Assessing the impact of choline chloride and benzyltrimethylammonium chloride-based deep eutectic solvents on the structure and conformational dynamics of bovine serum albumin: a combined steady-state, time-resolved fluorescence and fluorescence correlation spectroscopic study

Abstract

Although deep eutectic solvents (DESs) are regarded as useful substitutes for both ionic liquids and common organic solvents for storage and applications of biomolecules, it is still unclear whether all...

Exploring the Specific Role of Iron Center in the Catalytic Activity of Human Serum Transferrin: CTAB-Induced Conformational Changes and Sequestration by Mixed Micelles

“…The CD spectroscopy technique is often used to determine the changes in the secondary structure of proteins and monitor the conformational dynamics of protein–surfactant interactions. ,,, Far-UV CD spectra of Fe-hTF exhibit two negative peaks at 208 and 222 nm, which are the typical signatures of the presence of α-helix in the protein. As represented in Figure f, the CD signals of Fe-hTF increased marginally at 208 nm (however, they remained almost the same at 222 nm) upon the gradual addition of CTAB.…”

“…Mean residual ellipticity (MRE) was calculated using the following equation MRE false( deg 0.25em normalc m 2 0.25em dmo l − 1 false) = θ × M a × C × l Here, θ is observed CD (mdeg), M is the molecular weight of protein (g dmol –1 ), a is the number of amino acids (679 for transferrin), C is the concentration of the protein in g L –1 , and l is the path length of CD cuvette (0.1 cm). Further variation in the secondary structure of the protein (% α-helical content) was calculated by the following equation , α ‐ h e l i x false( % false) = false( − M R normalE 208 − 4000 false) 33 0.1em 000 − 4000 × 100 Here, MRE 208 is the calculated MRE value at 208 nm, 4000 is the MRE value of the β-form, and random coil conformation cross at 208 nm and 33000 is the MRE value of a pure α-helix at 208 nm.…”

“…Here, θ is observed CD (mdeg), M is the molecular weight of protein (g dmol −1 ), a is the number of amino acids (679 for transferrin), C is the concentration of the protein in g L −1 , and l is the path length of CD cuvette (0.1 cm). Further variation in the secondary structure of the protein (% α-helical content) was calculated by the following equation 33,34 helix (%) ( MRE 4000) 33000 4000 100…”

An eminent approach towards next generation solvents for sustainable packaging and stability of enzymes: a comprehensive study of ionic liquid and deep eutectic solvent mixtures

“…40,41 The CD spectra of Lyz exhibit two distinctively negative peaks due to the transition of the amide group of the peptide bond of the protein additives. 40–42 Therefore, the two negative bands at 208 and 222 nm represent the π–π* and n–π* protein transition, respectively. 39 Fig.…”

Deciphering the Role of Anions of Ionic Liquids in Modulating the Structure and Stability of ct-DNA in Aqueous Solutions

“…Consequently, they showcase distinct behaviors when introduced into an aqueous solution, and as a result, their interactions with ct -DNA are not uniform. Additionally, the static or dynamic nature of the quenching mechanism can be distinguished by monitoring the temperature dependence of the K sv . , It is evident from Table S1 that the K sv value increases with the rise in temperatures in the presence of each IL. This observation indicates that the fluorescence quenching of the DAPI-DNA complex by ILs is dynamic in nature.…”