badan Search Results


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AnaSpec fluorescent probe badan [6-bromoacetyl-2-dimethylaminonaphthalene]
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AnaSpec fluorescent label badan
GdnHCl-induced conformational changes of <t>GGBP/H152C–BADAN.</t> Structural changes of protein apo-form (red curves and circles) and holo-form (blue curves and triangles) recorded by intrinsic UV fluorescence (Panels A , B ) and by BADAN fluorescence (Panels C , D ) are represented. The dependences of total intrinsic fluorescence intensity and total BADAN fluorescence intensity on <t>the</t> <t>guanidine</t> hydrochloride (GdnHCl) concentrations are represented on panels ( A , C ). Intrinsic fluorescence was excited at 297 nm, and BADAN fluorescence was excited at 387 nm. Shifts in the intrinsic and BADAN fluorescence spectrum position induced by GdnHCl are presented by parameters A and B (Panels B , D ). Here A is a parameter for the intrinsic fluorescence spectrum position ( A = I 320 / I 365 , where I 320 and I 365 are fluorescence intensities recorded at 320 and 365 nm, λ ex = 297 nm), and B is a parameter for the BADAN fluorescence spectrum position ( B = I 498 / I 587 , I 498 and I 587 are fluorescence intensities of BADAN recorded at 498 and 587 nm, λ ex = 387 nm).
Fluorescent Label Badan, supplied by AnaSpec, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


GdnHCl-induced conformational changes of GGBP/H152C–BADAN. Structural changes of protein apo-form (red curves and circles) and holo-form (blue curves and triangles) recorded by intrinsic UV fluorescence (Panels A , B ) and by BADAN fluorescence (Panels C , D ) are represented. The dependences of total intrinsic fluorescence intensity and total BADAN fluorescence intensity on the guanidine hydrochloride (GdnHCl) concentrations are represented on panels ( A , C ). Intrinsic fluorescence was excited at 297 nm, and BADAN fluorescence was excited at 387 nm. Shifts in the intrinsic and BADAN fluorescence spectrum position induced by GdnHCl are presented by parameters A and B (Panels B , D ). Here A is a parameter for the intrinsic fluorescence spectrum position ( A = I 320 / I 365 , where I 320 and I 365 are fluorescence intensities recorded at 320 and 365 nm, λ ex = 297 nm), and B is a parameter for the BADAN fluorescence spectrum position ( B = I 498 / I 587 , I 498 and I 587 are fluorescence intensities of BADAN recorded at 498 and 587 nm, λ ex = 387 nm).

Journal: International Journal of Molecular Sciences

Article Title: Osmolyte-Like Stabilizing Effects of Low GdnHCl Concentrations on d -Glucose/ d -Galactose-Binding Protein

doi: 10.3390/ijms18092008

Figure Lengend Snippet: GdnHCl-induced conformational changes of GGBP/H152C–BADAN. Structural changes of protein apo-form (red curves and circles) and holo-form (blue curves and triangles) recorded by intrinsic UV fluorescence (Panels A , B ) and by BADAN fluorescence (Panels C , D ) are represented. The dependences of total intrinsic fluorescence intensity and total BADAN fluorescence intensity on the guanidine hydrochloride (GdnHCl) concentrations are represented on panels ( A , C ). Intrinsic fluorescence was excited at 297 nm, and BADAN fluorescence was excited at 387 nm. Shifts in the intrinsic and BADAN fluorescence spectrum position induced by GdnHCl are presented by parameters A and B (Panels B , D ). Here A is a parameter for the intrinsic fluorescence spectrum position ( A = I 320 / I 365 , where I 320 and I 365 are fluorescence intensities recorded at 320 and 365 nm, λ ex = 297 nm), and B is a parameter for the BADAN fluorescence spectrum position ( B = I 498 / I 587 , I 498 and I 587 are fluorescence intensities of BADAN recorded at 498 and 587 nm, λ ex = 387 nm).

Article Snippet: d -Glucose, guanidine hydrochloride, urea, tris(2-carboxyethylphosphine (TCEP), acrylamide (Sigma, St. Louis, MO, USA), and fluorescent label BADAN (AnaSpec, Fremont, CA, USA) were used without further purification.

Techniques: Fluorescence