The beta sheet, one type of secondary structure, is a higher level of organization of the protein's primary structure. Linus Pauling and Robert Corey first proposed the existence of this protein structure in 1951. Each polypeptide strand in a beta sheet makes a zig-zag pattern. Click here to see one strand (as a ball and stick model) Beta sheets are made up of multiple polypeptide strands. This beta sheet is made up of 5 strands. Click here to see each strand a different color. Hydrogen bonds are formed between the chains. Click here to see the hydrogen bonds (shown as thin, dashed, violet lines) between two adjacent beta strands in a beta sheet. Click here to see the hydrogen bonds between all five strands of the beta sheet. There are two types of beta sheets: Parallel (shown here) and Antiparallel (not shown). Parallel beta sheets In parallel beta sheets, the adjacent polypeptide chains run in the same direction. Typically parallel beta sheets are large structures that usually consist of at least five strands. Parallel beta sheets usually have hydrophobic residues on both sides of the sheet. Antiparallel beta sheets In antiparallel beta sheets, the beta strands run in the opposite direction. Antiparallel beta sheets can consist of as few as two strands. Unlike parallel beta sheets which typically distribute hydrophobic residues on both sides, antiparallel beta sheets typically distribute hydrophobic residues only on one side. There are numerous proteins that contain both antiparallel and parallel beta sheets. Shown here is flavodoxin which consists of a three-stranded antiparallel beta sheet and a five-stranded beta sheet (as well as 5 helices). 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 sheets consult: Garrett, R. and Grisham, C. (1995) Biochemistry pp: 145-147.
Each polypeptide strand in a beta sheet makes a zig-zag pattern. Click here to see one strand (as a ball and stick model) Beta sheets are made up of multiple polypeptide strands. This beta sheet is made up of 5 strands. Click here to see each strand a different color. Hydrogen bonds are formed between the chains. Click here to see the hydrogen bonds (shown as thin, dashed, violet lines) between two adjacent beta strands in a beta sheet. Click here to see the hydrogen bonds between all five strands of the beta sheet. There are two types of beta sheets: Parallel (shown here) and Antiparallel (not shown). Parallel beta sheets In parallel beta sheets, the adjacent polypeptide chains run in the same direction. Typically parallel beta sheets are large structures that usually consist of at least five strands. Parallel beta sheets usually have hydrophobic residues on both sides of the sheet. Antiparallel beta sheets In antiparallel beta sheets, the beta strands run in the opposite direction. Antiparallel beta sheets can consist of as few as two strands. Unlike parallel beta sheets which typically distribute hydrophobic residues on both sides, antiparallel beta sheets typically distribute hydrophobic residues only on one side. There are numerous proteins that contain both antiparallel and parallel beta sheets. Shown here is flavodoxin which consists of a three-stranded antiparallel beta sheet and a five-stranded beta sheet (as well as 5 helices). 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 sheets consult: Garrett, R. and Grisham, C. (1995) Biochemistry pp: 145-147.
Hydrogen bonds are formed between the chains. Click here to see the hydrogen bonds (shown as thin, dashed, violet lines) between two adjacent beta strands in a beta sheet. Click here to see the hydrogen bonds between all five strands of the beta sheet. There are two types of beta sheets: Parallel (shown here) and Antiparallel (not shown). Parallel beta sheets In parallel beta sheets, the adjacent polypeptide chains run in the same direction. Typically parallel beta sheets are large structures that usually consist of at least five strands. Parallel beta sheets usually have hydrophobic residues on both sides of the sheet. Antiparallel beta sheets In antiparallel beta sheets, the beta strands run in the opposite direction. Antiparallel beta sheets can consist of as few as two strands. Unlike parallel beta sheets which typically distribute hydrophobic residues on both sides, antiparallel beta sheets typically distribute hydrophobic residues only on one side. There are numerous proteins that contain both antiparallel and parallel beta sheets. Shown here is flavodoxin which consists of a three-stranded antiparallel beta sheet and a five-stranded beta sheet (as well as 5 helices). 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 sheets consult: Garrett, R. and Grisham, C. (1995) Biochemistry pp: 145-147.
