2012
DOI: 10.1016/j.jphotobiol.2011.11.002
|View full text |Cite
|
Sign up to set email alerts
|

Evaluation of solute binding to proteins and intra-protein distances from steady state fluorescence measurements

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

3
39
0
2

Year Published

2012
2012
2015
2015

Publication Types

Select...
8
1

Relationship

0
9

Authors

Journals

citations
Cited by 33 publications
(44 citation statements)
references
References 134 publications
3
39
0
2
Order By: Relevance
“…This binding process is represented in the initial lineal portion of the binding isotherm where n < 1. To confirm this result, we calculated also K b by applying the Encinas-Lissi (E-L) method [34,35], using the quenching efficiency of the intrinsic Trp-like fluorescence of the protein by RB as a function of the BSA concentration in the range between 1.7 and 21 lM to minimize the effect of self-protein aggregation. As briefly described in the Supporting Information, the E-L method allows the estimation of n as a function of [RB] free independently of both the binding and [RB] free values were also included in Fig.…”
Section: Spectroscopic and Photophysical Consequences Of Rb Binding Tmentioning
confidence: 93%
“…This binding process is represented in the initial lineal portion of the binding isotherm where n < 1. To confirm this result, we calculated also K b by applying the Encinas-Lissi (E-L) method [34,35], using the quenching efficiency of the intrinsic Trp-like fluorescence of the protein by RB as a function of the BSA concentration in the range between 1.7 and 21 lM to minimize the effect of self-protein aggregation. As briefly described in the Supporting Information, the E-L method allows the estimation of n as a function of [RB] free independently of both the binding and [RB] free values were also included in Fig.…”
Section: Spectroscopic and Photophysical Consequences Of Rb Binding Tmentioning
confidence: 93%
“…The red-shift in the absorbance spectrum of the NIR fluorescent IO-HSA nanoparticles compared with free CANIR dye is probably due to its physical binding to HSA, that places the dye in a more hydrophobic environment and affects the dipole moment of the dye. 40 Three types of NIR fluorescent IO-HSA nanoparticles were synthesized for comparison, ie, IO containing dyed gelatin in the core and a nondyed HSA shell, IO containing nondyed gelatin in the core and a dyed HSA shell, and IO containing dyed gelatin in the core as well as a dyed HSA shell. A comparison of the fluorescence intensity of each type shows that the nanoparticles composed of dye within the core as well as within the shell (nanoparticles of type 3) possess the highest fluorescence intensity (Figure 4).…”
Section: Fluorescence Measurementsmentioning
confidence: 99%
“…Special Issue Dedicated to the Memory of Elsa Beatriz Abuin Saccomano (1942-2012 Elsa was born in 1942 in Buenos Aires, Argentina, and obtained the degree of Licenciada en Ciencias Químicas (MS in Chemistry) in the College of Sciences (Facultad de Ciencias Exactas y Naturales) at the University of Buenos Aires in 1966. The same year, after the tragic "night of the long sticks", on July 29th (the night when the police forces broke into the College of Sciences at the University of Buenos Aires), which resulted in the resignation of a large percentage of the teaching staff in that College, she moved with the Lissi-Grotewold group to the Universidad T ecnica del Estado (UTE), Chile (now Universidad de Santiago de Chile), as a teaching assistant.…”
Section: Introductionmentioning
confidence: 99%