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Simple Overview of Proteins

Posted on April 20, 2021  Comments (0)

This webcasts provides a good, very simple, overview of proteins.

Learn more about proteins: How Lysozyme Protein in Our Tear-Drops Kill Bacteria – Molecular Motor Proteins – Fold.it, the Protein Folding Game

Molecular Motor Proteins

Posted on January 27, 2020  Comments (1)

Webcast on amazing processes inside cells by Ron Vale.

Molecular motor proteins are fascinating enzymes that power much of the movement performed by living organisms. The webcast provides an overview of the motors that move along cytoskeletal tracks (kinesin and dynein which move along microtubules and myosin which moves along actin). The talk first describes the broad spectrum of biological roles that kinesin, dynein and myosin play in cells. The talk then discusses how these nanoscale proteins convert energy from ATP hydrolysis into unidirectional motion and force production, and compares common principles of kinesin and myosin. The talk concludes by discussing the role of motor proteins in disease and how drugs that modulate motor protein activity can treat human disease.

Ron Vale is a Professor of Cellular and Molecular Pharmacology at the University of California, San Francisco and an Investigator of the Howard Hughes Medical Institute. He is also the founder of the iBiology project.

Related: Animations of Motor Proteins Moving Material Inside Cells – Science Explained: How Cells React to Invading Viruses – Looking Inside Living Cells

Animations of Motor Proteins Moving Material Inside Cells

Posted on December 23, 2017  Comments (1)

Very cool. This next video gives a bit more information on how these amazing parts of our cells move material around inside or cells.

This stuff is so interesting. I wish this type of interesting material and informative animations was what my biology education was like in k-12 instead of the boring stuff my classes were instead. I hope students today have better science classes than I did.

It is amazing how such mechanisms evolved to “walk” along transportation microtubules inside our cells.

Related: Molecular Motor Proteins webcast by Ron Vale, Professor of Cellular and Molecular Pharmacology at the University of California, San Francisco (35 minutes) – Looking Inside Living Cells – Science Explained: Cool Video of ATP Synthase, Which Provides Usable Energy to Us – Exploring Eukaryotic Cells

The Amazing Reality of Genes and The History of Scientific Inquiry

Posted on March 4, 2017  Comments (4)

cover of The Gene

The Gene by Siddhartha Mukherjee is a wonderful book. He does a great job of explaining the history of scientists learning about genes as well as providing understandable explanations for the current scientific understanding of genes and how they impact our lives.

As I have mentioned before, I find biology fascinating even though I found biology classes utterly boring and painful. I wish everyone could learn about biology with the insight people like Siddhartha Mukherjee provide. I realize not everyone is going to find the history and understanding of genes to be fascinating but for those who might this book is a great read. And don’t rule the idea out just because you found biology classes painful.

Life may be chemistry, but it’s a special circumstance of chemistry. Organisms exist not because of reactions that are possible, but because of reactions that are barely possible. Too much reactivity and we would spontaneously combust. Too little, and we would turn cold and die. Proteins enable these barely possible reactions, allowing us to live on the edges of chemical entropy – skating perilously, but never falling in.
– page 134

Whether it is the physics of our solar system or our biology there is a precarious band that allowed beings such as ourselves to evolve.

most genes, as Richard Dawkins describes them, are not “blueprints” but “recipes.” They do not specify parts, but processes; they are formulas, not forms. If you change a blueprint, the final product is change in a perfectly predictable manner: eliminate a widget specified in the plan, and you get a machine with a missing widget. But alteration of a recipe or formula doesn’t not change the product in a predictable manner: if you quadruple the amount of butter in a cake, the eventual effect is more complicated than just a quadruply buttered cake (try it; the whole thing collapses in an oily mess).
– page 454

The is a powerful idea. And when combined with turning genes on and off it is understandable how complex determining genetic impacts on biology and disease are. A few diseases or results (e.g. blue eyes) are nearly as simple as 1 or a few genes being altered in a specific way but most are not nearly so easy. And it isn’t like even that is so easy but with the amazing efforts scientists have made and the advanced tools those scientists created it can now seem simple to identify some such diseases.

