Interactions between identical DNA double helices
نویسندگان
چکیده
منابع مشابه
Homologous Pairing between Long DNA Double Helices.
Molecular recognition between two double stranded (ds) DNA with homologous sequences may not seem compatible with the B-DNA structure because the sequence information is hidden when it is used for joining the two strands. Nevertheless, it has to be invoked to account for various biological data. Using quantum chemistry, molecular mechanics, and hints from recent genetics experiments, I show her...
متن کاملHydrodynamic interactions between rotating helices.
Escherichia coli bacteria use rotating helical flagella to swim. At this scale, viscous effects dominate inertia, and there are significant hydrodynamic interactions between nearby helices. These interactions cause the flagella to bundle during the "runs" of bacterial chemotaxis. Here we use slender-body theory to solve for the flow fields generated by rigid helices rotated by stationary motors...
متن کاملDirect recognition of homology between double helices of DNA in Neurospora crassa
Chromosomal regions of identical or nearly identical DNA sequence can preferentially associate with one another in the apparent absence of DNA breakage. Molecular mechanism(s) underlying such homology-dependent pairing phenomena remain(s) unknown. Using Neurospora crassa repeat-induced point mutation (RIP) as a model system, we show that a pair of DNA segments can be recognized as homologous, i...
متن کاملMultiple interactions between transmembrane helices generate the oligomeric alpha1b-adrenoceptor.
Combinations of coimmunoprecipitation, single-cell fluorescence resonance energy transfer, and cell-surface time-resolved fluorescence resonance energy transfer demonstrated protein-protein interactions and quaternary structure for the alpha(1b)-adrenoceptor. Self-association of transmembrane domain 1 and its interaction with the full-length receptor indicated a symmetrical interface provided b...
متن کاملIdentifying interactions between transmembrane helices from the adenosine A2A receptor.
The human adenosine A(2A) receptor (A(2A)R) is an integral membrane protein and a member of the G-protein-coupled receptor (GPCR) superfamily, characterized by seven transmembrane (TM) helices. Although helix-helix association in the lipid bilayer is known to be an essential step in the folding of GPCRs, the determinants of their structures, folding, and assembly in the cell membrane are poorly...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Physical Review E
سال: 2020
ISSN: 2470-0045,2470-0053
DOI: 10.1103/physreve.101.032414