Sheets in Proteins: Difference between revisions
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Twisted sheets are found in globular proteins. Unlike the <scene name='Sheets_in_Proteins/Syn_sheet6/2'>above two types</scene> of sheets the valleys and the peaks of a <scene name='Sheets_in_Proteins/Gly_phosyl2/2'>twisted sheet</scene><ref>This sheet is part of the structure of domain 2 of glycogen phosphorylase (PDB code [[1abb]]).</ref> do not fall on parallel lines. Observe that the sheet is <scene name='Sheets_in_Proteins/Gly_phosyl/4'>parallel</scene>, and showing <scene name='Sheets_in_Proteins/Gly_phosyl3/1'>hydrogen bonds</scene>. Notice that in contrast to the hydrogen bonds of the antiparallel sheet shown above where the bonds were parallel here the bonds are diagonal to each other. Show <scene name='Sheets_in_Proteins/Gly_phosyl5/2'>psi and phi values</scene> for randomly chosen residues. There are a wide range of values for both psi and phi, +96 to +148 and -108 to -142, respectively. Sheet shown in the context of <scene name='Sheets_in_Proteins/Gly_phosyl4/1'>domain 2</scene> of glycogen phosphorylase. Examples of <scene name='Sheets_in_Proteins/1dtg1/1'>antiparallel sheets</scene><ref>These sheets are part of the structure of human transferrin n-lobe mutant (PDB code [[1dtg]]).</ref>. Showing only the <scene name='Sheets_in_Proteins/1dtg2/2'>sheets</scene>, and with <scene name='Sheets_in_Proteins/1dtg3/1'>hydrogen bonds</scene>. Show the <scene name='Sheets_in_Proteins/1dtg4/3'> range</scene> of values for psi and phi for randomly chosen residues to be +90 to +167 and -98 to -178, respectively. These ranges overlap the values for the twisted parallel showing that there is no difference in the values for the two types of twisted sheets. Median values for psi and phi are +140<sup>0</sup> and -125<sup>0</sup>, respectively, regardless if of parallel or antiparallel. | Twisted sheets are found in globular proteins. Unlike the <scene name='Sheets_in_Proteins/Syn_sheet6/2'>above two types</scene> of sheets the valleys and the peaks of a <scene name='Sheets_in_Proteins/Gly_phosyl2/2'>twisted sheet</scene><ref>This sheet is part of the structure of domain 2 of glycogen phosphorylase (PDB code [[1abb]]).</ref> do not fall on parallel lines. Observe that the sheet is <scene name='Sheets_in_Proteins/Gly_phosyl/4'>parallel</scene>, and showing <scene name='Sheets_in_Proteins/Gly_phosyl3/1'>hydrogen bonds</scene>. Notice that in contrast to the hydrogen bonds of the antiparallel sheet shown above where the bonds were parallel here the bonds are diagonal to each other. Show <scene name='Sheets_in_Proteins/Gly_phosyl5/2'>psi and phi values</scene> for randomly chosen residues. There are a wide range of values for both psi and phi, +96 to +148 and -108 to -142, respectively. Sheet shown in the context of <scene name='Sheets_in_Proteins/Gly_phosyl4/1'>domain 2</scene> of glycogen phosphorylase. Examples of <scene name='Sheets_in_Proteins/1dtg1/1'>antiparallel sheets</scene><ref>These sheets are part of the structure of human transferrin n-lobe mutant (PDB code [[1dtg]]).</ref>. Showing only the <scene name='Sheets_in_Proteins/1dtg2/2'>sheets</scene>, and with <scene name='Sheets_in_Proteins/1dtg3/1'>hydrogen bonds</scene>. Show the <scene name='Sheets_in_Proteins/1dtg4/3'> range</scene> of values for psi and phi for randomly chosen residues to be +90 to +167 and -98 to -178, respectively. These ranges overlap the values for the twisted parallel showing that there is no difference in the values for the two types of twisted sheets. Median values for psi and phi are +140<sup>0</sup> and -125<sup>0</sup>, respectively, regardless if of parallel or antiparallel. | ||
<table width='510' align='right' cellpadding='10'><tr><td bgcolor='#eeeeee'><center>'''Structures of Sheets'''<scene name='Sheets_in_Proteins/Syn sheet1/2'> (Initial scene)</scene></center></td></tr></table> | <table width='510' align='right' cellpadding='10'><tr><td bgcolor='#eeeeee'><center>'''Structures of Sheets'''<scene name='Sheets_in_Proteins/Syn sheet1/2'> (Initial scene)</scene></center></td></tr></table> | ||
== Notes and References == | == Notes and References == | ||
<references/> | <references/> | ||