A parallel beta-sheet is a type of protein secondary structure where adjacent beta strands run in the same direction and are connected by hydrogen bonds. This arrangement is less stable than antiparallel beta-sheets due to the less optimal alignment of hydrogen bonds, but it is still a common motif in protein structures.

Parallel Beta-sheet

parallel beta-sheet

Protein secondary structure refers to the local spatial arrangement of a polypeptide's backbone atoms, primarily stabilized by hydrogen bonds. The main types are alpha helices and beta sheets, which are crucial for a protein's overall 3D conformation and function.

protein secondary structure

adjacent beta strands

same direction

Hydrogen bonds are a type of weak chemical bond that forms when a hydrogen atom, already covalently bonded to a more electronegative atom like oxygen or nitrogen, experiences attraction to another electronegative atom within the vicinity. They play a crucial role in determining the structure and properties of water, proteins, and nucleic acids, thereby influencing numerous biological and chemical processes.

hydrogen bonds

antiparallel beta-sheets

less stable

Optimal alignment refers to the process of arranging sequences, such as DNA, RNA, or proteins, to identify regions of similarity that may indicate functional, structural, or evolutionary relationships. It is a fundamental technique in bioinformatics and computational biology, often utilizing algorithms like dynamic programming to achieve the best possible alignment according to a specific scoring system.

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