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The primary structure of a biological polymer to a large extent determines the three-dimensional shape (tertiary structure). Protein sequence can be used to predict local features , such as segments of secondary structure, or trans-membrane regions.
The primary structure of a protein is determined by the gene corresponding to the protein. A specific sequence of nucleotides in DNA is transcribed into mRNA , which is read by the ribosome in a process called translation .
The primary structure of a biopolymer is the exact specification of its atomic composition and the chemical bonds connecting those atoms (including stereochemistry).For a typical unbranched, un-crosslinked biopolymer (such as a molecule of a typical intracellular protein, or of DNA or RNA), the primary structure is equivalent to specifying the sequence of its monomeric subunits, such as amino ...
[36]: 37 Biochemists often refer to four distinct aspects of a protein's structure: [36]: 30–34 Primary structure: the amino acid sequence. A protein is a polyamide. Secondary structure: regularly repeating local structures stabilized by hydrogen bonds. The most common examples are the α-helix, β-sheet and turns. Because secondary ...
The primary structure of a protein, its linear amino-acid sequence, determines its native conformation. [11] The specific amino acid residues and their position in the polypeptide chain are the determining factors for which portions of the protein fold closely together and form its three-dimensional conformation.
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).
Studies have identified a number of target proteins for structure determination, including extracellular proteins that may be involved in pathogenesis, iron-regulatory proteins, current drug targets, and proteins predicted to have novel folds. So far, structures have been determined for 708 of the proteins encoded by M. tuberculosis.
Several lines of evidence have been presented in favor of the notion that primary protein sequence contains all the information required for overall three-dimensional protein structure, making the idea of a de novo protein prediction possible. First, proteins with different functions usually have different amino acid sequences.