Editing Beta sheet (section)

===Hydrogen bonding patterns===
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| image1 = Beta sheet bonding antiparallel-color.svg
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| caption1 = '''Antiparallel''' β-sheet [[hydrogen bonding]] patterns, represented by dotted lines. [[Oxygen]] atoms are colored <span style="color:red;">'''red'''</span> and [[nitrogen]] atoms colored <span style="color:blue;">'''blue'''</span>.
| caption2 = '''Parallel''' β-sheet [[hydrogen bonding]] patterns, represented by dotted lines. [[Oxygen]] atoms are colored <span style="color:red;">'''red'''</span> and [[nitrogen]] atoms colored <span style="color:blue;">'''blue'''</span>.
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Because peptide chains have a directionality conferred by their [[N-terminus]] and [[C-terminal end|C-terminus]], β-strands too can be said to be directional. They are usually represented in protein topology diagrams by an arrow pointing toward the C-terminus. Adjacent β-strands can form [[hydrogen bond]]s in antiparallel, parallel, or mixed arrangements.

In an antiparallel arrangement, the successive β-strands alternate directions so that the N-terminus of one strand is adjacent to the C-terminus of the next. This is the arrangement that produces the strongest inter-strand stability because it allows the inter-strand hydrogen bonds between carbonyls and amines to be planar, which is their preferred orientation. The peptide backbone dihedral angles (''φ'',&nbsp;''ψ'') are about (–140°,&nbsp;135°) in antiparallel sheets. In this case, if two atoms C{{su|p=α|b=''i''}} and C{{su|p=α|b=''j''}} are adjacent in two [[hydrogen bond|hydrogen-bonded]] β-strands, then they form two mutual backbone hydrogen bonds to each other's flanking [[peptide bond|peptide groups]]; this is known as a '''close pair''' of hydrogen bonds.

In a parallel arrangement, all of the N-termini of successive strands are oriented in the same direction; this orientation may be slightly less stable because it introduces nonplanarity in the inter-strand hydrogen bonding pattern. The dihedral angles (''φ'',&nbsp;''ψ'') are about (–120°,&nbsp;115°) in parallel sheets. It is rare to find less than five interacting parallel strands in a motif, suggesting that a smaller number of strands may be unstable, however it is also fundamentally more difficult for parallel β-sheets to form because strands with N and C termini aligned necessarily must be very distant in sequence {{Citation needed|date=August 2019}}. There is also evidence that parallel β-sheet may be more stable since small amyloidogenic sequences appear to generally aggregate into β-sheet fibrils composed of primarily parallel β-sheet strands, where one would expect anti-parallel fibrils if anti-parallel were more stable.

In parallel β-sheet structure, if two atoms C{{su|p=α|b=''i''}} and C{{su|p=α|b=''j''}} are adjacent in two [[hydrogen bond|hydrogen-bonded]] β-strands, then they do ''not'' hydrogen bond to each other; rather, one residue forms hydrogen bonds to the residues that flank the other (but not vice versa). For example, residue ''i'' may form hydrogen bonds to residues ''j''&nbsp;−&nbsp;1 and ''j''&nbsp;+&nbsp;1; this is known as a '''wide pair''' of hydrogen bonds. By contrast, residue ''j'' may hydrogen-bond to different residues altogether, or to none at all.

The hydrogen bond arrangement in parallel beta sheet resembles that in an [[amide ring]] motif with 11 atoms.

Finally, an individual strand may exhibit a mixed bonding pattern, with a parallel strand on one side and an antiparallel strand on the other. Such arrangements are less common than a random distribution of orientations would suggest, suggesting that this pattern is less stable than the anti-parallel arrangement, however bioinformatic analysis always struggles with extracting structural thermodynamics since there are always numerous other structural features present in whole proteins. Also proteins are inherently constrained by folding kinetics as well as folding thermodynamics, so one must always be careful in concluding stability from bioinformatic analysis.

The [[hydrogen bond]]ing of β-strands need not be perfect, but can exhibit localized disruptions known as [[beta bulge|β-bulge]]s.

The hydrogen bonds lie roughly in the plane of the sheet, with the [[peptide bond|peptide]] [[carbonyl]] groups pointing in alternating directions with successive residues; for comparison, successive carbonyls point in the ''same'' direction in the [[alpha helix]].