Results 211 to 220 of about 284,480 (260)
Integrated Enzyme- and Ultrasound-Assisted Extraction of Fennel Seed Proteins: Process Optimization, Structure, and Functionality. [PDF]
Food Sci NutrTurker I, Isleroglu H.
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Strategies to optimize the nutritional profile of mammalian meat for infants and geriatric population. [PDF]
Food Sci Anim ResourYoo MJY.
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Annual Review of Biochemistry, 1991
The denatured "state" of a protein is a distribution of many different molecular conformations, the averages of which are measured by experiments. The properties of this ensemble depend sensitively on the solution conditions. There is now considerable evidence that even in strong denaturants such as 6M GuHC1 and 9M urea, some structure may remain in ...
K A, Dill, D, Shortle
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The denatured "state" of a protein is a distribution of many different molecular conformations, the averages of which are measured by experiments. The properties of this ensemble depend sensitively on the solution conditions. There is now considerable evidence that even in strong denaturants such as 6M GuHC1 and 9M urea, some structure may remain in ...
K A, Dill, D, Shortle
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Nature, 1957
REPORTING on the influence of freezing-rate on the denaturation of cold-stored fish, Love1 states that organoleptically determined toughness of cod, stored at − 30° C., does not always involve decreased protein solubility.
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REPORTING on the influence of freezing-rate on the denaturation of cold-stored fish, Love1 states that organoleptically determined toughness of cod, stored at − 30° C., does not always involve decreased protein solubility.
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Critical Reviews in Biochemistry and Molecular Biology, 1990
This article summarizes all experimental facts concerning the cold denaturation of single-domain, multi-domain, and multimeric globular proteins in aqueous solutions with and without urea and guanidine hydrochloride. The facts obtained by various experimental techniques are analyzed thermodynamically and it is shown that the cold denaturation is a ...
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This article summarizes all experimental facts concerning the cold denaturation of single-domain, multi-domain, and multimeric globular proteins in aqueous solutions with and without urea and guanidine hydrochloride. The facts obtained by various experimental techniques are analyzed thermodynamically and it is shown that the cold denaturation is a ...
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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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THE FLUORESCENCE OF NATIVE, DENATURED AND REDUCED‐DENATURED PROTEINS*
Photochemistry and Photobiology, 1971Abstract— (1) By excitation at 295 nm tryptophan fluorescence from 17 proteins was examined free of contributions from tyrosine. The tryptophan quantum yields for native proteins were both higher and lower than that of the free amino acid and spanned a 5‐fold range.
M. J. KRONMAN, L. G. HOLMES
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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 K, IRONSIDE, R M, LOVE
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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, Md Sayem, Alam
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