On the stability of furanopyrimidin-2-one bases in oligonucleotidesElectronic supplementary information (ESI) available: experimental procedures for the preparation of the new compounds, protocols for the thermal denaturation and enzyme digestion experiments. See http://www.rsc.org/suppdata/cc/b4/b402559h/

2004 ◽  
pp. 1304 ◽  
Author(s):  
Guan-Sheng Jiao ◽  
Kevin Burgess
Keyword(s):  
Thermal Denaturation ◽  
Enzyme Digestion ◽  
Supplementary Information ◽  
The Stability ◽  
New Compounds

The stability of maize nuclei to restriction enzyme digestion differs with transcriptional activity

Caryologia ◽  
1993 ◽  
Vol 46 (1) ◽  
pp. 63-69 ◽  
Author(s):  
Valeria Mirkova ◽  
Maria Ivanchenko ◽  
Lubomir Stoilov ◽  
Jordanka Zlatanova
Keyword(s):  
Restriction Enzyme ◽  
Transcriptional Activity ◽  
Enzyme Digestion ◽  
Restriction Enzyme Digestion ◽  
The Stability

scholarly journals TADOSS: computational estimation of tandem domain swap stability

2018 ◽  
Vol 35 (14) ◽  
pp. 2507-2508 ◽  
Author(s):  
Aleix Lafita ◽  
Pengfei Tian ◽  
Robert B Best ◽  
Alex Bateman
Keyword(s):  
Large Scale ◽  
Domain Swapping ◽  
Coarse Grained ◽  
Supplementary Information ◽  
Simulation Studies ◽  
Computational Tools ◽  
Domain Swap ◽  
Computational Estimation ◽  
High Propensity ◽  
The Stability

Abstract Summary Proteins with highly similar tandem domains have shown an increased propensity for misfolding and aggregation. Several molecular explanations have been put forward, such as swapping of adjacent domains, but there is a lack of computational tools to systematically analyze them. We present the TAndem DOmain Swap Stability predictor (TADOSS), a method to computationally estimate the stability of tandem domain-swapped conformations from the structures of single domains, based on previous coarse-grained simulation studies. The tool is able to discriminate domains susceptible to domain swapping and to identify structural regions with high propensity to form hinge loops. TADOSS is a scalable method and suitable for large scale analyses. Availability and implementation Source code and documentation are freely available under an MIT license on GitHub at https://github.com/lafita/tadoss. Supplementary information Supplementary data are available at Bioinformatics online.

scholarly journals Stabilization of nucleic acids by unusual polyamines produced by an extreme thermophile, Thermus thermophilus

2005 ◽  
Vol 388 (2) ◽  
pp. 427-433 ◽  
Author(s):  
Yusuke TERUI ◽  
Mio OHNUMA ◽  
Kaori HIRAGA ◽  
Etsuko KAWASHIMA ◽  
Tairo OSHIMA
Keyword(s):  
Molecular Structure ◽  
Thermal Denaturation ◽  
Thermus Thermophilus ◽  
Amino Nitrogen ◽  
The Other ◽  
Extreme Thermophile ◽  
Scanning Calorimetry ◽  
Extreme Thermophiles ◽  
The Stability ◽  
Ammonium Compounds

Extreme thermophiles produce two types of unusual polyamine: long linear polyamines such as caldopentamine and caldohexamine, and branched polyamines such as quaternary ammonium compounds [e.g. tetrakis(3-aminopropyl)ammonium]. To clarify the physiological roles of long linear and branched polyamines in thermophiles, we synthesized them chemically and tested their effects on the stability of ds (double-stranded) and ss (single-stranded) DNAs and tRNA in response to thermal denaturation, as measured by differential scanning calorimetry. Linear polyamines stabilized dsDNA in proportion to the number of amino nitrogen atoms within their molecular structure. We used the empirical results to derive formulae that estimate the melting temperature of dsDNA in the presence of polyamines of a particular molecular composition. ssDNA and tRNA were stabilized more effectively by tetrakis(3-aminopropyl)ammonium than any of the other polyamines tested. We propose that long linear polyamines are effective to stabilize DNA, and tetrakis(3-aminopropyl)ammonium plays important roles in stabilizing RNAs in thermophile cells.

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