The abbreviated name,‘mfold web server’,describes a number of closely related software applications available on the World Wide Web (WWW) for the prediction of the secondary structure of single stranded nucleic acids. The objective of this web server is to provide easy access to RNA and DNA folding and hybridization software to the scientific community at large. By making use of universally available web GUIs (Graphical User Interfaces),the server circumvents the problem of portability of this software. Detailed output,in the form of structure plots with or without reliability information,single strand frequency plots and ‘energy dot plots’, are available for the folding of single sequences. A variety of ‘bulk’ servers give less information,but in a shorter time and for up to hundreds of sequences at once. The portal for the mfold web server is http://www.bioinfo.rpi.edu/applications/ mfold. This URL will be referred to as ‘MFOLDROOT’.

/pdf/mfold-web-server-for-nucleic-acid-folding-and-hybridization-3pzoe1h05m.pdf

Mfold web server for nucleic acid folding and hybridization prediction

A procedure for the isolation of deoxyribonucleic acid from micro-organisms

http://www.protocol-online.org/forums/index.php?app=core&module=attach&section=attach&attach_id=2894

Studies on transformation of Escherichia coli with plasmids

3.2.3. Hydroformylation 2467 3.2.4. Dimerization 2468 3.2.5. Oxidative Cleavage and Ozonolysis 2469 3.2.6. Metathesis 2470 4. Terpenes 2472 4.1. Pinene 2472 4.1.1. Isomerization: R-Pinene 2472 4.1.2. Epoxidation of R-Pinene 2475 4.1.3. Isomerization of R-Pinene Oxide 2477 4.1.4. Hydration of R-Pinene: R-Terpineol 2478 4.1.5. Dehydroisomerization 2479 4.2. Limonene 2480 4.2.1. Isomerization 2480 4.2.2. Epoxidation: Limonene Oxide 2480 4.2.3. Isomerization of Limonene Oxide 2481 4.2.4. Dehydroisomerization of Limonene and Terpenes To Produce Cymene 2481

Chemical Routes for the Transformation of Biomass into Chemicals

High-performance liquid chromatography is a promising alternative for determining the G+C content of bacterial deoxyribonucleic acid (DNA). The method which we evaluated involves enzymatic degradation of the DNA to nucleosides by P1 nuclease and bovine intestinal mucosa alkaline phosphatase, separation of the nucleosides by high-performance liquid chromatography, and calculation of the G+C content from the apparent ratios of deoxyguanosine and thymidine. Because the nucleosides are released from the DNA at different rates, incomplete degradation produces large errors in the apparent G+C content. For partially purified DNA, salts are a major source of interference in degradation. However, when the salts are carefully removed, the preparation and degradation of DNA contribute little error to the determination of G+C content. This method also requires careful selection of the chromatographic conditions to ensure separation of the major nucleosides from the nucleosides of modified bases and precise control of the flow rates. Both of these conditions are achievable with standard equipment and C18 reversed-phase columns. Then the method is precise, and the relative standard deviations of replicate measurements are close to 0.1%. It is also rapid, and a single measurement requires about 15 min. It requires small amounts of sample, and the G+C content can be determined from DNA isolated from a single bacterial colony. It is not affected by contamination with ribonucleic acid. Because this method yields a direct measurement, it may also be more accurate than indirect methods, such as the buoyant density and thermal denaturation methods. In addition, for highly purified DNA, the extent of modification can be determined.

Precise Measurement of the G+C Content of Deoxyribonucleic Acid by High-Performance Liquid Chromatography

Formation and properties of polyribonucleotide-polydeoxy-ribonucleotide helical complexes.

https://www.pnas.org/content/pnas/54/4/1167.full.pdf

The polarity of messenger translation in protein synthesis

Some observations on the configuration and precipitating activity of antibodies.

We report the DNA sequence of a cDNA clone complementary to the 5' end of the chick pro alpha 2(I) mRNA. The sequence enables us to deduce the amino acid sequence of this region, which has been refractory to conventional protein sequencing techniques. Its importance lies in the role of the prepropeptide in secretion, triple helix formation of the mature protein and initiation of fibrillogenesis. We have also located four of the five exons which code for this region on the genome. One exon is only 11bp in size and appears to code exclusively for the signal propeptidase cleavage site. This is an extreme example of an exon defining a functional unit.

Chick pro alpha 2 (I) collagen gene: exon location and coding potential for the prepropeptide.

Light scattering and viscosity studies have been made on solutions of sodium desoxyribonucleate in 0.2 M NaCl adjusted to pH values of 6.5, 3.0, and 2.6 by dialysis in order to prevent contact with more concentrated acid. It is found that the molecular weight (7,700,000) is the same under these three conditions and remains so when the acid solutions are adjusted to pH 6.5. Upon lowering the pH the molecular size decreases due to increased coiling, but returns to its original value upon reneutralization. At pH 2.6 the mean radius of the molecule is less than half the pH 6.5 value. It is argued that these observations invalidate the existing evidence for degradation or disaggregation accompanying the appearance of new titratable groups. However, it is likely that most of the amino groups have not been titrated at pH 2.6 at the ionic strength employed here. Consequently the possibility remains that the stability at pH 2.6 is a consequence of a hydrogen-bonded structure that is still largely intact.

Paul Doty

Papers

Formation and properties of polyribonucleotide-polydeoxy-ribonucleotide helical complexes.

The polarity of messenger translation in protein synthesis

Some observations on the configuration and precipitating activity of antibodies.

Chick pro alpha 2 (I) collagen gene: exon location and coding potential for the prepropeptide.

The changes induced in sodium desoxyribonucleate by dilute acid