-Cys-X-Pro-Gly-Y-Cvs-NHMe
    • Milburn, P.J., Konishi, Y., Meiwald, Y.C. & Scheraga, H.A. Chain reversals in model peptides: Studies of cystine-containing cyclic peptides I. Conformational free energies of cyclizationof hexapeptides of sequence Ac-Cys-X-Pro-Gly-Y-Cvs-NHMe. J. Am. Chem. Soc. 109, 4486-4496 (1987).
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 4486-4496
    • Milburn, P.J.1    Konishi, Y.2    Meiwald, Y.C.3    Scheraga, H.A.4
  • 6
    • 0030020571 scopus 로고    scopus 로고
    • Are turns required for the folding of ribonuclease T1?
    • Garrett, J.B., Mullins, L.S. & Raushel, F.M. Are turns required for the folding of ribonuclease T1? Prot. Sci. 5, 204-211 (1996).
    • (1996) Prot. Sci. , vol.5 , pp. 204-211
    • Garrett, J.B.1    Mullins, L.S.2    Raushel, F.M.3
  • 7
    • 0028856717 scopus 로고
    • Destabilizing loop swaps in the CDRs of an immunoglobulin VL domain
    • Helms, L.R. & Wetzel, R. Destabilizing loop swaps in the CDRs of an immunoglobulin VL domain. Prot. Sci. 4, 2073-2081 (1995).
    • (1995) Prot. Sci. , vol.4 , pp. 2073-2081
    • Helms, L.R.1    Wetzel, R.2
  • 8
    • 0027265713 scopus 로고
    • The role of turns in the structure of an α-helical protein
    • Brunet, A.P. et al. The role of turns in the structure of an α-helical protein. Nature 364, 355-358 (1993).
    • (1993) Nature , vol.364 , pp. 355-358
    • Brunet, A.P.1
  • 9
    • 0028284549 scopus 로고
    • Linking an easily detectable phenotype to the folding of a common structural motif. Selection of rare turn mutations that prevent the folding of Rop
    • Castagnoli, L., Vetriani, C. & Cesareni, G. Linking an easily detectable phenotype to the folding of a common structural motif. Selection of rare turn mutations that prevent the folding of Rop. J. Mol. Biol. 237, 378-387 (1994).
    • (1994) J. Mol. Biol. , vol.237 , pp. 378-387
    • Castagnoli, L.1    Vetriani, C.2    Cesareni, G.3
  • 10
    • 0028518995 scopus 로고
    • Restored heptad pattern continuity does not alter the folding of four α-helix bundle
    • Vlassi, M. et al. Restored heptad pattern continuity does not alter the folding of four α-helix bundle. Nature Struct. Biol. 1, 705-716 (1994).
    • (1994) Nature Struct. Biol. , vol.1 , pp. 705-716
    • Vlassi, M.1
  • 11
    • 0028932770 scopus 로고
    • The order of secondary structure elements does not determine the stucture of a protein but does affect its folding kinetics
    • Viguera, A.R., Blanco, F.J. & Serrano, L. The order of secondary structure elements does not determine the stucture of a protein but does affect its folding kinetics. J. Mol. Biol. 247, 670-681 (1995).
    • (1995) J. Mol. Biol. , vol.247 , pp. 670-681
    • Viguera, A.R.1    Blanco, F.J.2    Serrano, L.3
  • 12
    • 0027328752 scopus 로고
    • Structure and genetic analysis of protein folding and stability
    • Matthews, B.W. Structure and genetic analysis of protein folding and stability. Curr. Opin. Struct Biol. 3, 589-593 (1993).
    • (1993) Curr. Opin. Struct Biol. , vol.3 , pp. 589-593
    • Matthews, B.W.1
  • 13
    • 0025720536 scopus 로고
    • Effect of heme binding on the structure and stability of Escherichia coli apocytochromeb562
    • Feng, Y. & Sugar, S.G. Effect of heme binding on the structure and stability of Escherichia coli apocytochromeb562. Biochemistry 30, 10150-10155 (1991).
    • (1991) Biochemistry , vol.30 , pp. 10150-10155
    • Feng, Y.1    Sugar, S.G.2
  • 14
    • 0028821194 scopus 로고
    • Thermodynamic genetics of the folding of the B1 immunoglobin-binding domain from streptococcal protein G
    • O'Neil, K. T. Hoess, R.H., Raleigh, D.P. & DeGrado, W.F. Thermodynamic genetics of the folding of the B1 immunoglobin-binding domain from streptococcal protein G. Proteins, Struct. Funct. Genet. 21, 11-21 (1995).
    • (1995) Proteins, Struct. Funct. Genet. , vol.21 , pp. 11-21
    • O'Neil, K.T.1    Hoess, R.H.2    Raleigh, D.P.3    DeGrado, W.F.4
  • 15
    • 0028049177 scopus 로고
    • The thermodynamic effects of protein mutations
    • Sturtevant, J.M. The thermodynamic effects of protein mutations. Curr. Opin. Struct. Biol. 4, 69-78 (1994).
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 69-78
    • Sturtevant, J.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.