Scientists often conduct scientific research to gather more information about a specific field of study. You may have the impression that scientists often wear white coats and work in a lab. However, this is not the case because there are scientists who are communicators and developers, as well as entrepreneur and explorer scientists. There are also investigators and policy scientists, as well as regulators and teacher scientists. All of them greatly benefit from information technology in ways listed below.
Polymers are large molecules that are composed of several other smaller subunits. There are natural polymers found in the environment, and there are also synthetic or man-made polymers. Each of these macromolecules has different unique physical and chemical properties that make them beneficial for a wide variety of purposes. To better understand this, it is a good idea to get to know the different classifications of polymers first.
The recent pandemic brought about by COVID-19 has left a lot of people to rethink the way we conduct our daily lives. From people in authority to the common person you see in the street, no one has not made some acclimation to the new normal in response to the virus. But at the forefront in the battle against the pandemic, the people in the sciences have worked tirelessly in the past months to promote the continuity and normalcy in our day-to-day enterprise. Here are the areas in science that have stepped into the spotlight because of the virus:
The UK is home to some of the most advanced research facilities in the world, many of them housed within the nation’s many world-renowned universities. These facilities aren’t just there for the benefit of students and staff; they are also regularly open to academics and representatives of commercial businesses. Many excellent facilities in the country will be of interest to any science researcher. No matter what your chosen field of academic study is or where your research interests lie, there are lab facilities in the UK that are worth seeing. Below, we have listed just some of the world-class lab facilities that UK universities have to offer.
Laboratory tools and equipment don’t come cheap. And making sure your machines are all in top shape is a must, whether you’re managing a science lab at school or a clinic. Yes, availing of routine maintenance for your facilities is the key to preserve your devices. But giving relevant training to your staff on how to handle the equipment effectively is equally important. Doing this is worth it for a lot of reasons.
In September of this year, a sudden and unexpected explosion at a vast Soviet-era virology campus in Siberia (called Vector) caused widespread panic, as various buildings were set ablaze and windows were torn from their frames. At the heart of the most immediate concerns was the potential spread of dangerous viruses, and while it’s still not clear whether or not the explosion was the result of a deliberate attack, there has been a renewed focus on reinforcing safety structures and minimising the impact of future breaches. Make no mistake; the creation of safe and secure science laboratories is crucial to the environment and the general public as a whole, while this also guarantees the accuracy of findings and drives numerous, high-profile industries.
Most proteins become functional once they acquire their native three-dimensional structure, which is dictated by the primary amino acid sequence of the protein. Denaturation is the process in which proteins, or more specifically, nucleic acids, lose their three-dimensional structure. The occurrence of denaturation can be due to many external factors and subsequently, this event can irreversibly disrupt the protein’s functionality1. Forces Involved in Protein Stability In the cell, linear polypeptides are synthesized from a sequence of mRNA, through a process known as translation. As the polypeptide is synthesized, it begins to fold into its three-dimensional structure in a process known as protein folding. The secondary structure, which includes the alpha helices and beta sheets, is stabilized by intramolecular hydrogen bonds between the amide hydrogen and carbonyl oxygen of the peptide bond that links the amino acids of the primary structure. Interactions between side chains of amino acids that comprise the protein determine the tertiary structure. The structure is firmly maintained due to the strength of hydrophobic interactions and the disulfide that bridges between the cysteine residues of the amino acids.