Biochemistry and Molecular Biology Official Blog

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Wednesday, 12 February 2020

MODE OF ACTION OF EBOLA VIRUS


MODE OF ACTION OF EBOLA VIRUS
INTRODUCTION TO EBOLA:
          It was seen in Congo the very first time that’s why it is also known as the Congo virus. Later it was also seen that it affects some of the African countries.it becomes a very hot topic for scientists when an amazing fact was known about it that it has the death rate of 90%.there is a large number of Ebola virus types known till now but the most dangerous one is the Zaire virus. [MODE OF ACTION OF EBOLA VIRUS].

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TRANSFORMATION OF EBOLA VIRUS:
        There are many ways of transformation of the Ebola virus as other viruses but mainly thus viruses spread by the aerosol transformation. With the help of air. Another method which it uses is direct contact with the contaminated agents. Or it may spread by the feces of the Ebola-infected person.

SYMPTOMS OF EBOLA VIRUS INFECTION:
       Symptoms of Ebola virus is very much hard to define because it has very much similar symptoms of infection as other viruses have. Such as vomiting, chest pain, headache, are the major ones. All these symptoms may appear in any case of a viral infection is it is very hard to differentiate between Ebola and other virus infections.

STRUCTURE OF EBOLA VIRUS:
       Diameter of Ebola virus is about 80nm. And the length of Ebola is 800nm. A nucleocapsid is located at the center of Ebola virus. Ebola(Zaire) virus has an ssRNA genome on both sides of which NP, VP30, VP35, and L proteins are present. All this structure is wrapped by the envelope.

EBOLA PLAYS WITH OUR IMMUNE SYSTEM:
      Ebola dodges our immune system in a very great way. When our immune system is scanning our body about a problem in the meantime Ebola has done its work and our body has destroyed. When our body comes to know about the Ebola virus till that time our body is damaged till such a level that it is not possible to recover it.

MODE OF ACTION OF EBOLA VIRUS:
        Ebola actually uses our immune system to proceed infection cycle. Its infectivity is enhanced in the presence of antibodies produced by the immune response. A virus starts its activity after the attachment with the receptor on the cell. A ligand C1q helps the antibody-virus complex to bind with the receptor present on the cell. This ligand supports the Ebola to bind with the cell.
       Once the virus bind with the receptor it enters the host cell. After entering the body, the very first target of Ebola is macrophages and monocytes which are the immune cells Ebola destroy them by using the immune system, complement system of the host. Now white blood cells play their role against the virus and release the proinflammatory cytokines in a very large amount these cytokines, these cytokines enhance the permeability vascular endothelium.
Now because of these cytokines, the action virus can easily approach its secondary target or inner components of the cell which are the main target of the virus. The second task performed by the cytokine is to bring the new large number of the macrophages, and as the number of macrophages increases the virus has much more target to attack so due to a large amount of the macrophage the Ebola spread in a very large surface area. And have very much potential to cause disease. When cytokines are bringing new macrophages in the meantime virus destroy the hepatocytes. due to the hepatocytes destruction, the cell signal cannot be passed into the bloodstream.

ENTRY INTO ENDOTHELIAL:
         Now with the help of GP-mediated receptors the Ebola get entry into the endothelial cell. by using macro pinocytosis. With the help of micro pinocytosis, the small vesicle structure is formed which is known as macropinosomes. Now finally by using these macropinosomes viruses move into the acidic area of the cell at these compartments of the cell the PH dependent fusion of the virus takes place into endothelial cells among various viral and cell membranes. So as a result of this fusion and invagination the cell become totally disconnected from its neighbor cells as well as from its base. And completely loses its function as well as stability. Now Ebola replicates itself and made particles. These particles leave the cell with the help of lipids rafts and leave behind the destabilized vascular system. This system causes a huge blood loss which is the main characteristic of the patient affected by Ebola.


WHAT IS FUNCTION OF IMMUNE SYSTEM WHEN EBOLA TAKES CONTROL ON THE HOST BODY?
      At the time when Ebola takes control on the body, the immune system is completely out of control.


