Protein secondary structure refers to the local spatial arrangement of amino acids in a protein, primarily alpha-helices and beta-sheets. Understanding these structures is crucial for predicting protein function, stability, and interactions.
Enter your protein sequence using the one-letter code (A, R, N, D, etc.). The tool will analyze the sequence and predict the secondary structure elements, showing helices (H), sheets (E), and coils (C) along with confidence scores.
Alpha-helices are spiral structures stabilized by hydrogen bonds, beta-sheets are extended strands connected by hydrogen bonds, and coils are unstructured regions. Each has distinct characteristics and roles in protein function.
Secondary structure prediction is essential for understanding protein function, designing drugs, and studying protein evolution. It helps researchers identify functional domains and predict protein-protein interactions.
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