Thermal conformational changes of bovine fibrinogen by differential scanning calorimetry and circular dichroism

A novel glucose biosensor based on phosphonic acid-functionalized silica nanoparticles for sensitive detection of glucose in real samples

“…It has been widely used to analyze and estimate the secondary structure content of the proteins [27]. Fig.…”

Interactions of KLVFF‐PEG Peptide Conjugate with Fibrinogen in Neutral Aqueous Solutions

“…[35] CD results discussed on the paragraph above suggest that the change in conformation associated with the reduction in size upon KLVFF-PEG binding (Figure 2a, Table 1) takes place without a noticeable change in the secondary structure content of the Fbg or with a change in the less represented secondary structure percentage (i.e., b-turn).…”

“…Figure 6 shows two distinctive negative bands for Fbg, situated at %208 and %224 nm. [33][34][35][36] Variations in CD spectra with D purely arise due to inherent experimental error, without denoting any particular trend in the dependence of the secondary structure of Fbg on D.…”

Mechanical compression affecting the thermal-induced conformational stability and denaturation temperature of human fibrinogen

“…FBG like other proteins is easily modified by a number of compounds and treatments to reduce its biological function, due to the loss of its native structure [7][8][9][10][11][12][13]. When FBG was * Corresponding author.…”

“…S-Nitrosothiol has been found to change the secondary structure of FBG by interacting at specific aromatic-rich domains inhibit both blood clot formation and platelet aggregation [9]. Several studies have also focused on the influence of pH and temperature on the interaction between FBG and its platelet receptor, calcium or EDTA, but they are all in the buffer solution or D 2 O [9][10][11][12][13]. In the absence of thermal effect, the pressure-induced conformational changes of solid FBG structure have been found not only to transform ␣-helix to ␤-sheet, but also to unfold and aggregate the FBG [14].…”