User:Claire Lupton: Difference between revisions

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'''Structure:'''

Lengsin protein structure varies depending on the species in which it is presented due to the varying genetics within species. For example, in humans the n-terminal domain is the biggest indication that Lengsin contributes to the formation of the eye via evolution. This polymer consists of 421 residues composed of primarily alpha helix residues (140 residues) and 79 Beta Sheets. It is approximately 17 Angstroms in length and has a D-6 Dihedral globular symmetry. It also has twelve Glutamate-ammonia ligase proteins . lengsin is generally neither highly hydrophobic, nor highly hydrophilic. Although, it does have certain <scene name='83/837873/Hydrophobic_binding_sites/1'>hydrophobic binding sites</scene><scene name='83/837873/Hydrophobic_binding_sites/1'~~>Text To Be Displayed</scene~~> used for interaction with other hydrophobic molecules during lens formation. In total, there are six binding sites on lengsin which contribute to lens formation.<ref name=ref1>PMID:Grassi , F. J., Moretto, N. J., Rivetti, C. J., Cellai, S. J., Betti, M. J., Márquez , A. Ontonello, S. J. (2006). Structural and Functional Properties of Lengsin, a Pseduo-Glutamine Synthetase in the Transparent Human Lens . Retrieved from https://maryville.illiad.oclc.org/illiad/pdf/173917.pdf</ref> These proteins are found in a several vertebrate species, including prokaryotes, but they are most abundant in vertebrates.

Lengsin protein structure varies depending on the species in which it is presented due to the varying genetics within species. For example, in humans the n-terminal domain is the biggest indication that Lengsin contributes to the formation of the eye via evolution. This polymer consists of 421 residues composed of primarily alpha helix residues (140 residues) and 79 Beta Sheets. It is approximately 17 Angstroms in length and has a D-6 Dihedral globular symmetry. It also has twelve Glutamate-ammonia ligase proteins . lengsin is generally neither highly hydrophobic, nor highly hydrophilic. Although, it does have certain <scene name='83/837873/Hydrophobic_binding_sites/1'>hydrophobic binding sites</scene><scene name='83/837873/Hydrophobic_binding_sites/1'> used for interaction with other hydrophobic molecules during lens formation. In total, there are six binding sites on lengsin which contribute to lens formation.<ref name=ref1>PMID:Grassi , F. J., Moretto, N. J., Rivetti, C. J., Cellai, S. J., Betti, M. J., Márquez , A. Ontonello, S. J. (2006). Structural and Functional Properties of Lengsin, a Pseduo-Glutamine Synthetase in the Transparent Human Lens . Retrieved from https://maryville.illiad.oclc.org/illiad/pdf/173917.pdf</ref> These proteins are found in a several vertebrate species, including prokaryotes, but they are most abundant in vertebrates.

'''Function:'''

User:Claire Lupton: Difference between revisions

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 '''Structure:'''
-Lengsin protein structure varies depending on the species in which it is presented due to the varying genetics within species. For example, in humans the n-terminal domain is the biggest indication that Lengsin contributes to the formation of the eye via evolution. This polymer consists of 421 residues composed of primarily alpha helix residues (140 residues) and 79 Beta Sheets. It is approximately 17  Angstroms in length and has a D-6 Dihedral globular symmetry. It also has twelve Glutamate-ammonia ligase proteins . lengsin is generally neither highly hydrophobic, nor highly hydrophilic. Although, it does have certain <scene name='83/837873/Hydrophobic_binding_sites/1'>hydrophobic binding sites</scene><scene name='83/837873/Hydrophobic_binding_sites/1'>Text To Be Displayed</scene> used for interaction with other hydrophobic molecules during lens formation. In total, there are six binding sites on lengsin which contribute to lens formation.<ref name=ref1>PMID:Grassi , F. J., Moretto, N. J., Rivetti, C. J., Cellai, S. J., Betti, M. J., Márquez , A. Ontonello, S. J. (2006). Structural and Functional Properties of Lengsin, a Pseduo-Glutamine Synthetase in the Transparent Human Lens . Retrieved from https://maryville.illiad.oclc.org/illiad/pdf/173917.pdf</ref> These proteins are found in a several vertebrate species, including prokaryotes, but they are most abundant in vertebrates.
+Lengsin protein structure varies depending on the species in which it is presented due to the varying genetics within species. For example, in humans the n-terminal domain is the biggest indication that Lengsin contributes to the formation of the eye via evolution. This polymer consists of 421 residues composed of primarily alpha helix residues (140 residues) and 79 Beta Sheets. It is approximately 17  Angstroms in length and has a D-6 Dihedral globular symmetry. It also has twelve Glutamate-ammonia ligase proteins . lengsin is generally neither highly hydrophobic, nor highly hydrophilic. Although, it does have certain <scene name='83/837873/Hydrophobic_binding_sites/1'>hydrophobic binding sites</scene><scene name='83/837873/Hydrophobic_binding_sites/1'> used for interaction with other hydrophobic molecules during lens formation. In total, there are six binding sites on lengsin which contribute to lens formation.<ref name=ref1>PMID:Grassi , F. J., Moretto, N. J., Rivetti, C. J., Cellai, S. J., Betti, M. J., Márquez , A. Ontonello, S. J. (2006). Structural and Functional Properties of Lengsin, a Pseduo-Glutamine Synthetase in the Transparent Human Lens . Retrieved from https://maryville.illiad.oclc.org/illiad/pdf/173917.pdf</ref> These proteins are found in a several vertebrate species, including prokaryotes, but they are most abundant in vertebrates.
 '''Function:'''