منابع مشابه
Comparative Investigation of R213G Mutation in DNA-Binding Domain of P53 Protein via Molecular Dynamics Simulation
Introduction: P53 is a tumor suppressor protein with numerous missense mutations identified in its gene. These mutations are observed in a vast number of cancers. R213G is one of them which has a role in metastatic lung cancers. In this research, R213G was studied in comparison with the wild type via molecular dynamics simulation. Method: For the three-dimensional structure of the wild-type P53...
متن کاملComparative Investigation of R213G Mutation in DNA-Binding Domain of P53 Protein via Molecular Dynamics Simulation
Introduction: P53 is a tumor suppressor protein with numerous missense mutations identified in its gene. These mutations are observed in a vast number of cancers. R213G is one of them which has a role in metastatic lung cancers. In this research, R213G was studied in comparison with the wild type via molecular dynamics simulation. Method: For the three-dimensional structure of the wild-type P53...
متن کاملDNA-Binding Protein Gene
Four independent, spontaneous mutants of the adenovirus type 2-simian virus 40 hybrid Ad2+ND3 that allow efficient growth in monkey cells were isolated previously (C. W. Anderson, Virology 111:263-269, 1981). All four mutations have been mapped within the coding sequence for the adenovirus DNA-binding protein by marker rescue analysis. DNA sequence analysis of a region of ca. 1,000 base pairs s...
متن کاملDNA-protein binding force chip.
Force measurements provide new fundamental and complementary information on biomolecular interactions, particularly in the high and low affi nity regimes, which may hardly be obtained otherwise. [ 1 ] We introduce a label free parallel format assay to quantify the binding forces in protein–DNA complexes on a chip in crowded environments. It employs arrays of molecular force balances with fl uor...
متن کاملProtein-protein interactions facilitate DNA binding by the glucocorticoid receptor DNA-binding domain.
We have studied the interaction of the DNA-binding domain of the glucocorticoid receptor with a glucocorticoid response element from the tyrosine aminotransferase gene. This response element consists of two binding sites (half-sites) for the glucocorticoid receptor DNA-binding domain. The sequences of these two half-sites are not identical, and we have previously shown that binding occurs prefe...
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ژورنال
عنوان ژورنال: Frontiers in Chemistry
سال: 2018
ISSN: 2296-2646
DOI: 10.3389/conf.fchem.2018.01.00030