https://tiikmpublishing.com/proceedings/index.php/biotech/issue/feedProceedings of International Conference on BioScience and Biotechnology2019-05-28T06:08:13+0530Yasodara Premarathneproceedings@tiikmpublishing.comOpen Journal Systems<p>The Proceedings of International Conference on BioScience and Biotechnology is based on a theme which is annually introduced according to the novel trends in the field of BioScience and Biotechnology. This issue brings out the best research studies presented at the International Conference on BioScience and Biotechnology.</p>https://tiikmpublishing.com/proceedings/index.php/biotech/article/view/247THE STUDY OF BARLEY RESISTANCE TO CADMIUM AND ZINC2019-05-28T06:08:12+0530R. A. Alybayevaraya_aa@mail.ruA. E. Bektiyaraigera_22.96@mail.ruS. D. Atabayevasauleat@yandex.kzS. Sh. Asrandinaasaltanat@yandex.kz<p>The rich resource and raw material potential of Kazakhstan was the basis for the development of a powerful industry. However, it is industrial centers that are the areas of the highest pollution of the environment with heavy metals. A significant increase in the content of heavy metals in the environment is accompanied by their accumulation in plants, which has a negative impact on their growth, development and productivity. In this regard, the study of the reaction of plants to the action of heavy metals causes not only great scientific, but also practical interest. Different varieties of barley have been studied under conditions of natural soil contamination with heavy metals. The aim of the study is to identify resistant to cadmium and zinc barley varieties. The objects of the study are four varieties of barley from the collection of the East Kazakhstan Research Institute of Agriculture: Siberian Avant-Garde, Modern, Omsk, and Donetsk-8. The yield and survival of barley plants during the spring-summer vegetation were studied. Determination of physiological parameters was carried out according to the method of field experience. Productivity was determined by the direct method. Heavy metals (cadmium and zinc) were determined by atomic absorption with atomization in a flame and graphite furnace. The largest crop among the studied varieties has Modern variety of barley. The best survival is also demonstrated by Modern variety of barley. Donetsk-8 barley variety accumulates the least cadmium in the seeds. Siberian Avant-Garde barley variety accumulates the minimum amount of zinc in the seeds and at the same time is characterized by good survival during the spring-summer vegetation under conditions of polymetallic soil contamination.</p>2019-05-28T00:00:00+0530Copyright (c) 2019 Authorshttps://tiikmpublishing.com/proceedings/index.php/biotech/article/view/248STRUCTURAL CHARACTERIZATION OF NPAS4-ARNT DIMERIZATION THROUGH COMPUTATIONAL SIMULATION2019-05-28T06:08:13+0530Ammad Fahimmfbhatti@asab.nust.edu.pkZaira Rehmanrehman.zaira@yahoo.comMuhammad Faraz Bhattimfbhatti@asab.nust.edu.pkNasar Virknasarvirk@gmail.comRehan Zafar Paracharehanzfr@gmail.com<p>Neuronal PAS Domain Protein 4 (Npas4) is an activity dependent transcription factor harboring basic helix-loop-helix (bHLH)-PAS domain, mediating the expression of target genes involved in neuro-transmission. NPAS4 crucially regulates response to various excitatory stimuli and has a role in GABAergic neuronal synapse development. Functionally, NPAS4 as a transcription factor dimerizes with the ARNT protein to serve as complete transcription factor and start the transcription of downstream genes. However, NPAS4 dimerization characteristics with ARNT has not been studied so far. Hence the current study aimed to identify the interaction pattern of NPAS4-ARNT complex through computational docking via HADDOCK. The interaction pattern were determined through pdbSum. The electrostatic surface calculations were performed through APBS plugins in PyMOL. The results indicated that PASB domain of NPAS4 is involved in interactions with the PAS B domain of ARNT. A toll of 136 structures generated by HADDOCK were further grouped into 14 clusters. The cluster with the minimum energy value of -82.6 KJ/mol was then further selected for interaction analysis. The results showed that there is one salt bridge, 12 H-bonding interactions and 156 non-bonded contacts between two proteins. The important interactions among two proteins are Asp224:NPAS4 and Gln421:ARNT, Asp229:NPAS4 and Ser442:ARNT, Glu232:NPAS4 and Thr361:ARNT, Phe240, Glu241:NPAS4, and Arg440:ARNT. The electrostatic potential of these two proteins revealed the binding interface of NPAS4 and ARNT to be neutral hence favoring hydrophobic interactions. The findings can help elucidate Npas4 role in interacting with other neuronal proteins involved in neuronal signaling. Moreover, the interaction findings provide useful comparative insight with other bHLH proteins.</p>2019-05-28T00:00:00+0530Copyright (c) 2019 Authors