IndietroProtein Folding definitions
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1/15IndietroSkip to main contentIndietroPrimary Structure
Linear sequence of amino acids in a polypeptide chain, determining folding information through unique R groups. Peptide Bond
Covalent linkage connecting amino acids in a polypeptide, forming the backbone of protein structure. Secondary Structure
Local folding patterns of the polypeptide backbone, mainly alpha helices and beta sheets stabilized by hydrogen bonds. Alpha Helix
Rigid, cylindrical structure formed by hydrogen bonds between every fourth amino acid, common in skin proteins. Beta Sheet
Sheet-like arrangement of polypeptide segments, stabilized by hydrogen bonds, can be parallel or antiparallel. Tertiary Structure
Three-dimensional conformation of a single polypeptide, integrating motifs and domains for function and stability. Structural Motif
Combination of secondary structures forming a stable 3D unit, often with a specific function within a protein. Coiled Coil
Motif where two or three alpha helices wrap around each other, creating a stable, functional structure. Protein Domain
Independent, stable segment of a polypeptide, often recurring in different proteins and responsible for specific functions. Domain Shuffling
Evolutionary process mixing domains among proteins, generating new combinations and functional diversity. Quaternary Structure
Assembly of multiple polypeptide subunits, forming a functional protein complex with non-covalent or disulfide bonds. Subunit
Individual polypeptide chain within a multimeric protein, which may be identical or different from others. Homodimer
Protein complex composed of two identical polypeptide subunits. Heterodimer
Protein complex composed of two non-identical polypeptide subunits. Unstructured Region
Flexible, disordered segment of a protein, often providing adaptability and unique functional roles.
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