Secondary structure: Difference between revisions
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<applet load='1dtg' size='400' frame='true' align='right' caption='1dtg' scene='Cartoon_backbone_representation/1dtg_ss/1'/> | <applet load='1dtg' size='400' frame='true' align='right' caption='1dtg' scene='Cartoon_backbone_representation/1dtg_ss/1'/> | ||
Secondary structure of a protein refers to the three-dimensional structure of local segments of a protein. Each type of secondary structure has segments that have a repeating conformational pattern which is produced by a repeating pattern of values for the [[Psi and Phi Angles|phi and psi torsional angles]]. For this reason on a [[Ramachandran Plots|Ramachandran plot]] for a particular secondary structure the values for phi and psi are located at a particular area of the plot. for example alpha helices and beta sheets are secondary structure. The structure on the right of a human transferrin n-lobe mutant (PDB code [[1dtg]]) is shown in cartoon backbone representation to highlight its secondary structure, with alpha-helices in magenta and beta-sheets in yellow. | Secondary structure of a protein refers to the three-dimensional structure of local segments of a protein. Each type of secondary structure has segments that have a repeating conformational pattern which is produced by a repeating pattern of values for the [[Psi and Phi Angles|phi and psi torsional angles]]. For this reason on a [[Ramachandran Plots|Ramachandran plot]] for a particular secondary structure the values for phi and psi are located at a particular area of the plot. There are three important second structures - helix, β-sheets and turns, and there are several variations of each one of them. Alpha helix, pi helix and 3<sub>10</sub> helix are the three types of helices with the alpha helix being the most important. The characteristics of these three helices are given at [[Helices in Proteins]]. | ||
for example alpha helices and beta sheets are secondary structure. The structure on the right of a human transferrin n-lobe mutant (PDB code [[1dtg]]) is shown in cartoon backbone representation to highlight its secondary structure, with alpha-helices in magenta and beta-sheets in yellow. | |||
For more information, see [http://en.wikipedia.org/wiki/Secondary_structure Wikipedia's page on secondary structure]. | For more information, see [http://en.wikipedia.org/wiki/Secondary_structure Wikipedia's page on secondary structure]. | ||
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Revision as of 03:32, 10 February 2011
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Secondary structure of a protein refers to the three-dimensional structure of local segments of a protein. Each type of secondary structure has segments that have a repeating conformational pattern which is produced by a repeating pattern of values for the phi and psi torsional angles. For this reason on a Ramachandran plot for a particular secondary structure the values for phi and psi are located at a particular area of the plot. There are three important second structures - helix, β-sheets and turns, and there are several variations of each one of them. Alpha helix, pi helix and 310 helix are the three types of helices with the alpha helix being the most important. The characteristics of these three helices are given at Helices in Proteins.
for example alpha helices and beta sheets are secondary structure. The structure on the right of a human transferrin n-lobe mutant (PDB code 1dtg) is shown in cartoon backbone representation to highlight its secondary structure, with alpha-helices in magenta and beta-sheets in yellow.
For more information, see Wikipedia's page on secondary structure.