Match the descriptions / definitions with the term they best describe Three dime
ID: 189279 • Letter: M
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Match the descriptions / definitions with the term they best describe Three dimensional relationship of the different polypeptide .Coiled-coil chains in a multisubunit protein or protein complex B. Quaternary structure C.Side chain Common folding pattern in proteins in which a linear sequence of amino acids folds into a right-handed coil stabilized by internal hydrogen-bonding between polypeptide backbone atoms. Polypeptide backbone Protein domain Alpha-helix Secondary structure Tertiary structure The amino acid sequence of a protein A region on the surface of a protein that can interact with another molecule through noncovalent bonding. c H. B. Three-dimensional arrangement of alpha-helices and beta- sheets within a single polypeptide, typically stabilized by a 1. Beta-sheet variety of noncovalent bonds, including ionic and hydrogen bonds, and nonpolar interactions / hydrophobic force. Primary structure K. Protein L. The chain of repeating carbon and nitrogen atoms, linked by peptide bonds, in a protein. Binding site Common structural motif in proteins in which different sections of the polypeptide chain run alongside each other and are joined together by hydrogen bonding between atoms of the polypeptide backbone. Portion of a polypeptide chain that has a discrete tertiary structure of its own and can often fold independently of the rest of the chain A. Regular local folding patterns in a protein, including alpha- helix and beta-sheetExplanation / Answer
1) Three-dimensional relationship of the different polypeptide chains in a multisubunit protein or protein complex - Quaternary structure.
2) Common folding pattern in proteins, in which a linear sequence of amino acids folds into a right-handed helix stabilized by internal hydrogen bonding between backbone atoms - Alpha helix.
3) The amino acid sequence of a protein - Primary structure.
Linear sequence of monomer units in a polymer, such as the amino acid sequence of a protein primary structure.
4) Region on the surface of protein that can interact with another molecule through noncovalent bonding - Binding site.
6) The chain of repeating carbon and nitrogen atoms, linked by peptide bonds, in a protein- Polypeptide backbone
7) Common structural motif in proteins in which different sections of the polypeptide chain run alongside each other and are joined together by hydrogen bonding between atoms of the polypeptide backbone - Beta helix.
8) Protein domains are structural units that fold more or less independently of each other.It is the portion of a protein that has a tertiary structure of its own. larger proteins are generally composed of several domains, each connect to the next by short flexible regions of polypeptide chain. homologous domains are recognized in many different proteins.
9) Regular local folding patterns in a protein, including alpha helix and beta sheet - Secondary structure
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