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activation energy amount of energy required to get a reaction started active site pocket or groove on the surface of the enzyme where catalysis occurs allosteric site place on an enzyme where a molecule that is not a substrate may bind, thus changing the shape of the enzyme and influencing its ability to be active. amino acid organic molecule with amino and carboxyl groups catalyst chemical agent that changes the rate of a reaction without being consumed by the reaction coenzyme cofactor that is an organic molecule cofactor nonprotein helpers for catalytic activity covalent bond sharing of a pair of valence electrons by two atoms dehydration reaction denaturation molecules connected by a reaction where 2 molecules are covalently bonded to each other with loss of a water molecule when proteins lose their quaternary, tertiary, and secondary structures as a result of external stressors enzyme subgroup of catalysts -proteins or protein-based -highly specific enzyme-substrate complex the intermediate formed when a substrate molecule interacts with the active site of an enzyme functional group chemical groups affect molecular function by being directly involved in chemical reactions hydrogen bond non-covalent attraction between a hydrogen and an electronegative atom hydrophillic any substance that has an affinity for water hydrophobic substances that are nonionic and non-polar that seem to repel water. inhibitor substance that slow down or stops an enzyme catalyzed reaction isomer compounds that have the same numbers of atoms of the same elements but different structures and different properties monomer repeating units that serve as the building blocks of a polymer polar covalent bond one atom is bonded to a more electronegative atom; electrons of bonds are not shared equally. polar molecule overall charge of molecule is unevenly distributed polymer long molecule consisting of many similar or identical building blocks linked by covalent bonds polypeptide polymer of many amino acids linked by peptide bonds polypeptide bond bonds that hold together amino acids in a polypeptide chain primary structure unique linear sequence of amino acids protein consist of one or more polypeptides folded and coiled into specific conformations quaternary structure proteins that consist of more than one polypeptide chain. secondary structure how the polypeptide coils or folds into two distinct shapes substrate reactants in enzyme assisted reactions tertiary structure intricate three-dimensional shape or conformation of a protein that is superimposed on its secondary structure Van der Waals interaction ever-changing regions of positive and negative charge that enable all atoms and molecules to stick to one another