ACTION OF VP35 VIRAL PROTEIN:
       At the mean while the protein vp35 of the virus take command on the production of the interferon
And regulate their production


ACTION OF GP VIRAL PROTEIN:
       The GP protein takes control of the white blood cells regulation and trap the white blood cell into the circulatory system. That they could not perform their function.
      Now the remaining immune cells such as macrophages and monocytes release the cytokines these cytokines which are the proinflammatory due release of these cytokines virus take control over the vascular endothelium efficiently and damage it.


PARADOXICAL STATE:
            This state of the body is the paradoxical state it is the condition in which the patient dies because of hypovolemic shock from a huge hemorrhage and. Formation of huge clots of blood occur around the all body.
Keywords: [ ebola outbreak, ebola virus china, Ebola virus cure, ebola virus deaths, Ebola virus uk, Mode of action of ebola virus ]

Sunday, 8 December 2019

FULLY FUNDED Exchange Program for Pakistani Students in USA

FULLY FUNDED Exchange Program for Pakistani Students

SUSI 2020 Summer Exchange Program in the United States *NO IELTS/TOEFL Required.*
Students from any field of study can apply. *Undergraduates of (2,3,4,5,6,7) Semester are Eligible*

Type of scholarship: Fully funded by the Department of the United States
Duration: 5-6 Weeks

*SUSI Student Leaders 2020:* Male & Female Students Apply
Link: https://bit.ly/2OVQKMK
*Deadline*: December 17, 2019.

*SUSI Women Leaders 2020:*
Female Students Can Apply
Link: http://bit.ly/2DVZjlL
*Deadline*: December 10, 2019

*SUSI TIPS* https://bit.ly/2qWTuRZ

*Videos sessions* for your proper guidance and the preparation of the statement of purpose to increase the chances of your selection:

http://bit.ly/Video_Session_01
http://bit.ly/Video_Session_02
http://bit.ly/Video_Session_03
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You can also visit  : Japanese scholarships 


Thursday, 5 December 2019

Japanese and Chinese fully funded Scholarship Updates for December 2020

Scholarship Updates

Ritsumeikan University

Japan Fully Funded MEXT Scholarships 2020 
under Japanese Government for International Students from all over the world.
Apply Website: https://scholarships365.info/ritsumeikan-university-scholarship

Offers: Airfare, Tuition, and Monthly Allowance


Programs: MS and Ph.D. Programs.

Deadline: 8th Jan 2020
Scholarships365, No Agent,
Direct Apply toUniversity. Shanghai Jiao Tong University Scholarship 2020
Fully Funded for International Students
(All Countries Students Can Apply).

Apply Website: https://scholarships365.info/Shanghai-Jiaotong-University-Scholarship
Programs: 100+ Masters and Ph.D.
Programs Offers: Full Tuition, Accommodation, Monthly Stipend, and Medical. Deadline: 15th December 2019 No Agent, Direct Apply.

Japanese fully funded Scholarship Updates for December 2020
Japanese fully funded Scholarship Updates for December 2020

Wednesday, 4 September 2019

World Youth forum 2019 Sharm El-Sheikh, Egypt








World Youth forum 2019, Sharm El-Sheikh, Egypt is Now Back.* Fully Funded International Conference 2019

Biggest International Conference for all International Students & Egyptians. This Year in 2019 More than 5000 Participants will Participate.

Participants with *any academic disciplines* are eligible to apply. There are *No Academic or CGPA Requirements.* It’s not an academic program. It’s a Leadership Program

The aim of the WYF is to send a message of Peace & Make World Better.

Round Airfare Tickets, Meals, Full Accommodation, Local Transportation will be provided.

How to Apply Online *Link:* https://youtu.be/YjlVwnSxrJ8

Official Website Link: https://wyfegypt.com/index.php

*Deadline:* 10th November 2019

Keep Support & Share this Post in all your Facebook and WhatsApp groups for others Help. For More latest Upcoming Opportunities Stay Tuned. If you need any guidance Comments Or Inbox.

