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Taewang Lee

Revision as of 02:13, 8 December 2008 view source Taewang Lee (talk \| contribs) 86 edits No edit summary ← Older edit		Revision as of 02:18, 8 December 2008 view source Taewang Lee (talk \| contribs) 86 edits No edit summary Newer edit →
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	Glutamine is within uncharged polar <~~show~~ the uncharged polar groups ~~wiki text~~>. Usually, uncharged polar groups are classified as hydrophilic <~~show~~ the hydrophilic ~~wiki text~~> 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 <~~show~~ the polar ~~wiki text~~>. 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 <~~show~~ the hydrophobic of cysteine ~~wiki text~~> 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]


	Tertiary structure of protein is characterized by the “global” folding of a polypeptide chain. [http://www.stanford.edu/group/pandegroup/folding/education/prstruc.html] 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 <~~show~~ α-helix ~~wiki text~~> and the β-sheet <~~show~~ the β-sheet ~~wiki text~~> 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 <~~show~~ the H.B ~~wiki text~~> is crucial in stabilizing the tertiary structure. [http://webhost.bridgew.edu/fgorga/proteins/proteins.htm] On the other hand, disulfide bonds <~~show~~ the disulfide bonds of cysteine ~~wiki text~~> between cysteine residues stabilize the tertiary structure. [http://webhost.bridgew.edu/fgorga/proteins/proteins.htm]		Tertiary structure of protein is characterized by the “global” folding of a polypeptide chain. [http://www.stanford.edu/group/pandegroup/folding/education/prstruc.html] 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]