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In charge-dipole interactions Hydrogen bonding is important. How do the hydrogen bond donor and acceptor increase...

In charge-dipole interactions Hydrogen bonding is important. How do the hydrogen bond donor and acceptor increase the apparent PKa of an amino acid? (BIOCHEM QUESTION)

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Based on propensity of side chain to be in contact with water, amino acids are classified as hydrophobic, polar and charged. The charged amino acids include two basic, lysin and arginine and two acidic, aspartate and glutamate. Polar aminoacids include serine and threonine, asparagine and glutamine.histidine is also a polar residue, although it's behavior depends on polarity of it's environment. It has two -NH group with pKa of value around 6. When two groups are protonated, the side chain has a charge of+1. However pKa may be modulated by the environment inside the protein and when raised the side chain may give away a proton, loosing it's positive charge and becoming neutral. By other words may histidine easily give away and accept a proton, make it especially useful within enzmye active sites

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