Editing Beta sheet (section)

===β-meander motif===
A simple [[structural motif|supersecondary]] protein topology composed of two or more consecutive antiparallel β-strands linked together by [[beta hairpin|hairpin]] loops.<ref>{{Cite web |url=http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.c.bbf.html |title=SCOP: Fold: WW domain-like<!-- Bot generated title --> |access-date=2007-06-01 |archive-url=https://web.archive.org/web/20120204065925/http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.c.bbf.html |archive-date=2012-02-04 |url-status=dead }}</ref><ref>{{Cite web |url=http://www.cryst.bbk.ac.uk/PPS2/course/section9/sss/super2.html |title=PPS '96 – Super Secondary Structure<!-- Bot generated title --> |access-date=2007-05-31 |archive-date=2016-12-28 |archive-url=https://web.archive.org/web/20161228125148/http://www.cryst.bbk.ac.uk/PPS2/course/section9/sss/super2.html |url-status=dead }}</ref> This motif is common in β-sheets and can be found in several structural architectures including [[beta barrel|β-barrels]] and [[beta propeller|β-propellers]].

The vast majority of β-meander regions in proteins are found packed against other motifs or sections of the polypeptide chain, forming portions of the hydrophobic core that canonically drives formation of the folded structure.<ref>{{cite journal|vauthors=Biancalana M, Makabe K, Koide S|date=February 2010|title=Minimalist design of water-soluble cross-beta architecture|journal=Proceedings of the National Academy of Sciences of the United States of America|volume=107|issue=8|pages=3469–74|doi=10.1073/pnas.0912654107|pmc=2840449|pmid=20133689|bibcode=2010PNAS..107.3469B|doi-access=free}}</ref>  However, several notable exceptions include the Outer Surface Protein A (OspA) variants<ref name=":0" /> and the Single Layer β-sheet Proteins (SLBPs)<ref>{{Cite journal|last1=Xu|first1=Qingping|last2=Biancalana|first2=Matthew|last3=Grant|first3=Joanna C.|last4=Chiu|first4=Hsiu-Ju|last5=Jaroszewski|first5=Lukasz|last6=Knuth|first6=Mark W.|last7=Lesley|first7=Scott A.|last8=Godzik|first8=Adam|last9=Elsliger|first9=Marc-André|last10=Deacon|first10=Ashley M.|last11=Wilson|first11=Ian A.|date=September 2019|title=Structures of single-layer β-sheet proteins evolved from β-hairpin repeats|journal=Protein Science |volume=28|issue=9|pages=1676–1689|doi=10.1002/pro.3683|issn=1469-896X|pmc=6699103|pmid=31306512}}</ref> which contain single-layer β-sheets in the absence of a traditional hydrophobic core.  These β-rich proteins feature an extended single-layer β-meander β-sheets that are primarily stabilized via inter-β-strand interactions and hydrophobic interactions present in the turn regions connecting individual strands.