Hilaria Baldwin revealed that her 20-month-old daughter, Lucia, suffered a 'scary' fall.
as often as they would like. “Being truly present for each one of them is hard, and I obviously don’t get it right all the time,” she explained.
“My two oldest have nightly homework that I do with them, and to balance play with the younger ones, breast-feeding the youngest — it can get to be quite a juggle.”alum plan to expand their family in the future, the jury’s still out. “I would have said before [that I’m] definitely done,” she toldFor access to all our exclusive celebrity videos and interviews –
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Hilaria Baldwin shows daughter Lucia’s black eye from hitting face on table“I was out with my oldest [four children] yesterday and got that awful call that makes your heart sink,” the fitness guru shared of the 1-year-old’s “shiner.”
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Crews battle 2 fires in Baldwin County Friday nightTwo separate fires in Baldwin County Friday night had multiple crews working to put them out.
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The Walking Dead's Carl Actor Reveals Hidden Series Finale CameoDespite Carl being long since dead, actor Chandler Riggs had a cameo in TheWalkingDeadSeriesFinale 👀 'It was for one of their wide shots, and they were like, 'Let's get you in there. Here!' I was just in this shirt and jeans that I came down there in.'
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High-resolution structure of a fish aquaporin reveals a novel extracellular foldAquaporins are protein channels embedded in the lipid bilayer in cells from all organisms on earth that are crucial for water homeostasis. In fish, aquaporins are believed to be important for osmoregulation; however, the molecular mechanism behind this is poorly understood. Here, we present the first structural and functional characterization of a fish aquaporin; cpAQP1aa from the fresh water fish climbing perch ( Anabas testudineus ), a species that is of high osmoregulatory interest because of its ability to spend time in seawater and on land. These studies show that cpAQP1aa is a water-specific aquaporin with a unique fold on the extracellular side that results in a constriction region. Functional analysis combined with molecular dynamic simulations suggests that phosphorylation at two sites causes structural perturbations in this region that may have implications for channel gating from the extracellular side.
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