The genetic code is universal. A gene from a blue whale can be inserted into a microscopic bacterium and it will be deciphered accurately and with near perfect fidelity. A corollary: there is nothing particularly special about human genes.
– page 480

This is something I have known and understood but it is still amazing. Genes and proteins and how they act to create the incredible diversity of life is something that is awe inspiring.

This book is a wonderful adventure for those interested in life and scientific inquiry.

Related: Epigenetics, Scientific Inquiry and Uncertainty – Human Gene Origins: 37% Bacterial, 35% Animal, 28% Eukaryotic – Unexpected Risks Found In Editing Genes To Prevent Inherited Disorders – Epigenetic Effects on DNA from Living Conditions in Childhood Persist Well Into Middle Age – Why Don’t All Ant Species Replace Queens in the Colony, Since Some Do

Defying Textbook Science, Study Finds Proteins Built Without DNA Instructions

Posted on January 3, 2015  Comments (2)

Open any introductory biology textbook and one of the first things you’ll learn is that our DNA spells out the instructions for making proteins, tiny machines that do much of the work in our body’s cells. Results from a recent study show for the first time that the building blocks of a protein, called amino acids, can be assembled without blueprints – DNA and an intermediate template called messenger RNA (mRNA). A team of researchers has observed a case in which another protein specifies which amino acids are added.

“This surprising discovery reflects how incomplete our understanding of biology is,” says first author Peter Shen, Ph.D., a postdoctoral fellow in biochemistry at the University of Utah. “Nature is capable of more than we realize.”

To put the new finding into perspective, it might help to think of the cell as a well-run factory. Ribosomes are machines on a protein assembly line, linking together amino acids in an order specified by the genetic code. When something goes wrong, the ribosome can stall, and a quality control crew is summoned to the site. To clean up the mess, the ribosome is disassembled, the blueprint is discarded, and the partly made protein is recycled.

Yet this study reveals a surprising role for one member of the quality control team, a protein conserved from yeast to man named Rqc2. Before the incomplete protein is recycled, Rqc2 prompts the ribosomes to add just two amino acids (of a total of 20) – alanine and threonine – over and over, and in any order. Think of an auto assembly line that keeps going despite having lost its instructions. It picks up what it can and slaps it on.

“In this case, we have a protein playing a role similar to that filled by mRNA,” says Adam Frost, M.D., Ph.D., assistant professor at University of California, San Francisco (UCSF) and adjunct professor of biochemistry at the University of Utah. He shares senior authorship with Jonathan Weissman, Ph.D., a Howard Hughes Medical Institute investigator at UCSF, and Onn Brandman, Ph.D., at Stanford University. “I love this story because it blurs the lines of what we thought proteins could do.”

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Cancer Cells in Blind Mole Rats ‘commit suicide’

Posted on November 6, 2012  Comments (3)

Cancer cells in blind mole rats ‘commit suicide’

Blind mole rats don’t get cancer, and geneticists have worked out why — their cells kill themselves with a poisonous protein when they multiply too much.

Blind mole rats, which live in underground burrows throughout Southern and Eastern Africa, and the Middle East, are fascinating creatures. The naked mole rat, in particular, is the only cold-blooded mammal known to man, doesn’t experience pain, and is also arguably the only mammal (along with the Damaraland mole rat) to demonstrate eusociality — that is, they live in large hierarchical communities with a queen and workers, like ants or bees.

They’re also cancer-proof, which was found in 2011 to be down to a gene that stops cancerous cells from forming. The same team thought that two other cancer-proof mole rat species might have similar genes, but instead it turns out that they do develop cancerous cells — it’s just that those cells are programmed to destroy themselves if they become dangerous.

Very interesting research. The results of evolution are amazing. And while turning the medical research discoveries into workable treatments for people is very difficult the continued increase in our knowledge helps us find treatments that work.

