3P037 The unfolding simulation of goat α-lactalbumin
نویسندگان
چکیده
منابع مشابه
R120G αB-crystallin promotes the unfolding of reduced α-lactalbumin and is inherently unstable
α-Crystallin is the principal lens protein which, in addition to its structural role, also acts as a molecular chaperone, to prevent aggregation and precipitation of other lens proteins. One of its two subunits, αBcrystallin, is also expressed in many non-lenticular tissues, and a natural missense mutation, R120G, has been associated with cataract and desminrelated myopathy, a disorder of skele...
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Special value of goat milk in human nutrition and well being is associated with medical problems of food allergies which are caused by milk proteins such as β-lactoglobulin (BLG). Here, we employed transcription activator-like effector nuclease (TALEN)-assisted homologous recombination in goat fibroblasts to introduce human α-lactalbumin (hLA) genes into goat BLG locus. TALEN-mediated targeting...
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Many soluble proteins are known to interact with membranes in partially disordered states, and the mechanism and relevance of such interactions in cellular processes are beginning to be understood. Bovine α-lactalbumin (BLA) represents an excellent prototype for monitoring membrane interaction due to its conformational plasticity. In this work, we comprehensively monitored the interaction of ap...
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α-Lactalbumin is the second major protein in bovine milk (2-5% of the total protein in bovine milk). The human variant has several physiologic functions in the neonatal period. In the mammary gland, it participates in lactose synthesis and facilitates milk production and secretion. α-Lactalbumin binds divalent cations (Ca Zn) and may facilitate the absorption of essential minerals. Also, it pro...
متن کاملUnfolding Simulations Reveal the Mechanism of Extreme Unfolding Cooperativity in the Kinetically Stable α-Lytic Protease
Kinetically stable proteins, those whose stability is derived from their slow unfolding kinetics and not thermodynamics, are examples of evolution's best attempts at suppressing unfolding. Especially in highly proteolytic environments, both partially and fully unfolded proteins face potential inactivation through degradation and/or aggregation, hence, slowing unfolding can greatly extend a prot...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2005
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.45.s213_1