Identification of a conserved hydrophobic cluster in partially folded bovine β-lactoglobulin at pH 2
نویسندگان
چکیده
منابع مشابه
Identification of a conserved hydrophobic cluster in partially folded bovine beta-lactoglobulin at pH 2.
BACKGROUND NMR studies of denatured states, both fully unfolded and partially folded, give insight into the conformations and interactions formed during folding. Although the complete structural characterization of partially folded proteins is a very difficult task, the identification of structured subsets, such as hydrophobic clusters, is of value in understanding the structural organization o...
متن کاملStructure of bovine β-lactoglobulin-lactoferrin coacervates.
Lactoferrin (LF) and β-lactoglobulin (BLG) are among the protein pairs that exhibit heteroprotein coacervation, a unique and relatively unexamined type of liquid-liquid phase separation (LLPS). In prior work we found that LF and BLG undergo coacervation at highly constrained conditions of pH, ionic strength and protein stoichiometry. The molar stoichiometry in coacervate and supernatant is LF :...
متن کاملAdsorption of Milk Proteins (β-Casein and β-Lactoglobulin) and BSA onto Hydrophobic Surfaces
Here, we study films of proteins over planar surfaces and protein-coated microspheres obtained from the adsorption of three different proteins ( β -casein, β -lactoglobulin and bovine serum albumin (BSA)). The investigation of protein films in planar surfaces is performed by combining quartz crystal microbalance (QCM) and atomic force microscopy (AFM) measurements with all-atomic molecular dyna...
متن کاملHeteroprotein complex coacervation: bovine β-lactoglobulin and lactoferrin.
Lactoferrin (LF) and β-lactoglobulin (BLG), strongly basic and weakly acidic bovine milk proteins, form optically clear coacervates under highly limited conditions of pH, ionic strength I, total protein concentration C(P), and BLG:LF stoichiometry. At 1:1 weight ratio, the coacervate composition has the same stoichiometry as its supernatant, which along with DLS measurements is consistent with ...
متن کاملAmyloid-β adopts a conserved, partially folded structure upon binding to zwitterionic lipid bilayers prior to amyloid formation.
Aggregation at the neuronal cell membrane's lipid bilayer surface is implicated in amyloid-β (Aβ) toxicity associated with Alzheimer's disease; however, structural and mechanistic insights into the process remain scarce. We have identified a conserved binding mode of Aβ40 on lipid bilayer surfaces with a conserved helix containing the self-recognition site (K16-E22).
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Folding and Design
سال: 1997
ISSN: 1359-0278
DOI: 10.1016/s1359-0278(97)00039-4