2017
DOI: 10.1007/s10953-017-0612-0
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Thermal Aggregation of Bovine Serum Albumin in Conventional Buffers: An Insight into Molecular Level Interactions

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Cited by 22 publications
(9 citation statements)
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“…To summarize, in view of the current picture that the buffer influences the protein structure and stability by binding to its surface [16,17,18], the glycine buffer at low pH, where the HEWL molecule is highly positively charged has, itself in the cationic form, the lowest tendency to bind to the protein surface. This is reflected in destabilization of the protein structure upon increasing the ionic strength, as well as upon increasing temperature.…”
Section: Resultsmentioning
confidence: 99%
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“…To summarize, in view of the current picture that the buffer influences the protein structure and stability by binding to its surface [16,17,18], the glycine buffer at low pH, where the HEWL molecule is highly positively charged has, itself in the cationic form, the lowest tendency to bind to the protein surface. This is reflected in destabilization of the protein structure upon increasing the ionic strength, as well as upon increasing temperature.…”
Section: Resultsmentioning
confidence: 99%
“…Interfacial damage caused during sample agitation could also play an important role in fibril formation of HEWL. Small molecules, in this case buffer ions, can bind to the protein surface, and act as a protective coating, stabilizing the native structure of the protein [16,43,56].…”
Section: Discussionmentioning
confidence: 99%
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“…Some of the popular algorithms for inverting the measured correlation are described in several classical textbooks on the subject 16. Although most inversion techniques are based on Brownian diffusion (low concentration regime), there are some that are developed for gel-like systems26 typical of the high concentration scattering systems, such as the lens. Some arguments have been made to support the use of these models for inverting in vivo correlation data from the lens.…”
Section: Methodsmentioning
confidence: 99%
“…Micro-sized meshes can directly be assimilated as an ECM protein network offering a realistic support for cell growth. Hydrogels can be easily obtained by crosslinking a monomer solution either chemically [ 60 ], under radiation [ 61 ], but also by their self-assembling mechanisms [ 62 ] or through an aggregation mechanism after protein denaturation [ 63 ]. One can, for instance, find hydrogels based on alginate [ 64 ], gelatin [ 65 ], hydroxypropylmethyl cellulose [ 66 ], or hybrid combinations of fibrinogen and polyethylene glycol [ 67 ].…”
Section: Overview Of the Techniques Used For Fabrication Of Porousmentioning
confidence: 99%