Sandbox Reserved 773: Difference between revisions

Line 49:

Each monomer is divided into 3 structural <scene name='56/564049/3domain/1'>domains</scene>: <scene name='56/564049/Nterm/2'>N-terminal</scene> (~2-71), large domain (71-371), and small domain (372-477) (green link/figure 5) <ref name=jbc/>. A monomer is also composed of 49% helical structure and 13% beta sheet <ref name=4e10/>. One distinctively long α-helix which span from Val-359 to Arg-393 connects the large and small domains together (Figure 2). Through hydrophobic effect, the N-terminal regions of the two monomers interact with each other extensively. At the same time, the large domains interact extensively due to electrostatic interactions. Thus, the N-terminal regions and large domains form the dimer interfaces of HDC <ref name=jbc/>.

Each monomer is divided into 3 structural <scene name='56/564049/3domain/1'>domains</scene>: <scene name='56/564049/Nterm/2'>N-terminal</scene> (~2-71), <scene name='56/564049/Largedomain/1'>large domain</scene> (71-371), and small domain (372-477) (green link/figure 5) <ref name=jbc/>. A monomer is also composed of 49% helical structure and 13% beta sheet <ref name=4e10/>. One distinctively long α-helix which span from Val-359 to Arg-393 connects the large and small domains together (Figure 2). Through hydrophobic effect, the N-terminal regions of the two monomers interact with each other extensively. At the same time, the large domains interact extensively due to electrostatic interactions. Thus, the N-terminal regions and large domains form the dimer interfaces of HDC <ref name=jbc/>.

Sandbox Reserved 773: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

Revision as of 09:34, 2 December 2013 view source Wesley Yang (talk \| contribs) 185 edits →Sequence and Structure ← Older edit		Revision as of 09:51, 2 December 2013 view source Wesley Yang (talk \| contribs) 185 edits →Sequence and Structure Newer edit →
Line 49:		Line 49:


	Each monomer is divided into 3 structural <scene name='56/564049/3domain/1'>domains</scene>: <scene name='56/564049/Nterm/2'>N-terminal</scene> (~2-71), large domain (71-371), and small domain (372-477) (green link/figure 5) <ref name=jbc/>. A monomer is also composed of 49% helical structure and 13% beta sheet <ref name=4e10/>. One distinctively long α-helix which span from Val-359 to Arg-393 connects the large and small domains together (Figure 2). Through hydrophobic effect, the N-terminal regions of the two monomers interact with each other extensively. At the same time, the large domains interact extensively due to electrostatic interactions. Thus, the N-terminal regions and large domains form the dimer interfaces of HDC <ref name=jbc/>.		Each monomer is divided into 3 structural <scene name='56/564049/3domain/1'>domains</scene>: <scene name='56/564049/Nterm/2'>N-terminal</scene> (~2-71), <scene name='56/564049/Largedomain/1'>large domain</scene> (71-371), and small domain (372-477) (green link/figure 5) <ref name=jbc/>. A monomer is also composed of 49% helical structure and 13% beta sheet <ref name=4e10/>. One distinctively long α-helix which span from Val-359 to Arg-393 connects the large and small domains together (Figure 2). Through hydrophobic effect, the N-terminal regions of the two monomers interact with each other extensively. At the same time, the large domains interact extensively due to electrostatic interactions. Thus, the N-terminal regions and large domains form the dimer interfaces of HDC <ref name=jbc/>.