User:Chengfeng Ren/IFN beta 1a: Difference between revisions

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=='''Structure info. of IFNβ-1a'''==

IFNβ-1a consisting of 166 amino acids, around 20KDa. It has 5 helixs. There are several <scene name='56/566503/Important_hydrophobic_residues/2'>hydrophobic residues</scene>,such as Phe-70, Phe-154, Trp-79, and Trp-143, that are involved in interactions with each other that stabilize the core of the molecule. In addition, residues of the core form several <scene name='56/566503/H-bonding/3'>hydrogen bonding</scene> such as between Gln-10 and Gln-94 and between Ser-118 and Thr-58. Additional interactions that appear to stabilize the loop are <scene name='56/566503/H-bonding/2'>hydrogen bonds</scene> between Tyr-132 OH and Asp-34 O and between Arg-147 N and Leu-24 O. Cys-31 forms a disulfide bridge with Cys-141 of and plays an important role in the stabilization of protein structure

IFNβ-1a consisting of 166 amino acids, around 20KDa. It has 5 helixs. There are several <scene name='56/566503/Important_hydrophobic_residues/2'>hydrophobic residues</scene>,such as Phe-70, Phe-154, Trp-79, and Trp-143, that are involved in interactions with each other that stabilize the core of the molecule. In addition, residues of the core form several <scene name='56/566503/H-bonding/3'>hydrogen bonding</scene> such as between Gln-10 and Gln-94 and between Ser-118 and Thr-58. Additional interactions that appear to stabilize the loop are <scene name='56/566503/H-bonding/2'>hydrogen bonds</scene> between Tyr-132 OH and Asp-34 O and between Arg-147 N and Leu-24 O. Cys-31 forms a <scene name='56/566503/Disulfide_bridge/1'>disulfide bridge</scene> with Cys-141 of and plays an important role in the stabilization of protein structure

<scene name='56/566498/Interferon_beta_1a/1'>Interferon beta 1a</scene>

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 =='''Structure info. of IFNβ-1a'''==
-IFNβ-1a consisting of 166 amino acids, around 20KDa. It has 5 helixs. There are several <scene name='56/566503/Important_hydrophobic_residues/2'>hydrophobic residues</scene>,such as Phe-70, Phe-154, Trp-79, and Trp-143, that are involved in interactions with each other that stabilize the core of the molecule. In addition, residues of the core form several <scene name='56/566503/H-bonding/3'>hydrogen bonding</scene> such as between Gln-10 and Gln-94 and between Ser-118 and Thr-58. Additional interactions that appear to stabilize the loop are <scene name='56/566503/H-bonding/2'>hydrogen bonds</scene> between Tyr-132 OH and Asp-34 O and between Arg-147 N and Leu-24 O. Cys-31 forms a disulfide bridge with Cys-141 of and plays an important role in the stabilization of protein structure
+IFNβ-1a consisting of 166 amino acids, around 20KDa. It has 5 helixs. There are several <scene name='56/566503/Important_hydrophobic_residues/2'>hydrophobic residues</scene>,such as Phe-70, Phe-154, Trp-79, and Trp-143, that are involved in interactions with each other that stabilize the core of the molecule. In addition, residues of the core form several <scene name='56/566503/H-bonding/3'>hydrogen bonding</scene> such as between Gln-10 and Gln-94 and between Ser-118 and Thr-58. Additional interactions that appear to stabilize the loop are <scene name='56/566503/H-bonding/2'>hydrogen bonds</scene> between Tyr-132 OH and Asp-34 O and between Arg-147 N and Leu-24 O. Cys-31 forms a <scene name='56/566503/Disulfide_bridge/1'>disulfide bridge</scene> with Cys-141 of and plays an important role in the stabilization of protein structure
 <scene name='56/566498/Interferon_beta_1a/1'>Interferon beta 1a</scene>