Beta turns, also known as beta bends or tight turns, are a type of secondary structure. In a beta turn, a tight loop is formed when the carbonyl oxygen of one residue forms a hydrogen bond with the amide proton of an amino acid three residues down the chain. This hydrogen bond stabilizes the beta bend structure. Proline and Glycine are frequently found in beta turns, proline because its cyclic structure is ideally suited for the beta turn, and glycine because, with the smallest side chain of all the amino acids, it is the most sterically flexible. A beta turn is a means by which the protein can reverse the direction of its peptide chain. Beta turns often promote the formation of antiparallel beta sheets. Streptomyces subtilisin inhibitor (shown here) uses a beta turn to connect two of its antiparallel strands. You may wish to manipulate this image yourself: Click and hold the left mouse button to rotate the image about the x and y axes. Rotate about the z axis by pressing the shift key and right mouse button together. The image may be translated along the x and y axes by pressing control and the right mouse button. By pressing shift and the left mouse button together, you may zoom the image in or out. Clicking the right mouse button on the image gives a menu which offers several choices, including spinning the image and changing the appearance and color of the molecule. For more information of beta pleated turns consult: Garrett, R. and Grisham, C. (1995) Biochemistry pp: 147-148.
In a beta turn, a tight loop is formed when the carbonyl oxygen of one residue forms a hydrogen bond with the amide proton of an amino acid three residues down the chain. This hydrogen bond stabilizes the beta bend structure. Proline and Glycine are frequently found in beta turns, proline because its cyclic structure is ideally suited for the beta turn, and glycine because, with the smallest side chain of all the amino acids, it is the most sterically flexible. A beta turn is a means by which the protein can reverse the direction of its peptide chain. Beta turns often promote the formation of antiparallel beta sheets. Streptomyces subtilisin inhibitor (shown here) uses a beta turn to connect two of its antiparallel strands. You may wish to manipulate this image yourself: Click and hold the left mouse button to rotate the image about the x and y axes. Rotate about the z axis by pressing the shift key and right mouse button together. The image may be translated along the x and y axes by pressing control and the right mouse button. By pressing shift and the left mouse button together, you may zoom the image in or out. Clicking the right mouse button on the image gives a menu which offers several choices, including spinning the image and changing the appearance and color of the molecule. For more information of beta pleated turns consult: Garrett, R. and Grisham, C. (1995) Biochemistry pp: 147-148.
Proline and Glycine are frequently found in beta turns, proline because its cyclic structure is ideally suited for the beta turn, and glycine because, with the smallest side chain of all the amino acids, it is the most sterically flexible. A beta turn is a means by which the protein can reverse the direction of its peptide chain. Beta turns often promote the formation of antiparallel beta sheets. Streptomyces subtilisin inhibitor (shown here) uses a beta turn to connect two of its antiparallel strands. You may wish to manipulate this image yourself: Click and hold the left mouse button to rotate the image about the x and y axes. Rotate about the z axis by pressing the shift key and right mouse button together. The image may be translated along the x and y axes by pressing control and the right mouse button. By pressing shift and the left mouse button together, you may zoom the image in or out. Clicking the right mouse button on the image gives a menu which offers several choices, including spinning the image and changing the appearance and color of the molecule. For more information of beta pleated turns consult: Garrett, R. and Grisham, C. (1995) Biochemistry pp: 147-148.
A beta turn is a means by which the protein can reverse the direction of its peptide chain. Beta turns often promote the formation of antiparallel beta sheets. Streptomyces subtilisin inhibitor (shown here) uses a beta turn to connect two of its antiparallel strands. You may wish to manipulate this image yourself: Click and hold the left mouse button to rotate the image about the x and y axes. Rotate about the z axis by pressing the shift key and right mouse button together. The image may be translated along the x and y axes by pressing control and the right mouse button. By pressing shift and the left mouse button together, you may zoom the image in or out. Clicking the right mouse button on the image gives a menu which offers several choices, including spinning the image and changing the appearance and color of the molecule. For more information of beta pleated turns consult: Garrett, R. and Grisham, C. (1995) Biochemistry pp: 147-148.
Beta turns often promote the formation of antiparallel beta sheets. Streptomyces subtilisin inhibitor (shown here) uses a beta turn to connect two of its antiparallel strands. You may wish to manipulate this image yourself: Click and hold the left mouse button to rotate the image about the x and y axes. Rotate about the z axis by pressing the shift key and right mouse button together. The image may be translated along the x and y axes by pressing control and the right mouse button. By pressing shift and the left mouse button together, you may zoom the image in or out. Clicking the right mouse button on the image gives a menu which offers several choices, including spinning the image and changing the appearance and color of the molecule.
Streptomyces subtilisin inhibitor (shown here) uses a beta turn to connect two of its antiparallel strands.
You may wish to manipulate this image yourself:
For more information of beta pleated turns consult: Garrett, R. and Grisham, C. (1995) Biochemistry pp: 147-148.