Registrations for *KPITB's Digital Internship Program 2019-20 are open now




Registrations for *KPITB's Digital Internship Program 2019-20* are open now.

*Apply Now:* http://assami.kp.gov.pk/

Last date to apply: September 20, 2019

*SALIENT FEATURES:*

- Monthly stipend of PKR 14000/-

- ICT capacity building of KP youth to enable them to compete in Global ICT markets

- Skill ready workforce to ensure speedy expansion of ICT industry in KP

*ELIGIBILITY CRITERIA FOR SOFTWARE HOUSES:*

- 16 years of Education in IT, CS or ICT
FOR CALL CENTERS

- 14 years of Education (BA or equivalent)

*TERMS & CONDITIONS:*

- Applicants must have domicile of Khyber Pakhtunkhwa or Newly Merged Districts of Khyber Pakhtunkhwa (Former F.A.T.A)

- Applicants that graduated in the last 3 years (after 30th July 2016) are eligible to apply

- Fresh graduates may also apply by submitting final year transcript

- Applicants that already have Post-qualification work experience are not eligible

- Applicants that have already availed KPITB’s Digital Internship are not eligible

*Admin*

Admissions open in Universities

*ADMISSION ALERT*

UET Lahore announces Admissions for BSc Engineering Programs
*Deadline:* 16-09-2019
*Level*: Bachelor

VIRTUAL UNIVERSITY OF PAKISTAN, LAHORE
*Deadline:* 14-09-2019
*Level*: PhD, Bachelor, MA/MSc, MS

UNIVERSITY OF THE PUNJAB, LAHORE
*Deadline:* 06-09-2019
*Level*: MS

LAHORE COLLEGE FOR WOMEN UNIVERSITY, LAHORE
*Deadline:* 13-09-2019
*Level*: Bachelor, MS, PhD, MA/MSc

GOVERNMENT COLLEGE UNIVERSITY, LAHORE
*Deadline:* 04-09-2019
*Level*: MS

RACHNA COLLEGE OF ENGINEERING AND TECHNOLOGY, GUJRANWALA
*Deadline:* 16-09-2019
*Level*: Bachelor
ZIA-UD-DIN MEDICAL UNIVERSITY, KARACHI
*Deadline:* 10-09-2019
*Level*: MS

DHA SUFFA UNIVERSITY(MAIN CAMPUS), KARACHI
*Deadline:* 14-09-2019
Admissions open in Universities

*Level*: Bachelor, MS, PhD

THE GOVERNMENT SADIQ COLLEGE WOMEN UNIVERSITY, BAHAWAL PUR
*Deadline:* 20-09-2019
*Level*: Bachelor, MS, MA/MSc, PhD

UNIVERSITY OF HARIPUR, HARIPUR
*Deadline:* 10-09-2019
*Level*: Bachelor, MS, MA/MSc

MUHAMMAD NAWAZ SHARIF UNIVERSITY OF AGRICULTURE, MULTAN
*Deadline:* 20-09-2019
*Level*: Bachelor

NATIONAL UNIVERSITY OF MODERN LANGUAGES ( FAISALABAD CAMPUS ), FAISALABAD
*Deadline:* 30-08-2019
*Level*: MS, Bachelor, MA/MSc

SARHAD UNIVERSITY OF SCIENCE & INFORMATION TECHNOLOGY, PESHAWAR
*Deadline:* 30-08-2019
*Level*: Bachelor, MA/MSc

ABBOTTABAD UNIVERSITY OF SCIENCE AND TECHNOLOGY, ABBOTTABAD
*Deadline:* 02-09-2019
*Level*: Bachelor

IMPERIAL COLLEGE OF BUSINESS STUDIES, LAHORE
*Deadline:* 05-09-2019
*Level*: Bachelor

