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Protein Denaturation and Aggregation
Annals of the New York Academy of Sciences, 2006Abstract: Protein aggregation is a prominent feature of many neurodegenerative diseases, such as Alzheimer's, Huntington's, and Parkinson's diseases, as well as spongiform encephalopathies and systemic amyloidoses. These diseases are sometimes called protein misfolding diseases, but the latter term begs the question of what is the “folded” state of ...
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Freezing-induced denaturation of myofibrillar proteins in frozen meat
Critical reviews in food science and nutrition, 2022Freezing is commonly used to extend the shelf life of meat and meat products but may impact the overall quality of those products by inducing structural changes in myofibrillar proteins (MPs) through denaturation, chemical modification, and encouraging ...
Seonmin Lee+5 more
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Influence of micelles on protein's denaturation
International Journal of Biological Macromolecules, 2020To evaluate the role of micelles for protein-surfactant interaction, we have studied the binding modes of serum albumin proteins (human (HSA) and rabbit (RSA)) with anionic-surfactant, sodium dodecyl sulfate (SDS) by using UV-visible, fluorescence, circular dichroism, fluorescence lifetime, atomic force microscopy (AFM) techniques.
Rachana Srivastava+2 more
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Measurement of Denaturation of Fish Protein
Nature, 1956IT is well known that frozen fish alter in character during storage at sub-zero temperatures, becoming progressively tougher to eat, and exuding much fluid or ‘drip’ on thawing. The change proceeds more slowly the lower the temperature. There is a real need for an accurate objective method of measuring this deterioration, from the point of view of ...
J. I. M. Ironside, R. M. Love
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Denaturation and Renaturation of Proteins
Nature, 1945DESPITE the considerable advances that have been made in our knowledge of protein structure, the problem of denaturation remains somewhat obscure. A general theory of the phenomenon has been developed, which, although rough in its definition and speculative in character, is acceptable with varying degrees of qualification to most protein chemists. This
F. O. Howitt, D. Coleman
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Physical Chemistry, Chemical Physics - PCCP, 2014
The remarkable ability of guanidinium chloride (GdmCl) to denature proteins is a well studied yet controversial phenomenon; the exact molecular mechanism is still debatable, especially the role of hydration dynamics, which has been paid less attention ...
Nirnay Samanta+2 more
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The remarkable ability of guanidinium chloride (GdmCl) to denature proteins is a well studied yet controversial phenomenon; the exact molecular mechanism is still debatable, especially the role of hydration dynamics, which has been paid less attention ...
Nirnay Samanta+2 more
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Contrasting Effects of Nanoparticle Binding on Protein Denaturation
, 2014Understanding the interactions between nanoparticles (NPs) and proteins is essential for the design of bionanotechnology and biomedicine and for delineating the biological implications of nanomaterials for safe nanotechnology.
Pengyu Chen+7 more
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Protein Denaturant Binding Polynomials
Journal of Protein Chemistry, 2002We show how moments of the denaturant binding distribution function can be extracted from experimental data on the denaturation of a protein as a function of the concentration of denaturant and how in turn these moments can be used to construct the denaturant binding distribution function.
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Denaturation of proteins by fatty acids
Archives of Biochemistry and Biophysics, 1967Abstract Fatty acids are denaturants of egg albumin, and their effectiveness increases with the length of the carbon chain. The extent of denaturation is measured by the solubility of the protein at or near the isoelectric point in the presence of Na2SO4. The degree of denaturation depends, among other factors, on pH as well as the acid concentration.
Keith Breese, Henry B. Bull
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Journal of Physical Chemistry B, 2012
The mechanism of urea-induced protein denaturation is explored through studying the salting effect of urea on 14 amino acid side chain analogues, and N-methylacetamide (NMA) which mimics the protein backbone.
Weifeng Li, R. Zhou, Y. Mu
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The mechanism of urea-induced protein denaturation is explored through studying the salting effect of urea on 14 amino acid side chain analogues, and N-methylacetamide (NMA) which mimics the protein backbone.
Weifeng Li, R. Zhou, Y. Mu
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