title: [Hydrogen exchange and proteolytic degradation of ribonuclease A. The local splitting of the native structure and the conformation of loop segmentes].
abstract: The limited proteolytic sites or nicksites are present only in one of the five loops of the RNase A molecule. The splitted loop 15-23 connects two structural domains in the hinge region of the interdomain contacts of the V-shaped molecule. The other four loops are inside two domains, 64-71 and 112-115 in the domain I (1-19, 47-81, 102-106) and 36-42 and 88-95 in the domain II (20-46, 82-101). Because of enhanced chain flexibility of the splitted loop in the pH-dependent conformational isomerization, deformation of its structure is slighter under the influence of the intermolecular contacts in the crystal lattice and more significant changes occur in loop conformation at the formation of the 3D swapped dimer of the RNase A molecule. The proteolytic splitting of the 15-23 loop proceeds due to the local fluctuation of the native protein structure.
authors.forename: L V
authors.initials: LV
authors.lastname: Abaturov
authors.forename: N G
authors.initials: NG
authors.lastname: Nosova
mesh_terms: D000818:Animals; D003460:Crystallization; D019281:Dimerization; D006859:Hydrogen / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D007536:Isomerism; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D059748:Proteolysis; D051381:Rats; D012259:Ribonuclease, Pancreatic / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D006859:Hydrogen; D012259:Ribonuclease, Pancreatic