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. Strands are either in a parallel or and antiparallel arrangement, resulting in different hydrogen bonding patterns. 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 <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. Strands are either in a parallel or and antiparallel arrangement, resulting in different hydrogen bonding patterns. 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.

</StructureSection>

Beta sheet: Difference between revisions

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 <StructureSection load='' size='350' side='right' caption='' scene='88/889825/Toxin_1f94/1'>
 ==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. Strands are either in a parallel or and antiparallel arrangement, resulting in different hydrogen bonding patterns. 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 <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. Strands are either in a parallel or and antiparallel arrangement, resulting in different hydrogen bonding patterns. 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.
 </StructureSection>