BZU Multan
*Deadline* : 25-9-19
*LeveL*: BS and MS

RIPHAH INTERNATIONAL UNIVERSITY, ISLAMABAD
*Deadline:* 08-09-2019
*Level*: Bachelor

ABBOTTABAD UNIVERSITY OF SCIENCE AND TECHNOLOGY, ABBOTTABAD
*Deadline:* 13-09-2019
*Level*: MS, MA/MSc

CITY UNIVERSITY OF SCIENCE & INFORMATION TECHNOLOGY, PESHAWAR
*Deadline:* 16-09-2019
*Level*: Bachelor, MS, PhD, MA/MSc

LAHORE LEADS UNIVERSITY, LAHORE
*Deadline:* 17-09-2019
*Level*: Bachelor, MS, MA/MSc

THE UNIVERSITY OF LAHORE ( ISLAMABAD CAMPUS ), ISLAMABAD
*Deadline:* 06-09-2019
*Level*: Bachelor

NATIONAL TEXTILE UNIVERSITY FAISALABAD, SUB CAMPUS, KARACHI
*Deadline:* 14-09-2019
*Level*: Bachelor

THE UNIVERSITY OF LAHORE ( ISLAMABAD CAMPUS ), ISLAMABAD
*Deadline:* 15-09-2019
*Level*: Bachelor


*Admin*

Sunday, 1 September 2019

Do not die as Nikola

Nikola Tesla was Serbian origin scientist. He was inventor of alternate current and radio. He has hundreds of small and big inventions and discoveries to his credit.

But he died in ABJECT poverty.

If you are genius and still hand to mouth then what is the fun to be genius.

In the world of Thomas Edisons and Marconies, never end up as Nikola Tesla.

Get out of idealism. Monetize your talent. You, your family, your kids deserve better quality of life.


Friday, 18 January 2019

Mitochondrial DNA can be inherited from fathers, not just mothers

The DNA of eukaryotic organisms (such as animals, plants and fungi) is stored in two cellular compartments: in the nucleus and in organelles called mitochondria, which transform nutrients into energy to allow the cell to function. The nucleus harbours most of our genes, tightly packaged into 46 chromosomes, of which half are inherited from our mother’s egg and half from our father’s sperm. By contrast, mitochondrial DNA (mtDNA) was thought to derive exclusively from maternal egg cells, with no paternal contribution1Writing in Proceedings of the National Academy of Sciences, Luo et al.2 challenge the dogma of strict maternal mtDNA inheritance in humans, and provide compelling evidence that, in rare cases, the father might pass on his mtDNA to the offspring, after all.
Human eggs contain more than 100,000 copies of mtDNA, whereas sperm contain approximately 100 copies3. Early hypotheses suggested that paternal mtDNA molecules became diluted in number relative to maternal mtDNA ones in the fertilized egg, but these ideas were replaced when evidence from various organisms, such as the uni-cellular alga Chlamydomonas reinhardtii4 and medaka fish5, showed that paternal mtDNA is rapidly eliminated after fertilization. For decades, researchers have speculated on why healthy organisms obtain their cellular powerhouses from just one parent and on the possible evolutionary advantages conferred by mitochondrial genes inherited in this fashion.
A healthy individual’s mtDNA molecules are mostly identical. But in people with diseases caused by mtDNA mutations, normal and mutant mtDNA molecules typically coexist in a single cell — a situation termed heteroplasmy6. Disease severity is often associated with the amount of mutant mtDNA in cells, which is in turn determined by events that occurred when the person’s mother was still an embryo7. The developing eggs in the female embryo go through an ‘mtDNA bottle-neck’, in which the number of mtDNA copies is first reduced and then amplified to more than 100,000 copies8,9. Accordingly, variable amounts of mutant and normal mtDNA are present in the mature eggs of an individual woman, and, therefore, in the cells of her offspring. This phenomenon influences the severity of diseases caused by mtDNA mutations, and can lead to very different manifestations between individuals from the same family7.
Luo and colleagues identified three families with mtDNA heteroplasmy that could not be explained by maternal inheritance. The story started with a young boy suspected of having a mitochondrial disease. The authors performed high-resolution mtDNA sequencing, but did not identify any disease-causing mtDNA mutations. However, their analysis uncovered unusually high levels of mtDNA heteroplasmy. Intriguingly, the same unusual pattern of mtDNA variation was found in the boy’s mother and in his two healthy sisters (Fig. 1).


