Triplet Excited Fluoroquinolones as Mediators for Thymine Cyclobutane Dimer Formation in DNA

2007 ◽  
Vol 111 (25) ◽  
pp. 7409-7414 ◽  
Author(s):  
Virginie Lhiaubet-Vallet ◽  
M. Consuelo Cuquerella ◽  
Jose V. Castell ◽  
Francisco Bosca ◽  
Miguel A. Miranda
Keyword(s):  
Dimer Formation ◽  
Cyclobutane Dimer

Photochemical behavior of some α, β-unsaturated lactams. Dependence of reaction path on multiplicity

1969 ◽  
Vol 47 (15) ◽  
pp. 2781-2786 ◽  
Author(s):  
E. Cavalieri ◽  
S. Horoupian
Keyword(s):  
Excited State ◽  
Spectral Properties ◽  
Reaction Path ◽  
Triplet Excited State ◽  
Excited Singlet ◽  
Cleavage Reaction ◽  
Dimer Formation ◽  
Cyclobutane Dimer ◽  
Direct Irradiation ◽  
Cyclobutane Dimers

Whereas direct irradiation (2537 Å) of 5,6-dihydro-4,6,6-trimethyl-2(1H)-pyridone 1 (1a) produced almost exclusively the cleavage products 2 and 3, the acetophenone sensitized reaction (3500 Å) gave a single cyclobutane dimer. In contrast, direct (2537 Å) or sensitized (acetophenone, 3500 Å) irradiation of the homo derivative 7 of compound 1 gave approximately the same mixture of two cyclobutane dimers. It was thus demonstrated that dimer formation proceeded by way of a triplet excited state and that the cleavage reaction most probably occurred via an excited singlet state.A structure for each cyclobutane dimer in the seven-membered series was proposed on the basis of its spectral properties.

scholarly journals Base Pairing Enhances Fluorescence and Favors Cyclobutane Dimer Formation Induced upon Absorption of UVA Radiation by DNA

2011 ◽  
Vol 133 (14) ◽  
pp. 5163-5165 ◽  
Author(s):  
Akos Banyasz ◽  
Ignacio Vayá ◽  
Pascale Changenet-Barret ◽  
Thomas Gustavsson ◽  
Thierry Douki ◽  
...  
Keyword(s):  
Base Pairing ◽  
Dimer Formation ◽  
Cyclobutane Dimer ◽  
Uva Radiation

DLTS study of the oxygen dimer formation kinetics in silicon

2009 ◽  
Vol 404 (23-24) ◽  
pp. 4576-4578
Author(s):  
Nikolai Yarykin ◽  
Jörg Weber
Keyword(s):  
Dimer Formation ◽  
Formation Kinetics

A Computational Study of Three Frequent Mutations of EGFR and their Effects on Protein Dimer Formation and Non-Small Cell Lung Cancer Drug Resistance

2016 ◽  
Vol 11 (3) ◽  
pp. 382-391
Author(s):  
Zhiyong Shen ◽  
Debby D. Wang ◽  
Lichun Ma ◽  
Hong Yan ◽  
Maria P. Wong ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Drug Resistance ◽  
Computational Study ◽  
Small Cell ◽  
Cancer Drug ◽  
Small Cell Lung ◽  
Dimer Formation ◽  
Cancer Drug Resistance ◽  
Protein Dimer ◽  
Frequent Mutations

scholarly journals Solvent Exposure and Ionic Condensation Drive Fuzzy Dimerization of Disordered Heterochromatin Protein Sequence

Biomolecules ◽  
2021 ◽  
Vol 11 (6) ◽  
pp. 915
Author(s):  
Jazelli Mueterthies ◽  
Davit A. Potoyan
Keyword(s):  
Phase Separation ◽  
Low Complexity ◽  
Nuclear Bodies ◽  
Disordered Proteins ◽  
Solvent Exposure ◽  
Ion Release ◽  
Dimer Formation ◽  
Eukaryotic Organisms

Proteins with low complexity, disordered sequences are receiving increasing attention due to their central roles in the biogenesis and regulation of membraneless organelles. In eukaryotic organisms, a substantial fraction of disordered proteins reside in the nucleus, thereby facilitating the formation of nuclear bodies, nucleolus, and chromatin compartmentalization. The heterochromatin family of proteins (HP1) is an important player in driving the formation of gene silenced mesoscopic heterochromatin B compartments and pericentric regions. Recent experiments have shown that the HP1a sequence of Drosophila melanogaster can undergo liquid-liquid phase separation under both in vitro and in vivo conditions, induced by changes of the monovalent salt concentration. While the phase separation of HP1a is thought to be the mechanism underlying chromatin compartmentalization, the molecular level mechanistic picture of salt-driven phase separation of HP1a has remained poorly understood. The disordered hinge region of HP1a is seen as the driver of salt-induced condensation because of its charge enriched sequence and post-translational modifications. Here, we set out to decipher the mechanisms of salt-induced condensation of HP1a through a systematic study of salt-dependent conformations of single chains and fuzzy dimers of disordered HP1a hinge sequences. Using multiple independent all-atom simulations with and without enhanced sampling, we carry out detailed characterization of conformational ensembles of disordered HP1a chains under different ionic conditions using various polymeric and structural measures. We show that the mobile ion release, enhancement of local transient secondary structural elements, and side-chain exposure to solvent are robust trends that accompany fuzzy dimer formation. Furthermore, we find that salt-induced changes in the ensemble of conformations of HP1a disordered hinge sequence fine-tune the inter-chain vs. self-chain interactions in ways that favor fuzzy dimer formation under low salt conditions in the agreement with condensation trends seen in experiments.

scholarly journals AMP-activated Protein Kinase Regulates HNF4α Transcriptional Activity by Inhibiting Dimer Formation and Decreasing Protein Stability

2003 ◽  
Vol 278 (30) ◽  
pp. 27495-27501 ◽  
Author(s):  
Yu Holly Hong ◽  
Usha S. Varanasi ◽  
Wenbo Yang ◽  
Todd Leff
Keyword(s):  
Protein Kinase ◽  
Protein Stability ◽  
Transcriptional Activity ◽  
Dimer Formation ◽  
Amp Activated Protein Kinase
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