scholarly journals Protein denaturation and protein:drugs interactions from intrinsic protein fluorescence measurements at the nanolitre scale

2010 ◽  
Vol 19 (8) ◽  
pp. 1544-1554 ◽  
Author(s):  
Gaudet Matthieu ◽  
Remtulla Nina ◽  
Jackson Sophie E. ◽  
Main Ewan R. G. ◽  
Bracewell Daniel G. ◽  
...  
Keyword(s):  
Protein Denaturation ◽  
Protein Fluorescence ◽  
Intrinsic Protein ◽  
Fluorescence Measurements ◽  
Intrinsic Protein Fluorescence

Sodium and potassium binding to parvalbumins measured by means of intrinsic protein fluorescence

1983 ◽  
Vol 749 (2) ◽  
pp. 185-191 ◽  
Author(s):  
Eugene A. Permyakov ◽  
Lina P. Kalinichenko ◽  
Vyacheslav N. Medvedkin ◽  
Edward A. Burstein ◽  
Charles Gerday
Keyword(s):  
Protein Fluorescence ◽  
Intrinsic Protein ◽  
Potassium Binding ◽  
Intrinsic Protein Fluorescence ◽  
Sodium And Potassium

Effect of calcium binding on conformational changes of staphylococcal metalloproteinase measured by means of intrinsic protein fluorescence

1986 ◽  
Vol 871 (2) ◽  
pp. 177-181 ◽  
Author(s):  
Zygmunt Wasylewski ◽  
Wiesław Stryjewski ◽  
Alicja Waśniowska ◽  
Jan Potempa ◽  
Krystyna Baran
Keyword(s):  
Conformational Changes ◽  
Calcium Binding ◽  
Protein Fluorescence ◽  
Intrinsic Protein ◽  
Intrinsic Protein Fluorescence

Monitoring of Demasking of Peptide Bonds During Proteolysis by Analysis of the Apparent Spectral Shift of Intrinsic Protein Fluorescence

2011 ◽  
Vol 6 (4) ◽  
pp. 519-526 ◽  
Author(s):  
Mikhail M. Vorob’ev ◽  
Vitali Vogel ◽  
Günnur Güler ◽  
Werner Mäntele
Keyword(s):  
Spectral Shift ◽  
Protein Fluorescence ◽  
Peptide Bonds ◽  
Intrinsic Protein ◽  
Intrinsic Protein Fluorescence

scholarly journals Correction: Thioamide quenching of intrinsic protein fluorescence

2020 ◽  
Vol 56 (25) ◽  
pp. 3699-3699
Author(s):  
Jacob M. Goldberg ◽  
Rebecca F. Wissner ◽  
Alyssa M. Klein ◽  
E. James Petersson
Keyword(s):  
Protein Fluorescence ◽  
Intrinsic Protein ◽  
Intrinsic Protein Fluorescence

Correction for ‘Thioamide quenching of intrinsic protein fluorescence’ by Jacob M. Goldberg et al., Chem. Commun., 2012, 48, 1550–1552.

Comparative Study of Recombinant Rat Nucleoside Diphosphate Kinases α and β By Intrinsic Protein Fluorescence

1999 ◽  
Vol 16 (4) ◽  
pp. 955-968 ◽  
Author(s):  
Nicolay Ya. Orlov ◽  
Tatiana G. Orlova ◽  
Yana K. Reshetnyak ◽  
Edward A. Burstein ◽  
Narimichi Kimura
Keyword(s):  
Comparative Study ◽  
Protein Fluorescence ◽  
Intrinsic Protein ◽  
Nucleoside Diphosphate Kinases ◽  
Intrinsic Protein Fluorescence

The «in vivo» study of blood 5-fluorouracil content by quenching of intrinsic protein fluorescence

2017 ◽  
Vol 192 ◽  
pp. 424-427 ◽  
Author(s):  
Regina R. Kayumova ◽  
Aleksandr V. Sultanbaev ◽  
Sergey S. Ostakhov ◽  
Sergey L. Khursan ◽  
Marat F. Abdullin ◽  
...  
Keyword(s):  
In Vivo Study ◽  
Protein Fluorescence ◽  
Intrinsic Protein ◽  
Intrinsic Protein Fluorescence

Analysis of fluorescence quenching data by the method of Levine.

1980 ◽  
Vol 26 (13) ◽  
pp. 1869-1871 ◽  
Author(s):  
D L Parsons
Keyword(s):  
Fluorescence Quenching ◽  
Binding Site ◽  
Specific Binding ◽  
Binding Constants ◽  
Protein Fluorescence ◽  
Binding Properties ◽  
Easy Method ◽  
Intrinsic Protein ◽  
Intrinsic Protein Fluorescence

Abstract The quenching of intrinsic protein fluorescence upon binding of ligand is a relatively quick and easy method for studying these interactions. The method of Steiner et al. (J. Biol. Chem. 241: 560, 1966) and the method of Levine (Clin. Chem. 23: 2292, 1977) have been used by different authors to interpret the data obtained from fluorescence-quenching studies. However, as is shown here, the method of Levine is not strictly valid when the protein contains more than one binding site for the ligand. Therefore, this method only approximates binding constants from such data, with an accuracy that depends on the specific binding properties of the interactants.

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