Related: Webcast of a T-cell Killing a Cancerous Cell – Synthetic Biologists Design a Gene that Forces Cancer Cells to Commit Suicide

Evolution Follows a Predictable Genetic Pattern

Posted on November 1, 2012  Comments (0)

Far from random, evolution follows a predictable genetic pattern

The researchers carried out a survey of DNA sequences from 29 distantly related insect species, the largest sample of organisms yet examined for a single evolutionary trait. Fourteen of these species have evolved a nearly identical characteristic due to one external influence — they feed on plants that produce cardenolides, a class of steroid-like cardiotoxins that are a natural defense for plants such as milkweed and dogbane.

Though separated by 300 million years of evolution, these diverse insects — which include beetles, butterflies and aphids — experienced changes to a key protein called sodium-potassium adenosine triphosphatase, or the sodium-potassium pump, which regulates a cell’s crucial sodium-to-potassium ratio. The protein in these insects eventually evolved a resistance to cardenolides, which usually cripple the protein’s ability to “pump” potassium into cells and excess sodium out.
…
Andolfatto and his co-authors examined the sodium-potassium pump protein because of its well-known sensitivity to cardenolides. In order to function properly in a wide variety of physiological contexts, cells must be able to control levels of potassium and sodium. Situated on the cell membrane, the protein generates a desired potassium to sodium ratio by “pumping” three sodium atoms out of the cell for every two potassium atoms it brings in.

Cardenolides disrupt the exchange of potassium and sodium, essentially shutting down the protein, Andolfatto said. The human genome contains four copies of the pump protein, and it is a candidate gene for a number of human genetic disorders, including salt-sensitive hypertension and migraines. In addition, humans have long used low doses of cardenolides medicinally for purposes such as controlling heart arrhythmia and congestive heart failure.

Cool stuff. It makes sense to me which is nice (it is nice to get confirmation that I find what actually exists is sensible). When things that are true just seem crazy it is a bit disconcerting – like quantum mechanics. It is fun to read stuff that totally shakes up preconceived notions, but even then it is nice once I think understand it to find it sensible.

Related: All present-day Life on Earth Has A Single Ancestor – Cambrian Explosion Song – Bacteriophages: The Most Common Life-Like Form on Earth – Microcosm by Carl Zimmer

2012 Nobel Prize in Chemistry to Robert Lefkowitz and Brian Kobilka

Posted on October 10, 2012  Comments (0)

The Royal Swedish Academy of Sciences has decided to award the Nobel Prize in Chemistry for 2012 to

  • Robert J. Lefkowitz, Howard Hughes Medical Institute and Duke University Medical Center, Durham, NC, USA
  • and Brian K. Kobilka, Stanford University School of Medicine, Stanford, CA, USA

for studies of G-protein–coupled receptors.

Your body is a fine-tuned system of interactions between billions of cells. Each cell has tiny receptors that enable it to sense its environment, so it can adapt to new situtations. Robert Lefkowitz and Brian Kobilka are awarded the 2012 Nobel Prize in Chemistry for groundbreaking discoveries that reveal the inner workings of an important family of such receptors: G-protein–coupled receptors.

For a long time, it remained a mystery how cells could sense their environment. Scientists knew that hormones such as adrenalin had powerful effects: increasing blood pressure and making the heart beat faster. They suspected that cell surfaces contained some kind of recipient for hormones. But what these receptors actually consisted of and how they worked remained obscured for most of the 20th Century.

Lefkowitz started to use radioactivity in 1968 in order to trace cells’ receptors. He attached an iodine isotope to various hormones, and thanks to the radiation, he managed to unveil several receptors, among those a receptor for adrenalin: β-adrenergic receptor. His team of researchers extracted the receptor from its hiding place in the cell wall and gained an initial understanding of how it works.

The team achieved its next big step during the 1980s. The newly recruited Kobilka accepted the challenge to isolate the gene that codes for the β-adrenergic receptor from the gigantic human genome. His creative approach allowed him to attain his goal. When the researchers analyzed the gene, they discovered that the receptor was similar to one in the eye that captures light. They realized that there is a whole family of receptors that look alike and function in the same manner.

