Beta sheet: Difference between revisions

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==Structure, hydrogen bonding and composition==

The <scene name='88/889825/Toxin_1f94/1'>initial scene</scene> shows a protein with two sheets, one composed of four strands and the other of two. Beta strands are characterized by the extended conformation of the main chain (with phi and psi angles in the upper left quadrant of the [[Ramachandran plot]]) and hydrogen bonds to the neighboring strands.

The <scene name='88/889825/Toxin_1f94/1'>initial scene</scene> shows a protein with two sheets, one composed of four strands and the other of two. Beta strands are characterized by the extended conformation of the main chain (with phi and psi angles in the upper left quadrant of the [[Ramachandran plot]]) and hydrogen bonds to the neighboring strands. The beta sheet is also called beta pleated sheet because the peptide planes follow a zig-zag pattern.

For a strand in the middle of a sheet (as opposed to on its edge), all main chain hydrogen bond donors (the N-H groups) and acceptors (the C=O groups) are part of inter-strand hydrogen bonds. Strands are either in <scene name='88/889825/6l26_direction/1'>a parallel or an antiparallel arrangement</scene>, resulting in different <scene name='88/889825/6l26_direction/2'>hydrogen bonding patterns</scene> [https://www.ncbi.nlm.nih.gov/books/NBK22580/#_A328_]. Accordingly, beta sheets are classified as parallel, antiparallel or mixed. The antiparallel arrangement of strands is more prevalent <ref>DOI:10.1021/ci200027d</ref>. The beta strands on the edge of a sheet will have hydrogen bond donors and acceptors that have no other strand to partner with unless the sheet forms a cylindrical structure called a beta barrel, such as in the [[green fluorescent protein]] structure.

Beta sheet: Difference between revisions

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 ==Structure, hydrogen bonding and composition==
 <StructureSection load='' size='350' side='right' caption='' scene='88/889825/Toxin_1f94/1'>
-The <scene name='88/889825/Toxin_1f94/1'>initial scene</scene> shows a protein with two sheets, one composed of four strands and the other of two. Beta strands are characterized by the extended conformation of the main chain (with phi and psi angles in the upper left quadrant of the [[Ramachandran plot]]) and hydrogen bonds to the neighboring strands.
+The <scene name='88/889825/Toxin_1f94/1'>initial scene</scene> shows a protein with two sheets, one composed of four strands and the other of two. Beta strands are characterized by the extended conformation of the main chain (with phi and psi angles in the upper left quadrant of the [[Ramachandran plot]]) and hydrogen bonds to the neighboring strands. The beta sheet is also called beta pleated sheet because the peptide planes follow a zig-zag pattern.
 For a strand in the middle of a sheet (as opposed to on its edge), all main chain hydrogen bond donors (the N-H groups) and acceptors (the C=O groups) are part of inter-strand hydrogen bonds. Strands are either in <scene name='88/889825/6l26_direction/1'>a parallel or an antiparallel arrangement</scene>, resulting in different <scene name='88/889825/6l26_direction/2'>hydrogen bonding patterns</scene> [https://www.ncbi.nlm.nih.gov/books/NBK22580/#_A328_]. Accordingly, beta sheets are classified as parallel, antiparallel or mixed. The antiparallel arrangement of strands is more prevalent <ref>DOI:10.1021/ci200027d</ref>.  The beta strands on the edge of a sheet will have hydrogen bond donors and acceptors that have no other strand to partner with unless the sheet forms a cylindrical structure called a beta barrel, such as in the [[green fluorescent protein]] structure.