title: Staphylococcal nuclease reviewed: a prototypic study in contemporary enzymology. IV. The nuclease as a model for protein folding.
abstract: This is the last in a series of four articles in which the chemical, enzymological and crystallographic work on Ribonucleate (deoxyribonucleate)-3'-nucleotidohydrolase, EC 3.1.4.4 (staphylococcal nuclease, micrococcal nuclease) will be reviewed and correlated. This article discusses the use of the nuclease as a model system for the study of the mechanisms and energetics of the folding-unfolding reaction in proteins and for the study of the interrelationships between amino acid sequence and three-dimensional structure.
mesh_terms: D000939:Epitopes; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008024:Ligands; D008836:Micrococcal Nuclease / Q000276:immunology / Q000378:metabolism; D008956:Models, Chemical; D010446:Peptide Fragments; D011487:Protein Conformation; D011489:Protein Denaturation; D013816:Thermodynamics
chemical_list: D000939:Epitopes; D008024:Ligands; D010446:Peptide Fragments; D008836:Micrococcal Nuclease