polypeptide
(noun)
Any polymer of (same or different) amino acids joined via peptide bonds.
Examples of polypeptide in the following topics:
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Protein Structure
- A protein's primary structure is the unique sequence of amino acids in each polypeptide chain that makes up the protein.
- Really, this is just a list of which amino acids appear in which order in a polypeptide chain, not really a structure.
- For example, the pancreatic hormone insulin has two polypeptide chains, A and B.
- Rarely does a single secondary structure extend throughout the polypeptide chain.
- Proteins made from a single polypeptide will not have a quaternary structure.
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Amino Acids
- An amino acid contains an amino group, a carboxyl group, and an R group, and it combines with other amino acids to form polypeptide chains.
- The resulting chain of amino acids is called a polypeptide chain.
- Each polypeptide has a free amino group at one end.
- When reading or reporting the amino acid sequence of a protein or polypeptide, the convention is to use the N-to-C direction.
- Although the terms polypeptide and protein are sometimes used interchangeably, a polypeptide is technically any polymer of amino acids, whereas the term protein is used for a polypeptide or polypeptides that have folded properly, combined with any additional components needed for proper functioning, and is now functional.
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The Mechanism of Protein Synthesis
- Catalyzing the formation of a peptide bond removes the bond holding the growing polypeptide chain to the P-site tRNA.
- The growing polypeptide chain is transferred to the amino end of the incoming amino acid, and the A-site tRNA temporarily holds the growing polypeptide chain, while the P-site tRNA is now empty or uncharged.
- This causes the polypeptide chain to detach from its tRNA, and the newly-made polypeptide is released.
- The growing polypeptide chain is attached to the tRNA in the ribosome P site.
- This creates a peptide bond between the C terminus of the growing polypeptide chain and the A site amino acid.
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The Central Dogma: DNA Encodes RNA and RNA Encodes Protein
- These nucleotide triplets are called codons; they instruct the addition of a specific amino acid to a polypeptide chain.
- Three of the 64 codons terminate protein synthesis and release the polypeptide from the translation machinery.
- Translation is the process by which mRNA is decoded and translated to produce a polypeptide sequence, otherwise known as a protein.
- In translation, a cell decodes the mRNA's genetic message and assembles the brand-new polypeptide chain.
- The main function of tRNA is to transfer a free amino acid from the cytoplasm to a ribosome, where it is attached to the growing polypeptide chain. tRNAs continue to add amino acids to the growing end of the polypeptide chain until they reach a stop codon on the mRNA.
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The Protein Synthesis Machinery
- For instance, ribosomes may consist of different numbers of rRNAs and polypeptides depending on the organism.
- A ribosome is a complex macromolecule composed of structural and catalytic rRNAs, and many distinct polypeptides.
- The peptidyl-tRNA carrying the growing polypeptide chain is held in the P site.
- (More accurately, the growing polypeptide chain is added to each new amino acid bound in by a tRNA.)
- (More accurately, the growing polypeptide chain is added to each new amino acid brought in by a tRNA.)
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Types and Functions of Proteins
- These amino acids are covalently attached to one another to form long linear chains called polypeptides, which then fold into a specific three-dimensional shape.
- Sometimes these folded polypeptide chains are functional by themselves.
- Other times they combine with additional polypeptide chains to form the final protein structure.
- Sometimes non-polypeptide groups are also required in the final protein.
- For instance, the blood protein hemogobin is made up of four polypeptide chains, each of which also contains a heme molecule, which is ring structure with an iron atom in its center.
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Lipid-Derived, Amino Acid-Derived, and Peptide Hormones
- The structure of peptide hormones is that of a polypeptide chain (chain of amino acids).
- The peptide hormones include molecules that are short polypeptide chains, such as antidiuretic hormone and oxytocin produced in the brain and released into the blood in the posterior pituitary gland.
- Amino acid-derived and polypeptide hormones are water-soluble and insoluble in lipids.
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The Incorporation of Nonstandard Amino Acids
- A protein (also called a polypeptide) is a chain of amino acids.
- For instance, the peptide hormone insulin is cut twice after disulfide bonds are formed, and a propeptide is removed from the middle of the chain; the resulting protein consists of two polypeptide chains connected by disulfide bonds.
- Also, most nascent polypeptides start with the amino acid methionine because the "start" codon on mRNA also codes for this amino acid.
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Denaturation and Protein Folding
- At higher pHs pepsin's conformation, the way its polypeptide chain is folded up in three dimensions, begins to change.
- It is often possible to reverse denaturation because the primary structure of the polypeptide, the covalent bonds holding the amino acids in their correct sequence, is intact.
- The chaperonins clump around the forming protein and prevent other polypeptide chains from aggregating.
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Proteolytic Degradation
- The breakdown of proteins into smaller polypeptides, or its respective amino acids, are necessary for metabolic and cellular homeostasis.
- Polypeptides are commonly broken down via hydrolysis of the peptide bonds by utilizing a class of enzymes called proteases.