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Hydration in deep eutectic solvents induces non-monotonic changes in the conformation and stability of proteins
A Sanchez-Fernandez, M Basic, J **ang… - Journal of the …, 2022 - ACS Publications
The preservation of labile biomolecules presents a major challenge in chemistry, and deep
eutectic solvents (DESs) have emerged as suitable environments for this purpose. However …
eutectic solvents (DESs) have emerged as suitable environments for this purpose. However …
Binding, unfolding and refolding dynamics of serum albumins
Background The serum albumins (human and bovine serum albumin) occupy a seminal
position among all proteins investigated until today as they are the most abundant …
position among all proteins investigated until today as they are the most abundant …
Characterization of subdomain IIA binding site of human serum albumin in its native, unfolded, and refolded states using small molecular probes
OK Abou-Zied, OIK Al-Shihi - Journal of the American Chemical …, 2008 - ACS Publications
Subdomain IIA binding site of human serum albumin (HSA) was characterized by examining
the change in HSA fluorescence in the native, unfolded, and refolded states. The study was …
the change in HSA fluorescence in the native, unfolded, and refolded states. The study was …
Polysaccharide-protein interactions and their relevance in food colloids
AK Ghosh, P Bandyopadhyay - The complex world of …, 2012 - books.google.com
Polysaccharides and proteins are natural polymers that are widely used as functional
ingredients for various food colloids or emulsion formulations. Majority of food emulsions are …
ingredients for various food colloids or emulsion formulations. Majority of food emulsions are …
Understanding the physical and chemical nature of the warfarin drug binding site in human serum albumin: experimental and theoretical studies
O K. Abou-Zied - Current Pharmaceutical Design, 2015 - benthamdirect.com
Human serum albumin (HSA) is one of the major carrier proteins in the body and constitutes
approximately half of the protein found in blood plasma. It plays an important role in lipid …
approximately half of the protein found in blood plasma. It plays an important role in lipid …
Evaluation of 3-hydroxybutyrate as an enzyme-protective agent against heating and oxidative damage and its potential role in stress response of poly (3 …
Abstract Poly (3-hydroxybutyrate)(PHB) is a common carbon-and energy-storage compound
simultaneously produced and degraded into its monomer 3-hydroxybutyrate (3HB) by …
simultaneously produced and degraded into its monomer 3-hydroxybutyrate (3HB) by …
Thermally induced conformational changes and protein–protein interactions of bovine serum albumin in aqueous solution under different pH and ionic strengths as …
Thermal-induced conformational changes and protein–protein interactions of bovine serum
albumin (BSA) in aqueous solution are assessed by small angle X-ray scattering (SAXS) at …
albumin (BSA) in aqueous solution are assessed by small angle X-ray scattering (SAXS) at …
Contrasting changes in strongly and weakly bound hydration water of a protein upon denaturation
M Hishida, A Kaneko, Y Yamamura… - The Journal of Physical …, 2023 - ACS Publications
Water is considered integral for the stabilization and function of proteins, which has recently
attracted significant attention. However, the microscopic aspects of water ranging up to the …
attracted significant attention. However, the microscopic aspects of water ranging up to the …
Reversibility in protein folding: effect of β-cyclodextrin on bovine serum albumin unfolded by sodium dodecyl sulphate
The mechanism by which the protein bovine serum albumin undergoes unfolding induced
by the anionic surfactant sodium dodecyl sulphate (SDS) and then the subsequent refolding …
by the anionic surfactant sodium dodecyl sulphate (SDS) and then the subsequent refolding …
Osmolyte counteracts urea-induced denaturation of α-chymotrypsin
The stability of proteins is reduced by urea, which is methylamine and nonprotecting
osmolyte; eventually urea destabilizes the activity and function and alters the structure of …
osmolyte; eventually urea destabilizes the activity and function and alters the structure of …