Backbone torsion angles, specifically phi (φ) and psi (ψ), are crucial in determining the three-dimensional structure of proteins by defining the rotation around the bonds in the protein backbone. These angles influence the protein's secondary structure, such as alpha helices and beta sheets, and are essential for understanding protein folding and stability.

Backbone Torsion Angles

Backbone torsion angles

Phi (Φ)

Psi (Ψ)

three-dimensional structure of proteins

rotation around the bonds

The protein backbone is the continuous chain of atoms that forms the core structure of a protein, consisting of repeating units of nitrogen, carbon, and oxygen atoms. It plays a crucial role in determining the overall three-dimensional shape and stability of the protein, which directly impacts its biological function.

protein backbone

protein's secondary structure

alpha helices

beta sheets

Protein folding is the process by which a protein structure assumes its functional shape or conformation, which is crucial for its biological function. Misfolding can lead to diseases, making understanding this process vital for developing therapeutic interventions.

protein folding

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.

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