Cation-dependent structural features of β-casein-(1‒25)
نویسندگان
چکیده
منابع مشابه
Self-assembly of β-casein and lysozyme
The self-assembly of β-casein and lysozyme, a linear and a globular protein with isoelectric point of pH 5.0 and 10.7, respectively, was studied. Polydisperse electrostatic complex micelles formed when mixing β-casein and lysozyme aqueous solutions. After the micelle solution was heated, lysozyme gelated and β-casein was trapped in the gel, producing narrowly dispersed nanoparticles. The nanopa...
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Protein aggregation and precipitation is associated with many debilitating diseases including Alzheimer's, Parkinson's, and light-chain amyloidosis. β-Casein, a member of the casein family, has been demonstrated to exhibit chaperone-like activity to protect protein form aggregation. Hofmeister salts (lyotropice series) are a class of ions which have an effect on the solubility and also the stab...
متن کاملDetecting β-Casein Variation in Bovine Milk.
In bovine species, β-casein (β-CN) is characterized by genetic polymorphism. The two most common protein variants are β-CN A² (the original one) and A¹, differing from A² for one amino acid substitution (Pro67 to His67). Several bioactive peptides affecting milk nutritional properties can originate from β-CN. Among them, β-casomorphin-7 (BCM7) ranging from amino acid 60 to 66 can be released mo...
متن کاملCation–π–cation interactions in structural biology
Biological structures are stabilized by a variety of noncovalent interactions, such as hydrogen bonds, π –stacking, salt bridges or hydrophobic interactions. Besides hydrogen bonds and π– stacking, cation–π interactions between aromatic rings and positively charged groups have emerged as one of the most important interactions in structural biology. Although the role and energetic characteristic...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 2001
ISSN: 0264-6021
DOI: 10.1042/0264-6021:3560277