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Chapter 4 Cell Funct
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| Term | Definition |
|---|---|
| active site | region of an enzyme surface to which a substrate molecule binds before it undergoes a catalyzed reaction |
| allosteric | describes a protein that exists in two or more confromations depending of the binding of a molecule (ligand) at a site other than the catalytic site |
| alpha helix | common structural motif of proteins in which a linear sequence of amino acids folds into a right-handed helix stabilized by internal hydrogen bonding between backbone atoms |
| beta sheet | folding pattern found in many proteins in which neighboring regionsof the polypeptide chain associate with each other through hydrogen bonds to give a rigid, flattened structure |
| binding site | region on the surface of a protein, typically a cavity or groove, that is complementary in shape to, and forms multiple noncovalent bonds with, a second molecule (the ligand) |
| conformation | spatial location of the atoms of a molecule. the precise shape of a protein or other macromolecule in three dimensions |
| disulfide bond (s-s bond) | covalent linkage formed between two sulfhydryl groups on cysteines. common way to join two proteins to link together different pats of the same protein in the extracellular space |
| enzyme | a protein that catalyzes a specific chemical reaction |
| feedback inhibition | a form of metabolic control in which the end-product of a chain of enzymatic reactions reduces the activity of an enzyme early in the pathway |
| fibrous proteins | a protein with an elongated shape (i.e.- collagen); able to associate into long filamentous structures |
| globular protein | any protein with an approximately round shape. most enzymes are globular |
| GTP-binding protein | allosteric protein whose conformation is determined by the association with either GTP or GDP. includes many protein in cell signaling |
| helix | an elongated structure in which a filament or thread twists in regular fashion around a central axis |
| ligand | molecule such as a hormone or a neurotransmitter that binds to a specific site on a protein |
| motor protein | protein such as myosin that was energy derived from ATP hydrolysis to propel itself along a protein filament or polymeric molecule |
| peptide bond | chemical bonds between the carbonyl group of one amino acid and the amino group of a second amino acid - a special form of amide linkage |
| polypeptide | linear polymer composed of multiple amino acids. proteins are large polpeptides, and the two names can be used interchangeably |
| polypeptide chain | the backbone of atoms containing repeating peptide bonds that runs through a protein molecule and to which amino acid side chains are attached |
| primary structure | linear sequence of amino acids in a polypeptide held together by peptide bonds (covalent bonds) |
| secondary structure | localized, repetitive coiling or folding of the polypeptide backbone- held together with H-bonds between atoms of backbone and does NOT involve side chains (alpha helix/beta sheet/random coil) |
| tertiary structure | overall 3-D structure of one polypeptide, held together by interactions between side chain-side chain or side chain-backbone |
| quaternary structure | overall 3-D fold of 2 or more polypeptide chains; side chain-side chain or side chain-backbone interactions |
| protein domain | compact and stable folded structure; region of polypeptide that can be separated by one or two cuts of polypeptide backbone and still fold - usually specific for single function |
| protein family | group of proteins that have a similar sequence, similar structure, similar function |
| protein kinase | one of a very large number of enzymes that transfers the terminal phosphate group of ATP to a specific amino acid of a target protein |
| protein phosphotase (phosphoprotein phophotase) | enzyme that removes, by hydrolysis, a phosphate group from a protein, usually with high specificity |
| protein phosphorylation | the covalent addition of a phosphate group to a side chain of a protein catalyzed by a protein kinase |
| side chain | portion of an amino acid not involved in making peptide bonds and which give each amino acid its unique properties |
| subunit | a chemical group or molecule that forms part of a larger molecule; a monomer. (i.e.- amino acid to protein) |
| transition site | chemical structure that forms transiently in the course of a reaction and has the highest free energy of any reaction intermeidate |
Created by:
jcamillo
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