Figure 1 | Family tree revealing paternal inheritance of mitochondrial DNA (mtDNA). Luo et al.2 sequenced the mtDNA of several members of a family in which many individuals had a high level of mtDNA heteroplasmy (the presence of distinct genetic variants in the same cell). This mtDNA variability is denoted by two colours in the same silhouette of an individual. The analysis showed that some of the individuals with heteroplasmy had inherited mtDNA from both of their parents, breaking the usual pattern of exclusive maternal inheritance of mtDNA. Luo et al. suggest that the ability to inherit paternal mtDNA is a genetic trait.

To trace the origin of this mysterious mtDNA pattern, Luo et al. extended their investigation to the previous generation. Sequencing of the mtDNA of the boy’s maternal grandparents revealed an unexpected contribution: his unusual mtDNA pattern seemed to be the product of mtDNA from both grandparents. The authors went on to identify two additional and unrelated families that had biparental mitochondrial transmission. A similar scenario was previously observed in an individual with mitochondrial disease who had a paternally inherited mtDNA variant10. Together, these reports provide evidence for biparental mitochondrial inheritance in humans.
Human disease-causing mtDNA mutations were originally reported in 1988 (refs 6, 11)6,11, and more than 200 such mutations (see go.nature.com/2fucdqt) have been discovered since then, most of them occurring in a hetero-plasmic context7. More-over, the estimated frequency of mutations of matrilineal mtDNA has made it a useful and often-used tool in studies of ancestry and evolution, as well as in forensic identification12. Human mtDNA has also been a valuable tool in archaeology, because its small size (16,569 base pairs) and circular form make it more resistant to degradation than is nuclear DNA (which has around 3 billion base pairs)13.
Given this long and multifaceted research history, why would paternal mtDNA have remained undetected? Luo et al. suggest that mtDNA heteroplasmy is often overlooked in diagnostics when it does not involve a disease-causing variant. Although this might be true to some extent, it is a rather unsatisfactory explanation in this era of deep DNA sequencing. Nevertheless, Luo and colleagues’ findings should provoke a re-assessment of the extensive global mtDNA sequencing data available, for those wishing to unearth further instances of atypical heteroplasmy. If the paternal contribution to mtDNA is more common than previously realized, this could alter some estimated timings of human evolution, because these are often based on predictions of mtDNA sequence variation under the assumption of exclusive maternal inheritance.
Although biparental inheritance of mtDNA and heteroplasmy coincided with disease symptoms in some of the individuals studied by Luo et al., the authors’ data do not demonstrate a causal link with disease. In fact, we cannot be certain that the study participants have mitochondrial disease, because no specific examinations to confirm this diagnosis are reported. Further study is needed to identify more cases of potential paternal mtDNA inheritance, and to determine the functional consequences of such heteroplasmy. Notably, this knowledge is relevant to mitochondrial-donation therapy (“three-parent babies”), which aims to prevent the transmission of disease-causing mtDNA to offspring14, but which can also potentially generate individuals with two types of mtDNA, one from the donor and another from the mother.
Could the amount of paternal mtDNA in a fertilized egg or developing embryo be deliberately boosted to diminish the adverse effects of mutant maternal mtDNA when this is present? This is an interesting option, but still far from reality. In addition to evading elimination, paternal mtDNA molecules would need to have a considerable replicative advantage over maternal ones to reach meaningful proportions.
Will Luo and colleagues’ findings affect the counselling of individuals carrying disease-causing mtDNA mutations who are considering having children? Not greatly, because paternal mitochondrial transmission seems to be exceedingly rare in humans. At present, this discovery represents an interesting conceptual breakthrough, rather than one that will directly influence clinical practice.
Previous work15 has shown that mitophagy, the process by which cells ‘eat’ their own mitochondria, has a role in the selective elimination of paternal mitochondria. Given our rapidly expanding knowledge of mammalian mitophagy in vivo16, these rare instances of paternal mtDNA transmission might be attributed to defective mitochondrial turnover. The inheritance pattern of paternal mtDNA in Luo and colleagues’ study suggests that a yet unidentified gene on one of the autosomes (non-sex chromosomes) is involved in eliminating paternal mitochondria. The families in whom paternal mtDNA inheritance was observed provide an exciting opportunity to decipher the signalling pathways that modulate paternal mitochondrial elimination and prevent biparental mitochondrial transfer.
Nature 565, 296-297 (2019)
doi: 10.1038/d41586-019-00093-1


