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| - | Glutamine synthetase from Salmonella typhimurium has 23 helix-helix interactions involving helices of chain A and four different types of interactions. [http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=2gls&template=protein.html&o=HELIX_INTERACTIONS&l=1&s=1&c=7&chain=A] Helix-helix interactions are the only interaction that can affect the folding of the proteins in Salmonella typhimurium. <scene name='Sandbox108/Hydrophobic/1'>Hydrophobic(purple)</scene> and <scene name='Sandbox108/Polar/1'>polar (blue)</scene> regions of the protein residues are on the helices of chain A. Also, uncharged polar groups are usually classified as hydrophilic that is found on the outside of proteins, but for glutamine in Salmonella typhimurium its side chain is uncharged and formed by replacing the hydroxyl of glutamic acid with an amine functional group. [http://en.wikipedia.org/wiki/Glutamine] Moreover, on the helices of chain A has <scene name='Sandbox108/Charged_region/1'>the charged regions</scene>. | + | Glutamine synthetase from Salmonella typhimurium has 23 helix-helix interactions involving helices of chain A and four different types of interactions. [http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=2gls&template=protein.html&o=HELIX_INTERACTIONS&l=1&s=1&c=7&chain=A] Helix-helix interactions are the only interaction that can affect the folding of the proteins in Salmonella typhimurium. <scene name='Sandbox108/Hydrophobic/1'>Hydrophobic(purple)</scene> and <scene name='Sandbox108/Polar/1'>polar(blue)</scene> regions of the protein residues are on the helices of chain A. Also, uncharged polar groups are usually classified as hydrophilic that is found on the outside of proteins, but for glutamine in Salmonella typhimurium its side chain is uncharged and formed by replacing the hydroxyl of glutamic acid with an amine functional group. [http://en.wikipedia.org/wiki/Glutamine] Moreover, on the helices of chain A has <scene name='Sandbox108/Charged_region/1'>the charged regions(blue and red)</scene>. |
Revision as of 00:37, 17 December 2008
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 23 helix-helix interactions involving helices of chain A and four different types of interactions. [5] Helix-helix interactions are the only interaction that can affect the folding of the proteins in Salmonella typhimurium. and regions of the protein residues are on the helices of chain A. Also, uncharged polar groups are usually classified as hydrophilic that is found on the outside of proteins, but for glutamine in Salmonella typhimurium its side chain is uncharged and formed by replacing the hydroxyl of glutamic acid with an amine functional group. [6] Moreover, on the helices of chain A has .
