β折叠（β-sheet），又称β片层结构（β-pleated sheet）或β转角，是蛋白质的一种二级结构。

在β折叠中，两条以上氨基酸链（肽链），或同一条肽链之间的不同部分形成平行或反平行排列，成为“股”。肽平面之间呈手风琴状折叠，股与股之间会通过氢键固定，但氢键主要在股间而不是股内。氨基酸残基的R侧链分布在片层的上下。

β折叠层并不是平的，因为侧链的存在使得它看上去像手风琴一样波纹起伏。（英语pleated）这样每一股会更紧密排列，氢键更容易创建。氢键的距离为7埃。在蛋白质结构中β折叠通常会用箭头表示。肽链的氮端在同侧为顺式，两残基间距为0.65nm；不在同侧为反式，两残基间距为0.70nm。反式较顺式平行折叠更加稳定。

The β-sheet (also β-pleated sheet) is the second form of regular secondary structure in proteins. Beta sheets consist of beta strands (also β-strand) connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet. A β-strand is a stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformation. The higher-level association of β-sheets has been implicated in formation of the protein aggregates and fibrils observed in many human diseases, notably the amyloidoses such as Alzheimer's disease.