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Glutamine synthetase assignment by UMBC undergraduate students
OUTLINE
Glutamine synthetase of Salmonella typhimurium
Tertiary structure of protein is characterized by the “global” folding of a polypeptide chain [1] and has two domains in refined atomic model of glutamine synthetase from Salmonella typhimurium. Hydrophobic interaction is a major driving force determining the most tertiary structure of the proteins. [2] Hydrogen bonding is crucial in stabilizing the tertiary structure as well. [3] Also, disulfide bonds between cysteine residues stabilize the tertiary structure. [4] However, for glutamine synthetase for Salmonella, the most important interaction will be the helix-helix interactions.
Glutamine synthetase from Salmonella typhimurium has twenty three helix-helix interactions, and is four different types of interactions. [5] and regions of the protein residues
is within uncharged polar <insert wiki showing the uncharged polar groups>. Usually, uncharged polar groups are classified as hydrophilic <insert wiki showing the hydrophilic> that is found on the outside of proteins. Also, amino acids with the character of acidic or basic side chains are polar, showing on the outside of molecules <insert wiki showing the polar>. For glutamine, its side chain is uncharged and formed by replacing the hydroxyl of glutamic acid with an amine functional group. [6] In the other hand, glutamine has no side chain on non-polar group, however the side chain on non-polar groups of the proteins usually tends to be hydrophobic <insert wiki showing the hydrophobic of cysteine> and to cluster together on the inside.[7]
