The beta-alpha-beta motif is a fundamental protein structural arrangement where two parallel beta sheets are connected by an alpha helix, stabilizing the protein by creating a favorable hydrogen bonding network. This motif is crucial in many proteins' folding patterns, contributing to their functional configuration and stability.

Beta-alpha-beta Motif

Fundamental protein structural arrangement

Parallel beta sheets

The alpha helix is a common structural motif in proteins, characterized by a right-handed coiled shape stabilized by hydrogen bonds between the backbone amide hydrogen and carbonyl oxygen of every fourth amino acid. This structure is crucial for the stability and functionality of many proteins, contributing to their ability to perform a wide range of biological functions.

Alpha Helix

Favorable hydrogen bonding network

Proteins' folding patterns

Functional configuration

Protein stability refers to the ability of a protein to maintain its structural integrity and functional conformation under various environmental conditions. It is crucial for protein function and is influenced by factors such as temperature, pH, ionic strength, and the presence of stabilizing or destabilizing agents.

Concepts

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