There are two types of beta sheets: Parallel (shown here) and Antiparallel (not shown). Parallel beta sheets In parallel beta sheets, the adjacent polypeptide chains run in the same direction. Typically parallel beta sheets are large structures that usually consist of at least five strands. Parallel beta sheets usually have hydrophobic residues on both sides of the sheet. Antiparallel beta sheets In antiparallel beta sheets, the beta strands run in the opposite direction. Antiparallel beta sheets can consist of as few as two strands. Unlike parallel beta sheets which typically distribute hydrophobic residues on both sides, antiparallel beta sheets typically distribute hydrophobic residues only on one side. There are numerous proteins that contain both antiparallel and parallel beta sheets. Shown here is flavodoxin which consists of a three-stranded antiparallel beta sheet and a five-stranded beta sheet (as well as 5 helices). 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 sheets consult: Garrett, R. and Grisham, C. (1995) Biochemistry pp: 145-147.
Parallel beta sheets In parallel beta sheets, the adjacent polypeptide chains run in the same direction. Typically parallel beta sheets are large structures that usually consist of at least five strands. Parallel beta sheets usually have hydrophobic residues on both sides of the sheet. Antiparallel beta sheets In antiparallel beta sheets, the beta strands run in the opposite direction. Antiparallel beta sheets can consist of as few as two strands. Unlike parallel beta sheets which typically distribute hydrophobic residues on both sides, antiparallel beta sheets typically distribute hydrophobic residues only on one side. There are numerous proteins that contain both antiparallel and parallel beta sheets. Shown here is flavodoxin which consists of a three-stranded antiparallel beta sheet and a five-stranded beta sheet (as well as 5 helices). 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 sheets consult: Garrett, R. and Grisham, C. (1995) Biochemistry pp: 145-147.
Typically parallel beta sheets are large structures that usually consist of at least five strands.
Parallel beta sheets usually have hydrophobic residues on both sides of the sheet. Antiparallel beta sheets In antiparallel beta sheets, the beta strands run in the opposite direction. Antiparallel beta sheets can consist of as few as two strands. Unlike parallel beta sheets which typically distribute hydrophobic residues on both sides, antiparallel beta sheets typically distribute hydrophobic residues only on one side. There are numerous proteins that contain both antiparallel and parallel beta sheets. Shown here is flavodoxin which consists of a three-stranded antiparallel beta sheet and a five-stranded beta sheet (as well as 5 helices). 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 sheets consult: Garrett, R. and Grisham, C. (1995) Biochemistry pp: 145-147.
Antiparallel beta sheets In antiparallel beta sheets, the beta strands run in the opposite direction. Antiparallel beta sheets can consist of as few as two strands. Unlike parallel beta sheets which typically distribute hydrophobic residues on both sides, antiparallel beta sheets typically distribute hydrophobic residues only on one side. There are numerous proteins that contain both antiparallel and parallel beta sheets. Shown here is flavodoxin which consists of a three-stranded antiparallel beta sheet and a five-stranded beta sheet (as well as 5 helices). 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 sheets consult: Garrett, R. and Grisham, C. (1995) Biochemistry pp: 145-147.
Unlike parallel beta sheets which typically distribute hydrophobic residues on both sides, antiparallel beta sheets typically distribute hydrophobic residues only on one side. There are numerous proteins that contain both antiparallel and parallel beta sheets. Shown here is flavodoxin which consists of a three-stranded antiparallel beta sheet and a five-stranded beta sheet (as well as 5 helices). 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.
There are numerous proteins that contain both antiparallel and parallel beta sheets. Shown here is flavodoxin which consists of a three-stranded antiparallel beta sheet and a five-stranded beta sheet (as well as 5 helices).
You may wish to manipulate this image yourself:
For more information of beta pleated sheets consult: Garrett, R. and Grisham, C. (1995) Biochemistry pp: 145-147.