User:Michael Adams/Sandbox 1: Difference between revisions

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Developmental Biology, Swiss Federal Institute of Technology, Zurich, 21 June 1973. Web. 12 Nov. 2015</ref>. This is done by the transfer of an N-phosphoryl group from phosphocreatine to ADP.

== Structure ==

The structure of <scene name='71/716599/My3/1'>arginine kinase</scene> is mainly α-helical and contains an N-terminal region with a specificity loop for specific substrate binding. (Figure 2). However, when compared to creatine kinase, arginine kinase is not terminated at the N-terminal end with a pair of proline-glycine residues. Typically within creatine kinase, the proline molecules restrict changes in conformation and is the amino acid that terminates helices. The glycine chains are usually associated with flexibility. However, in arginine kinase this is typically not the case. On the C-terminal end, there is an eight-stranded antiparallel <scene name='71/716599/Beta/1'>β-sheet</scene> with seven <scene name='71/716599/Mynewscene/1'>α-helices</scene> flanking the sheet (Figure 1). Residue <scene name='71/716599/330/1'>330</scene> is an arginine that appears to play a crucial role in maintaining structural stability. Studies show that a mutation in the residue leads to a steep decline in enzymatic activity <ref>DOI 10.1016/j.ijbiomac.2012.12.015</ref>.

The structure of <scene name='71/716599/My3/1'>arginine kinase</scene> is mainly α-helical and contains an N-terminal region with a specificity loop for specific substrate binding. (Figure 2). However, when compared to creatine kinase, arginine kinase is not terminated at the N-terminal end with a pair of proline-glycine residues. Typically within creatine kinase, the proline molecules restrict changes in conformation and is the amino acid that terminates helices. The glycine chains are usually associated with flexibility. However, in arginine kinase this is typically not the case. On the C-terminal end, there is an eight-stranded antiparallel <scene name='71/716599/Beta/1'>β-sheet</scene> with seven <scene name='71/716599/Mynewscene/1'>α-helices</scene> flanking the sheet (Figure 1). Residue <scene name='71/716599/330/2'>330</scene> is an arginine that appears to play a crucial role in maintaining structural stability. Studies show that a mutation in the residue leads to a steep decline in enzymatic activity <ref>DOI 10.1016/j.ijbiomac.2012.12.015</ref>.

User:Michael Adams/Sandbox 1: Difference between revisions

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@@ Line 9: / Line 9: @@
 Developmental Biology, Swiss Federal Institute of Technology, Zurich, 21 June 1973. Web. 12 Nov. 2015</ref>. This is done by the transfer of an N-phosphoryl group from phosphocreatine to ADP.
 == Structure ==
-The structure of <scene name='71/716599/My3/1'>arginine kinase</scene> is mainly α-helical and contains an N-terminal region with a specificity loop for specific substrate binding.  (Figure 2). However, when compared to creatine kinase, arginine kinase is not terminated at the N-terminal end with a pair of proline-glycine residues. Typically within creatine kinase, the proline molecules restrict changes in conformation and is the amino acid that terminates helices. The glycine chains are usually associated with flexibility. However, in arginine kinase this is typically not the case. On the C-terminal end, there is an eight-stranded antiparallel <scene name='71/716599/Beta/1'>β-sheet</scene> with seven <scene name='71/716599/Mynewscene/1'>α-helices</scene> flanking the sheet (Figure 1). Residue <scene name='71/716599/330/1'>330</scene> is an arginine that appears to play a crucial role in maintaining structural stability. Studies show that a mutation in the residue leads to a steep decline in enzymatic activity <ref>DOI 10.1016/j.ijbiomac.2012.12.015</ref>.
+The structure of <scene name='71/716599/My3/1'>arginine kinase</scene> is mainly α-helical and contains an N-terminal region with a specificity loop for specific substrate binding.  (Figure 2). However, when compared to creatine kinase, arginine kinase is not terminated at the N-terminal end with a pair of proline-glycine residues. Typically within creatine kinase, the proline molecules restrict changes in conformation and is the amino acid that terminates helices. The glycine chains are usually associated with flexibility. However, in arginine kinase this is typically not the case. On the C-terminal end, there is an eight-stranded antiparallel <scene name='71/716599/Beta/1'>β-sheet</scene> with seven <scene name='71/716599/Mynewscene/1'>α-helices</scene> flanking the sheet (Figure 1). Residue <scene name='71/716599/330/2'>330</scene> is an arginine that appears to play a crucial role in maintaining structural stability. Studies show that a mutation in the residue leads to a steep decline in enzymatic activity <ref>DOI 10.1016/j.ijbiomac.2012.12.015</ref>.
 [[Image:F1.large.jpg|left|frame|none|alt=Alt text|Figure 1. Structure of an AK in substrate-bound form<ref>http://www.pnas.org/content/95/15/8449/F1.large.jpg</ref>]]