Propionate buffer

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In the Tenebrio antifreeze protein there are tandem 12-residue repeats (TCTxSxxCxxAx) that form a β-helix with regularly spaced threonine residues ( nm and nm), each turn of the helix, that make a match to water molecules in the ice prism plane ( nm and nm (see right [ 2802 ]). A similar binding site has been found in the ice-binding protein of the Antarctic bacterium Marinomonas primoryensis that is used to anchor the organism to Antarctic ice flows where oxygen and nutrients are more available [ 2805 ]). The protein binds to sea ice through a flat, repetitive two-dimensional array of Thr and Asn polar and non-polar groups create order in the water molecules surrounding them but their ability to do this and the types of ordering produced are very different. Polar groups are most capable of creating ordered hydration through hydrogen bonding and ionic interactions (an excellent guide to amino acid hydrogen bonding is given elsewhere). The ordering created in the water surrounding proteins extends the proteins' electrostatic surfaces well away from their physical (that is, amino acid) surfaces giving them far greater electrostatic visibility to visiting ligands [ 1156 ]. This non-specific electrostatic effect of the water effect is additional to any specific directed hydrogen bonding that may extend away into the bulk from the surface

Subsidies and financial assistance are given for drugs approved under the Standard Drug List (SDL) and Medication Assistance Fund (MAF). Drugs approved under the SDL and MAF must be registered with the Health Sciences Authority (HSA) and assessed to be clinically- and cost-effective. MAF drugs are generally newer and more expensive, and therefore MAF applies only when these drugs are used for suitable clinical indications so that MAF drugs are appropriately used. In exceptional cases, MAF can also support HSA-registered drugs that are not on the SDL or MAF list, on a case-by-case basis.

Propionate buffer

propionate buffer

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