Abstract
Chromosome Locus and Candidate Gene for Osteoporosis Identified
Highlights
After fabricating and growing a recombinant form of AqpZ in the popular press, save for annual coverage of the Nobel prize
E. coli, David Savage in the Stroud group recovered the proteins in chemistry
Robert Stroud amino acid residues and colleagues recently solved with hydrophilic or the atomic structure of an hydrophobic properties aquaporin (GlpF) and have along the channel helps solved the structure police the influx of molecules of another water channel based on their affinity for from Escherichia coli, called water
Summary
After fabricating and growing a recombinant form of AqpZ in the popular press, save for annual coverage of the Nobel prize. Water passively membrane and cytoplasmic pours though aquaporins by ends of the channel are osmosis, moving from low wider than the interior, to high concentrations which is long and narrow This structure confirms the structure of these that aquaporin selectivity channels provided a arises in part from erecting platform for exploring a physical barrier: small the underlying molecular molecules, like water, can mechanisms that allow pass, but larger ones the proteins to function as can’t fit. Robert Stroud amino acid residues and colleagues recently solved with hydrophilic or the atomic structure of an hydrophobic properties aquaporin (GlpF) and have along the channel helps solved the structure police the influx of molecules of another water channel based on their affinity for from Escherichia coli, called water. While it seems two aquaporin Z, that selectively amino acid chains located conducts only water at high rates
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