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English: Functional proteins have four levels of structural organization: 1) Primary Structure : the linear structure of amino acids in the polypeptide chain 2) Secondary Structure : hydrogen bonds between peptide group chains in an alpha helix or beta 3) Tertiary Structure : three-dimensional structure of alpha helixes and beta helixes folded
In general, protein structures are classified into four levels: primary (sequences), secondary (local conformation of the polypeptide chain), tertiary (three-dimensional structure of the protein fold), and quaternary (association of multiple polypeptide structures). Structural bioinformatics mainly addresses interactions among structures taking ...
Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function.The structure of these molecules may be considered at any of several length scales ranging from the level of individual atoms to the relationships among entire protein subunits.
Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a repeating unit of a polymer.
Nuclear-interacting partner of ALK (NIPA), also known as zinc finger C3HC-type protein 1 (ZC3HC1), is a protein that in humans is encoded by the ZC3HC1 gene on chromosome 7. [5] [6] It is ubiquitously expressed in many tissues and cell types though exclusively expressed in the nuclear subcellular location.
An alpha-helix with hydrogen bonds (yellow dots) The α-helix is the most abundant type of secondary structure in proteins. The α-helix has 3.6 amino acids per turn with an H-bond formed between every fourth residue; the average length is 10 amino acids (3 turns) or 10 Å but varies from 5 to 40 (1.5 to 11 turns).
The secondary-structure elements are connected by "loop" or "coil" regions of non-repetitive conformation, which are sometimes quite mobile or disordered but usually adopt a well-defined, stable arrangement. [16] The overall, compact, 3D structure of a protein is termed its tertiary structure or its "fold".
Protein quaternary structure describes the number and arrangement of multiple folded protein subunits in a multi-subunit complex. It includes organizations from simple dimers to large homooligomers and complexes with defined or variable numbers of subunits. [1] In contrast to the first three levels of protein structure, not all proteins will ...