Sandbox108: Difference between revisions
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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 consist of two domains. Hydrophobic interaction is a major driving force determining the tertiary structure of the proteins. [http://www.stanford.edu/group/pandegroup/folding/education/prstruc.html] The reason why hydrophobic interaction is important is because of relationship with the hydrogen bonding. The peptide backbone is hydrophilic, but in the middle of proteins is mostly in a hydrophobic circumstance. So, in order to reduce the hydrophilicity, to maximize the hydrogen bonding, the α-helix <insert wiki showing α-helix> and the β-sheet <insert wiki showing the β-sheet> can break down the C=O and N-H groups in the peptide bonds so that the hydrogen bonds are maximum. [http://www.massey.ac.nz/~wwbioch/Prot/thirds/framset.htm] Also, all polar and hydrophilic side chains interact with H-bonds. Hydrogen bonding <insert wiki showing the H.B> is crucial in stabilizing the tertiary structure. [http://webhost.bridgew.edu/fgorga/proteins/proteins.htm] On the other hand, disulfide bonds <insert wiki showing the disulfide bonds of cysteine> between cysteine residues stabilize the tertiary structure. [http://webhost.bridgew.edu/fgorga/proteins/proteins.htm] | |||
Glutamine 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 | Glutamine 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 01:05, 17 December 2008
Glutamine synthetase assignment by UMBC undergraduate studentsGlutamine synthetase assignment by UMBC undergraduate students
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| 2qc8, resolution 2.60Å () | |||||||||
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| Ligands: | , , , | ||||||||
| Gene: | GLUL, GLNS (Homo sapiens) | ||||||||
| Activity: | Glutamate--ammonia ligase, with EC number 6.3.1.2 | ||||||||
| Related: | 2ojw | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
OUTLINEOUTLINE
Tertiary Structure
Tertiary structure of protein is characterized by the “global” folding of a polypeptide chain [1] and consist of two domains. Hydrophobic interaction is a major driving force determining the tertiary structure of the proteins. [2] The reason why hydrophobic interaction is important is because of relationship with the hydrogen bonding. The peptide backbone is hydrophilic, but in the middle of proteins is mostly in a hydrophobic circumstance. So, in order to reduce the hydrophilicity, to maximize the hydrogen bonding, the α-helix <insert wiki showing α-helix> and the β-sheet <insert wiki showing the β-sheet> can break down the C=O and N-H groups in the peptide bonds so that the hydrogen bonds are maximum. [3] Also, all polar and hydrophilic side chains interact with H-bonds. Hydrogen bonding <insert wiki showing the H.B> is crucial in stabilizing the tertiary structure. [4] On the other hand, disulfide bonds <insert wiki showing the disulfide bonds of cysteine> between cysteine residues stabilize the tertiary structure. [5]
Glutamine 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]