34 Model of doublecortin tandem --DCXDCXCC--DCXDCX
35 Structure of the N-terminal domain of doublecortin bbabbba3C-terma2b5b2a1b1b4b3
36 (deg cm2 dmol-1) x 106 (nm) Circular dichroism spectra of isolated domains andDCX-tandem of doublecortin (deg cm2 dmol-1) x 106TandemN-DCXC-DCX (nm)Measurements were performed in 50 mM phosphate, 300mM NaCl, pH 7.0, protein concentration: 50M
40 Analiza krzywej denaturacyjnej an+bn[GdmHCl] - intensywność fluorescencji stanu natywnegoau+bu[GdmHCl] - intensywność fluorescencji stanu zdenaturowanegom - zależność Gden od [GdmHCl]Gden - zmiana swobodnej entalpii denaturacji
41 Denaturacja termiczna FGF Fraction unfoldedTemperature (oC)Tm = 40.5 oC,DHvH = 68.9 kcal/molMeasurement was performed in 25mM phosphate pH 7.3, 0.7M GdmHCl, heating rate = 0.25 oC/min, proteinconc.= 80 g/ml. The transition was monitored by the increase of fluorescence at 353nm on excitation at 280nm
42 Denaturacja chemiczna FGF Fraction unfoldedDG = 5.53 kcal/molGdm½ = 1.13 Mm = 4.8 kcal/mol MGdmHCl (M)Measurements were performed in 25mM phosphate pH 7.3, protein concentration = 25 g/ml. The transitions weremonitored by the increase of fluorescence at 353nm on excitation at 280nm
43 Thermal unfolding transition of N-DCX and DCX-tandem of doublecortin Measurements were performed in 25mM phosphate, 300mM NaCl, pH 7.0, heating rate = 1oC/min, protein conc.= 20 g/ml. Transitions were monitored by the changes of the CD signal at 220nm.
44 pH titration of N-DCX of doublecortin 8.07.05.95.04.03.02.0
47 Widma CD mutantów FGF-1Circular dichroism spectra of the wild-type of FGF-1 (○), V109I (■), H102Y (▲), L44F (Δ),F108Y (□) and H21Y (●) mutants.
48 Denaturacja termiczna wariantów FGF-1 bNormalized thermal denaturation curves of the wild-type (○), V109I (■), H102Y (▲), L44F (Δ), F108Y (□), H21Y (●) mutants monitored by changes of fluorescence (a) or ellipticity (b).
49 Parametry denaturacji chemicznej mutantów FGF-1 w obecności heparyny Thermal induced unfolding were performed in 25mM phosphate, 1.5M Urea, pH 7.3, scan rate oC/min.10x molar excess of heparin were used.The transitions were monitored by the residual ellipticity at 227 nmMutant Tm DH Tm DH(oC) (kcal/mol) (oC) (kcal/mol)WTV109IF108YH102YH21YL44F
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