Monday, 14 January 2019

Protein modification fine-tunes the cell’s force producers

Actin is one of the most abundant proteins in our cells. It assembles into filaments that produce force for many processes that are essential to the life of animals, plants and fungi — including cell migration and division, and muscle contraction1. The organization and dynamics of actin filaments in cells are regulated by a large array of actin-binding proteins. Moreover, post-translational modifications of actin — the addition of certain chemical groups to its amino-acid residues, or their removal — is thought to have a role in controlling the cellular functions of actin filaments. However, the proteins that catalyse these changes have been elusive. Writing in Nature, Wilkinson et al.2 report the identification of the long-sought enzyme that catalyses the methylation (addition of a methyl group) of actin, and shed light on the biological role of this post-translational modification in animals.


Some post-translational modifications of actin are present in all isoforms (structural variants) of the protein, whereas others are more specific. 


The protein’s amino-terminal region can be modified by acetylation (addition of an acetyl group) and arginylation (addition of an arginine amino-acid residue)3. Recent studies identified the enzyme responsible for amino-terminal acetylation of actin and demonstrated that this modification affects the elongation and depolymerization of actin filaments4,5.
Most actin isoforms are also methylated at a particular histidine amino-acid residue known as His73, which is close to the site to which one of two nucleotides, ATP or ADP, binds. Hydrolysis of ATP to ADP plus one free phosphate molecule is essential for the turnover of actin filaments, and hence for their ability to produce force in cells. Although methylation of His73 was identified more than five decades ago6, the enzyme responsible and the biological functions of this modification have remained unknown.
The study by Wilkinson et al. and a related study published in eLife7 report that the SETD3 protein is the enzyme that methylates actin at His73 (Fig. 1). This is the first time an actin methyltransferase (an enzyme that catalyses methylation) has been identified, and also the first time a histidine methyltransferase has been identified in animals. Earlier work suggested that SETD3 methylates lysine amino-acid residues in histone H38, a protein associated with DNA, but Wilkinson et al. convincingly demonstrate that SETD3 is not a methyltransferase for histones. The authors provide extensive biochemical and cell-biological evidence showing that, at least in mammals, SETD3 is the only enzyme that catalyses the His73 methylation of actin, and that actin is the only substrate of SETD3. They also show that SETD3 and His73 methylation of actin are present in a wide range of organisms, including plants and animals, but that SETD3 is not present in budding yeast, which also lacks His73-methylated actin.
Figure 1 | Methylation of actin by the SETD3 protein.Wilkinson et al.2 show that SETD3 catalyses the addition of a methyl chemical group (methylation) to a histidine amino-acid residue (His73) of the protein actin, and that this modification fine-tunes the protein’s function. His73 is close to a site to which either an ATP or an ADP nucleotide binds. The switch between ATP and ADP is essential to allow actin filaments to produce force in cells. Other evolutionarily conserved post-translational modifications of actin, including the addition of an acetyl chemical group (acetylation) to its amino-terminal region, are distant from the nucleotide-binding pocket of actin.
Why does SETD3 methylate actin, but not other proteins? To answer this question, Wilkinson et al. determined the atomic structure of SETD3 in complex with a short chain of amino acids (a peptide) that has the same amino-acid sequence as the region of actin around His73. They found that this peptide occupies an extended groove in the domain of SETD3 that is responsible for the enzyme’s methyltransferase activity. The interface between SETD3 and the actin peptide has many specific interactions, which explain why SETD3 binds to and methylates only actin.
