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Volumn 8, Issue 5, 2007, Pages 567-573

Phosphorylation-induced conformational changes in short peptides probed by fluorescence resonance energy transfer in the 10 Å domain

Author keywords

FRET; Kinases; Peptides; Phosphorylation; Time resolved spectroscopy

Indexed keywords

2,3 DIAZABICYCLO[2.2.2]OCT 2 ENE; ALKENE DERIVATIVE; ASPARAGINE; PEPTIDE DERIVATIVE; POLYPEPTIDE; TRYPTOPHAN; TRYPTOPHYLLYSYLARGINYLTHREONINELEUCYLARGINYLARGINYL ASPARAGINE; TRYPTOPHYLLYSYLARGINYLTHREONYLLEUCYLARGINYLARGINYL ASPARAGINE; UNCLASSIFIED DRUG; ARGININE; PEPTIDE; PHOSPHATE; SERINE; THREONINE; WATER;

EID: 34447629057     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.200600466     Document Type: Article
Times cited : (25)

References (44)
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    • Fang Huang, University of Cambridge, has pointed out that a more accurate version of Equation (3) should take into account differences in R 0 values for the different Trp lifetime components, which have been related to different rotamers (cf. ref, 26, Assuming that the differences of the two lifetime components for the reference peptides ref-I and ref-II (factor of 2-3) affect the fluorescence quantum yields to the same extent, variations in the R0 values (square-root-of-6 dependence) of 12-20% could result, and the R0 values determined in Table 2 would lie in between. Such a refined analysis (which cannot be rigorously implemented due to lack of experimental data for the individual R0 values of the proposed Trp rotamers) could lead to slight estimated <10, variations in the recovered absolute distances, but would not affect the relative trends
    • 0 values of the proposed Trp rotamers) could lead to slight (estimated <10%) variations in the recovered absolute distances, but would not affect the relative trends.
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    • Fittings according to the worm-like chain model afforded the same relative trends in terms of variations in distances and chain flexibility persistence length
    • Fittings according to the worm-like chain model afforded the same relative trends in terms of variations in distances and chain flexibility (persistence length).
  • 36
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    • unpublished results
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  • 37
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    • CD measurements performed for peptides I, pI, II, and pII did not provide evidence for a stable secondary structure either (H. Sahoo, W. M. Nau, Indian J. Radiat. Res. 2006, 3, 104-112).
    • CD measurements performed for peptides I, pI, II, and pII did not provide evidence for a stable secondary structure either (H. Sahoo, W. M. Nau, Indian J. Radiat. Res. 2006, 3, 104-112).
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    • K. D. Collins, M. W. Washabaugh, Q. Rev. Biophys. 1985, 18, 323-422.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.