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Volumn 1, Issue , 2008, Pages 445-453

A Guide to Measuring and Interpreting Φ-values

Author keywords

Deletions; Measuring; Mutations; Thermodynamic data; Tools

Indexed keywords


EID: 84889792013     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527619498.ch13     Document Type: Chapter
Times cited : (1)

References (19)
  • 1
    • 0026511656 scopus 로고
    • The folding of an enzyme I. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht, A. R., Matouschek, A. & Serrano, L. The folding of an enzyme I. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 224, 771-782 (1992).
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 2
    • 0022443598 scopus 로고
    • Quantitative-analysis of structure activity relationships in engineered proteins by linear freeenergy relationships
    • Fersht, A. R., Leatherbarrow, R. J. & Wells, T. N. Quantitative-analysis of structure activity relationships in engineered proteins by linear freeenergy relationships. Nature 322, 284-286 (1986).
    • (1986) Nature , vol.322 , pp. 284-286
    • Fersht, A.R.1    Leatherbarrow, R.J.2    Wells, T.N.3
  • 3
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding
    • Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding. J. Mol. Biol. 254, 260-288 (1995).
    • (1995) J. Mol. Biol. , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 4
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • Matouschek, A., Jr., Kellis, J. T. K., Serrano, L. & Fersht, A. R. Mapping the transition state and pathway of protein folding by protein engineering. Nature 340, 122-126 (1989).
    • (1989) Nature , vol.340 , pp. 122-126
    • Matouschek Jr., A.1    Kellis, J.T.K.2    Serrano, L.3    Fersht, A.R.4
  • 5
    • 0027948175 scopus 로고
    • Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding
    • Otzen, D. E., Itzhaki, L. S., ElMasry, N. F., Jackson, S. E. & Fersht, A. R. Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding. Proc. Natl Acad. Sci. USA 91, 10422-10425 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10422-10425
    • Otzen, D.E.1    Itzhaki, L.S.2    ElMasry, N.F.3    Jackson, S.E.4    Fersht, A.R.5
  • 7
    • 0023657031 scopus 로고
    • Dissection of the structure and activity of the tyrosyltRNA synthetase by site-directed mutagenesis
    • Fersht, A. R. Dissection of the structure and activity of the tyrosyltRNA synthetase by site-directed mutagenesis. Biochemistry 26, 8031-8037 (1987).
    • (1987) Biochemistry , vol.26 , pp. 8031-8037
    • Fersht, A.R.1
  • 8
    • 0003595276 scopus 로고    scopus 로고
    • Perspectives on Structure and Mechanism in Organic Chemistry
    • Brooks/Cole Publishing, London
    • Carroll, F. A. Perspectives on Structure and Mechanism in Organic Chemistry. Brooks/Cole Publishing, London (1998).
    • (1998)
    • Carroll, F.A.1
  • 9
    • 0027384577 scopus 로고
    • Effects of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2
    • Jackson, S. E., Moracci, M., El Masry, N., Johnson, C. M. & Fersht, A. R. Effects of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2. Biochemistry 32, 11259-11269 (1993).
    • (1993) Biochemistry , vol.32 , pp. 11259-11269
    • Jackson, S.E.1    Moracci, M.2    El Masry, N.3    Johnson, C.M.4    Fersht, A.R.5
  • 10
    • 0026516310 scopus 로고
    • Effect of alanine versus glycine in a-helices on protein stability
    • Serrano, L., Neira, J.-L., Sancho, J. & Fersht, A. R. Effect of alanine versus glycine in a-helices on protein stability. Nature 356, 453-455 (1992).
    • (1992) Nature , vol.356 , pp. 453-455
    • Serrano, L.1    Neira, J.-L.2    Sancho, J.3    Fersht, A.R.4
  • 12
    • 0028037217 scopus 로고
    • Single versus parallel pathways of protein folding and fractional formation of structure in the transition state
    • Fersht, A. R., Itzhaki, L. S., ElMasry, N. F., Matthews, J. M. & Otzen, D. E. Single versus parallel pathways of protein folding and fractional formation of structure in the transition state. Proc. Natl Acad. Sci. USA 91, 10426-10429 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10426-10429
    • Fersht, A.R.1    Itzhaki, L.S.2    ElMasry, N.F.3    Matthews, J.M.4    Otzen, D.E.5
  • 13
    • 0026354152 scopus 로고
    • Protein engineering in analysis of protein folding pathways and stability
    • Matouschek, A. & Fersht, A. R. Protein engineering in analysis of protein folding pathways and stability. Methods Enzymol. 202, 82-112 (1991).
    • (1991) Methods Enzymol. , vol.202 , pp. 82-112
    • Matouschek, A.1    Fersht, A.R.2
  • 14
    • 0037117477 scopus 로고    scopus 로고
    • Unspecific hydrophobic stabilization of folding transition states
    • Viguera, A. R., Vega, C. & Serrano, L. Unspecific hydrophobic stabilization of folding transition states. Proc. Natl Acad. Sci. USA 99, 5349-5354 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.99 , pp. 5349-5354
    • Viguera, A.R.1    Vega, C.2    Serrano, L.3
  • 15
    • 0036266942 scopus 로고    scopus 로고
    • Conformational strain in the hydrophobic core and its implications for protein folding and design
    • Ventura, S., Vega, M. C., Lacroix, E., Angrand, I., Spagnolo, L. & Serrano, L. Conformational strain in the hydrophobic core and its implications for protein folding and design. Nature Struct. Biol. 9, 485-493 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 485-493
    • Ventura, S.1    Vega, M.C.2    Lacroix, E.3    Angrand, I.4    Spagnolo, L.5    Serrano, L.6
  • 16
    • 0031472252 scopus 로고    scopus 로고
    • Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment: description of the folding pathway
    • Bond, C. J., Wong, K. B., Clarke, J., Fersht, A. R. & Daggett, V. Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment: description of the folding pathway. Proc. Natl Acad. Sci. USA 9, 13409-13413 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.9 , pp. 13409-13413
    • Bond, C.J.1    Wong, K.B.2    Clarke, J.3    Fersht, A.R.4    Daggett, V.5
  • 17
    • 0003818541 scopus 로고    scopus 로고
    • Structure and Mechanism in Protein Science
    • W.H. Freeman and Company, New York
    • Fersht, A. Structure and Mechanism in Protein Science. W.H. Freeman and Company, New York (1998).
    • (1998)
    • Fersht, A.1
  • 18
  • 19
    • 0037686252 scopus 로고    scopus 로고
    • The present view of the mechanism of protein folding
    • Daggett, V. & Fersht, A. R. The present view of the mechanism of protein folding. Nature Rev. Mol. Cell Biol. 4, 497-502 (2003).
    • (2003) Nature Rev. Mol. Cell Biol. , vol.4 , pp. 497-502
    • Daggett, V.1    Fersht, A.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.