To examine the biological functions of this post-translational modification, Wilkinson et al. generated ‘knockout’ mice and cell lines in which the gene encoding SETD3 was inactive. They observed that actin is no longer methylated in these models. Surprisingly, the mice lacking SETD3 seemed to be healthy, which demonstrates that methylation of actin at His73 is not essential in mammals. However, female mice lacking SETD3 took longer to give birth than did mice in which this protein was present. The delay resulted from defective contraction of certain muscles of the uterus during labour. Moreover, the migration of SETD3-knockout cells in culture was slower than that of wild-type cells. Finally, non-methylated actin purified from the SETD3-knockout cells polymerized slightly more slowly than did methylated actin, and had a faster rate of exchange of nucleotides on single actin molecules than did actin purified from wild-type cells.
These experiments provide evidence that, despite being evolutionarily conserved across a broad group of organisms, methylation at His73 is not essential for the normal functioning of actin. Instead, this modification seems to fine-tune the protein’s biochemical properties and cellular roles.
Future studies should investigate the SETD3-knockout mice in more detail for possible additional differences from wild-type mice, and should examine the effects of SET
D3 deletion in other model organisms. Also, the effects of His73 methylation on actin biochemistry should be studied more precisely. Previously, analysing these effects was possible only by mutating the His73 residue in actin or by producing human actin in yeast, in which this protein cannot be methylated9,10. The new findings will enable careful side-by-side comparison of wild-type actin and actin that lacks methylation only at His73. 
Because His73 is close to the nucleotide-binding site of actin, it will be especially interesting to study how this modification affects the functions of proteins that catalyse nucleotide exchange on actin11and that rely on ATP hydrolysis and subsequent release of free phosphate for their interactions with actin filaments12.
Nature 565, 297-298 (2019)
doi: 10.1038/d41586-018-07882-0

Friday, 21 December 2018

Call for Microsoft Imagine Cup 2019 Pakistan

The Higher Education Commission & Microsoft are collaborating to bring to faculty, students and academia Microsoft’s Imagine Cup - the world’s most prestigious student technology competition, bringing together student innovators from all over the world. 
Each year, a team is chosen from Pakistan that completes against the best from around the world, to get a chance to win $100,000 USD.
This is an amazing opportunity for you to participate and utilize your potential by bringing your imagination and their passion towards creating technological solutions and compete to win great prizes! 
Microsoft along with the HEC is striving for nurturing innovation and transforming technology among the youth of Pakistan. It is hoped that the platform made available through this collaborated effort will help students of Pakistan in recognition of their innovative ideas and relative projects. 
To ensure quality output, the competing teams from Pakistan are initially evaluated in Regional finals that are held in different cities. The winning teams compete for National Finals to select a National winner. A mix of judges from both academia (as directed by HEC) and industry evaluates the solutions during both rounds. Both regional finals as well as National Finals evaluations are made based over team’s deliverables submitted online on the Imagine Cup portal using the criterion listed in 2019 Imagine Cup Competition Official Rules and Regulations (attached with this email).
Regional & National Finals detailed per team plan and relative winner’s announcements will be made on Official MSDN Pakistan Community Blog: https://blogs.msdn.microsoft.com/pakistan/.
The deadline for the project submission for the Regional Finals is 15 January 2019.
All interested students are requested to contact their faculty members concerned as early as possible to participate in the Imagine Cup 2019 with reference of this email. 
Please click onto https://imaginecup.microsoft.com/en-us/pakistan for further details. 





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