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==Glutamine synthetase assignment by UMBC undergraduate students== | ==Glutamine synthetase assignment by UMBC undergraduate students== | ||
{{STRUCTURE_2gls | PDB=2gls | SCENE= }} | {{STRUCTURE_2gls | PDB=2gls | SCENE= }} | ||
| - | <scene name='User:Taewang_Lee/Exercise_2/1'>Exercise 2</scene> | ||
| - | <scene name='User:Taewang_Lee/Exercise_3/5'>Exercise 3</scene> | ||
| - | <scene name='Sandbox108/Exercise_4/1'>Exercise 4</scene> | ||
| - | <scene name='User:Taewang_Lee/Exercise_4/5'>Exercise 4(Practiced)</scene> | ||
== OUTLINE == | == OUTLINE == | ||
| - | '' | + | ''Glutamine synthetase of Salmonella'' |
| - | Tertiary structure of protein is characterized by the “global” folding of a polypeptide chain [http://www.stanford.edu/group/pandegroup/folding/education/prstruc.html] 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. [http://www.stanford.edu/group/pandegroup/folding/education/prstruc.html] Hydrogen bonding | + | Tertiary structure of protein is characterized by the “global” folding of a polypeptide chain [http://www.stanford.edu/group/pandegroup/folding/education/prstruc.html] 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. [http://www.stanford.edu/group/pandegroup/folding/education/prstruc.html] Hydrogen bonding is crucial in stabilizing the tertiary structure as well. [http://webhost.bridgew.edu/fgorga/proteins/proteins.htm] Also, disulfide bonds between cysteine residues stabilize the tertiary structure. [http://webhost.bridgew.edu/fgorga/proteins/proteins.htm] However, for glutamine synthetase for Salmonella, the most important interaction will be the helix-helix interactions. |
| - | Glutamine synthetase from Salmonella has twenty three helix-helix interactions and is 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] <scene name='Sandbox108/Hydrophobic/1'>Hydrophobic (purple)</scene> on the protein residues and polar < | + | Glutamine synthetase from Salmonella has twenty three helix-helix interactions and is 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] <scene name='Sandbox108/Hydrophobic/1'>Hydrophobic (purple)</scene> on the protein residues and <scene name='Sandbox108/Polar/1'>polar</scene> regions of the protein residues are represented by deep blue color. |
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. [http://en.wikipedia.org/wiki/Glutamine] 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.[http://www.bmb.uga.edu/wampler/tutorial/prot3.html] | 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. [http://en.wikipedia.org/wiki/Glutamine] 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.[http://www.bmb.uga.edu/wampler/tutorial/prot3.html] | ||
Revision as of 23:45, 16 December 2008
Glutamine synthetase assignment by UMBC undergraduate students
OUTLINE
Glutamine synthetase of Salmonella
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 has twenty three helix-helix interactions and is four different types of interactions. [5] on the protein residues and regions of the protein residues are represented by deep blue color.
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]
