An Empirical Potential Study of the Interaction of L—;Lysine—;L—;Alanine—;L—;Alanine Tripeptide with Four models of B—;DNA with different Compositions

Abstract

The empirical potential including the intra- and intermolecular energy terms was used to study the interaction of L-Lysine-L-Alanine-L-Alanine Tripeptide with four models of B-DNA with different compositions. On the basis of a detailed search of the respective potential energy surface, it was found that the peptide is preferentially bounded to the AT-rich sequences. Analysis of the different energy contributions indicated that the electrostatic term is responsible for this preference. The results agree with the experimental data on the selectivity of some DNA—binding proteins and polypeptides to AT—;rich DNA.     

Novel screening methods — biosensors

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Translational biomaterials — the journey from the bench to the market — think ‘product’

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Molecular pharming — VLPs made in plants

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Drinking water microbiology — from measurement to management

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Cyanobacterial H<Subscript>2</Subscript> production — a comparative analysis

Several unicellular and filamentous, nitrogen-fixing and non-nitrogen-fixing cyanobacterial strains have been investigated on the molecular and the physiological level in order to find the most efficient organisms for photobiological hydrogen production. These strains were screened for the presence or absence of hup and hox genes, and it was shown that they have different sets of genes involved in H₂ evolution. The uptake hydrogenase was identified in all N₂-fixing cyanobacteria, and some of these strains also contained the bidirectional hydrogenase, whereas the non-nitrogen fixing strains only possessed the bidirectional enzyme. In N₂-fixing strains, hydrogen was mainly produced by the nitrogenase as a by-product during the reduction of atmospheric nitrogen to ammonia. Therefore, hydrogen production was investigated both under non-nitrogen-fixing conditions and under nitrogen limitation. It was shown that the hydrogen uptake activity is linked to the nitrogenase activity, whereas the hydrogen evolution activity of the bidirectional hydrogenase is not dependent or even related to diazotrophic growth conditions. With regard to large-scale hydrogen evolution by N₂-fixing cyanobacteria, hydrogen uptake-deficient mutants have to be used because of their inability to re-oxidize the hydrogen produced by the nitrogenase. On the other hand, fermentative H₂ production by the bidirectional hydrogenase should also be taken into account in further investigations of biological hydrogen production.Abbreviations Chl chlorophyll - MV methyl viologen     

RNA epigenetics — chemical messages for posttranscriptional gene regulation

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Ipso-substitution — the hidden gate to xenobiotic degradation pathways

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Making connections — strategies for single molecule fluorescence biophysics

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Nanostructured sensors for biomedical applications — a current perspective

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Extremozymes — biocatalysts with unique properties from extremophilic microorganisms

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Protein homeostasis — more than resisting a hot bath

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Presence of Ornithine in the Urate-binding α<Subscript>1</Subscript>—<Subscript>2</Subscript>Globulin

THE urate-binding α₁–α₂ globulin has been isolated from human plasma in a highly purified state¹. The protein was purified by DEAE-‘Sephadex’, ammonium sulphate precipitation and semi-preparative Polyacrylamide gel electrophoresis. The urate-binding α₁–α₂ globulin is a rod-shaped glycoprotein, containing 12.1% carbohydrate, with an isoelectric point of 4.6 and a molecular weight of 67,000 ± 4,000. Amino-acid analysis indicated an unknown basic compound which appeared as an extra peak just in front of lysine¹. To identify this compound, high voltage paper electrophoresis has been carried out on a plate electrophoresis apparatus in pyridine-acetate buffer pH 3.5. A spot separated out corresponding to ornithine. Amino-acid analysis on a BC-200 automatic analyser (Bio-Cal Instruments Co., West Germany), with a 54 cm column at 55° C and with 0.35 M sodium citrate buffer, pH 5.28, as elution buffer at a flow-rate of 150 ml./h, showed that ornithine was present. The presence of ornithine in the protein hydrolysate was also verified by gas chromatography/mass spectrometry².     

Safeguarding China′s Botanical HeritageFoundation item: BGCI′S Program in China——BGCI′s integrated conservation programme in China

China′s rich floral diversity includes more than 33000 vascular plant species, representing approximately 10 percent of all known plant species. Over half of these species are endemic to China. However, China′s rapid economic development in the last 30 years and continuous population growth have seriously damaged plant resources in the wild and the ecological environment, resulting in a dramatic increase in the number of endangered species. There are nearly 4000 to 5000 higher plants that are now threatened or on the verge of extinction. To help halt the loss of Chinese plant diversity, Botanic Gardens Conservation International (BGCI) has developed a China programme and opened its first office based in Guangzhou in 2008. This office works along with Chinese partners aiming to secure Chinese plant diversity through integrated conservation approaches with reintroduction/population reinforcement, engagement of local communities in conservation activities, capacity building in horticulture and environmental education and public outreach.     

Heavy enzymes — experimental and computational insights in enzyme dynamics

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Mechanisms of mechanosensing — mechanosensitive channels,function and re-engineering

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trans-Cyclooctene — a stable,voracious dienophile for bioorthogonal labeling

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Microfluidics in systems biology — hype or truly useful?

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