Sheets in Proteins: Difference between revisions
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<Structure load='Silk 64.mol' size='500' frame='true' align='right' caption='Insert caption here' scene='Sheets_in_Proteins/Syn_sheet1/1' /> | <Structure load='Silk 64.mol' size='500' frame='true' align='right' caption='Insert caption here' scene='Sheets_in_Proteins/Syn_sheet1/1' /> | ||
A β-pleated sheet contains multiple peptide strands that are positioned adjacent to one another (such as the one <scene name='Sheets_in_Proteins/Syn sheet1/1'>shown</scene> on the right). The planes of the <scene name='Sheets_in_Proteins/Syn_sheet2/2'>pleats</scene> are formed by the planes of the peptide bond. The alpha carbons of the peptide chain are at the valleys and peaks of the pleats. The peptides are <scene name='Sheets_in_Proteins/Syn_sheet3/1'>rainbow colored</scene> (blue amino end changing to red carboxy end) to show that the adjacent peptides are running in opposite directions making the sheet antiparallel. | A β-pleated sheet contains multiple peptide strands that are positioned adjacent to one another (such as the one <scene name='Sheets_in_Proteins/Syn sheet1/1'>shown</scene> on the right). The planes of the <scene name='Sheets_in_Proteins/Syn_sheet2/2'>pleats</scene> are formed by the planes of the peptide bond. The alpha carbons of the peptide chain are at the valleys and peaks of the pleats. The peptides are <scene name='Sheets_in_Proteins/Syn_sheet3/1'>rainbow colored</scene> (blue amino end changing to red carboxy end) to show that the adjacent peptides are running in opposite directions making the sheet antiparallel. The adjacent chains align so that <scene name='Sheets_in_Proteins/Syn_sheet3/2'>hydrogne bonds</scene> are formed between the imino hydrogens of one chain and the carbonyl oxygens of an adjacent chain. Psi and phi values that permit this alignment in antiparallel sheets have mean values of | ||
Revision as of 02:22, 16 February 2011
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A β-pleated sheet contains multiple peptide strands that are positioned adjacent to one another (such as the one on the right). The planes of the are formed by the planes of the peptide bond. The alpha carbons of the peptide chain are at the valleys and peaks of the pleats. The peptides are (blue amino end changing to red carboxy end) to show that the adjacent peptides are running in opposite directions making the sheet antiparallel. The adjacent chains align so that are formed between the imino hydrogens of one chain and the carbonyl oxygens of an adjacent chain. Psi and phi values that permit this alignment in antiparallel sheets have mean values of