scholarly journals Characterisation of Conformational and Ligand Binding Properties of Membrane Proteins Using Synchrotron Radiation Circular Dichroism (SRCD)

2016 ◽  
pp. 43-59 ◽  
Author(s):  
Rohanah Hussain ◽  
Giuliano Siligardi
Keyword(s):  
Circular Dichroism ◽  
Synchrotron Radiation ◽  
Membrane Proteins ◽  
Ligand Binding ◽  
Binding Properties ◽  
Circular Dichroïsm

scholarly journals Investigation by Synchrotron Radiation Circular Dichroism of the Secondary Structure Evolution of Pepsin under Oxidative Environment

Foods ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 998
Author(s):  
Laetitia Théron ◽  
Aline Bonifacie ◽  
Jérémy Delabre ◽  
Thierry Sayd ◽  
Laurent Aubry ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Synchrotron Radiation ◽  
Secondary Structure ◽  
Proteolytic Activity ◽  
Digestive Enzyme ◽  
Structure Evolution ◽  
Food Protein ◽  
Maldi Tof ◽  
Kinetics Of ◽  
Circular Dichroïsm

Food processing affects the structure and chemical state of proteins. In particular, protein oxidation occurs and may impair protein properties. These chemical reactions initiated during processing can develop during digestion. Indeed, the physicochemical conditions of the stomach (oxygen pressure, low pH) favor oxidation. In that respect, digestive proteases may be affected as well. Yet, very little is known about the link between endogenous oxidation of digestive enzymes, their potential denaturation, and, therefore, food protein digestibility. Thus, the objective of this study is to understand how oxidative chemical processes will impact the pepsin secondary structure and its hydrolytic activity. The folding and unfolding kinetics of pepsin under oxidative conditions was determined using Synchrotron Radiation Circular Dichroism. SRCD gave us the possibility to monitor the rapid kinetics of protein folding and unfolding in real-time, giving highly resolved spectral data. The proteolytic activity of control and oxidized pepsin was investigated by MALDI-TOF mass spectrometry on a meat protein model, the creatine kinase. MALDI-TOF MS allowed a rapid evaluation of the proteolytic activity through peptide fingerprint. This study opens up new perspectives by shifting the digestion paradigm taking into account the gastric digestive enzyme and its substrate.

scholarly journals Circular dichroism spectroscopy of membrane proteins

2016 ◽  
Vol 45 (18) ◽  
pp. 4859-4872 ◽  
Author(s):  
A. J. Miles ◽  
B. A. Wallace
Keyword(s):  
Circular Dichroism ◽  
Membrane Proteins ◽  
Circular Dichroism Spectroscopy ◽  
Circular Dichroism Spectra ◽  
Helical Bundle ◽  
Beta Barrel ◽  
Circular Dichroïsm

Circular dichroism spectra of helical bundle (red), beta barrel (blue), and mixed helical/sheet/unordered (green) membrane proteins.

scholarly journals Effects of Trehalose on Thermodynamic Properties of Alpha-synuclein Revealed through Synchrotron Radiation Circular Dichroism

Biomolecules ◽  
2015 ◽  
Vol 5 (2) ◽  
pp. 724-734 ◽  
Author(s):  
Paolo Ruzza ◽  
Rohanah Hussain ◽  
Barbara Biondi ◽  
Andrea Calderan ◽  
Isabella Tessari ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Synchrotron Radiation ◽  
Thermodynamic Properties ◽  
Alpha Synuclein ◽  
Circular Dichroïsm

Circular Dichroism and Synchrotron Radiation Circular Dichroism Applications to Biomaterials

2019 ◽  
pp. 147-172
Author(s):  
Rohanah Hussain ◽  
Tamás Jávorfi ◽  
Charlotte S. Hughes ◽  
Giuliano Siligardi
Keyword(s):  
Circular Dichroism ◽  
Synchrotron Radiation ◽  
Circular Dichroïsm
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