Today this family is referred to as G-protein–coupled receptors. About a thousand genes code for such receptors, for example, for light, flavour, odour, adrenalin, histamine, dopamine and serotonin. About half of all medications achieve their effect through G-protein–coupled receptors.

The studies by Lefkowitz and Kobilka are crucial for understanding how G-protein–coupled receptors function. Furthermore, in 2011, Kobilka achieved another break-through; he and his research team captured an image of the β-adrenergic receptor at the exact moment that it is activated by a hormone and sends a signal into the cell. This image is a molecular masterpiece – the result of decades of research.

Related: More details on the research – 2011 Nobel Prize in Chemistry – 2009 Nobel Prize in Chemistry: the Structure and Function of the Ribosome – The Nobel Prize in Chemistry 2008

Should Giant Viruses Be Included on the Tree of Life?

Posted on September 14, 2012  Comments (1)

A new study of giant viruses supports the idea that viruses are ancient living organisms and not inanimate molecular remnants. The study may reshape the universal family tree, adding a fourth major branch to the three that most scientists agree represent the fundamental domains of life. But I am not sure that makes sense. The reason given for viruses not being “life” is that they cannot reproduce themselves – they hijack living cells to reproduce. The research in the past history of viruses as they evolved into current viruses is interesting but I don’t see the reason to classify current viruses as life.

The researchers used a relatively new method to peer into the distant past. Rather than comparing genetic sequences, which are unstable and change rapidly over time, they looked for evidence of past events in the three-dimensional, structural domains of proteins. These structural motifs, called folds, are relatively stable molecular fossils that Рlike the fossils of human or animal bones Рoffer clues to ancient evolutionary events, said University of Illinois crop sciences and Institute for Genomic Biology professor Gustavo Caetano-Anoll̩s, who led the analysis.

“Just like paleontologists, we look at the parts of the system and how they change over time,” Caetano-Anollés said. Some protein folds appear only in one group or in a subset of organisms, he said, while others are common to all organisms studied so far.

“We make a very basic assumption that structures that appear more often and in more groups are the most ancient structures,” he said.

Most efforts to document the relatedness of all living things have left viruses out of the equation, Caetano-Anollés said.

“We’ve always been looking at the Last Universal Common Ancestor by comparing cells,” he said. “We never added viruses. So we put viruses in the mix to see where these viruses came from.”

The researchers conducted a census of all the protein folds occurring in more than 1,000 organisms representing bacteria, viruses, the microbes known as archaea, and all other living things. The researchers included giant viruses because these viruses are large and complex, with genomes that rival Рand in some cases exceed Рthe genetic endowments of the simplest bacteria, Caetano-Anoll̩s said.

Related: Plants, Unikonts, Excavates and SARs – Bacteriophages: The Most Common Life-Like Form on Earth – 8 Percent of the Human Genome is Old Virus Genes – Microbes Retroviruses

Open access paper: Giant Viruses Coexisted With the Cellular Ancestors and Represent a Distinct Supergroup Along With Superkingdoms Archaea, Bacteria and Eukarya

The discovery of giant viruses with genome and physical size comparable to cellular organisms, remnants of protein translation machinery and virus-specific parasites (virophages) have raised intriguing questions about their origin. Evidence advocates for their inclusion into global phylogenomic studies and their consideration as a distinct and ancient form of life.
…
Results call for a change in the way viruses are perceived. They likely represent a distinct form of life that either predated or coexisted with the last universal common ancestor (LUCA) and constitute a very crucial part of our planet’s biosphere.

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How do Plants Grow Into the Sunlight?

Posted on April 18, 2012  Comments (3)

Plants are extremely competitive in gaining access to sunlight. A plant’s primary weapon in this fight is the ability to grow towards the light, getting just the amount it needs and shadowing its competition. Now, scientists have determined precisely how leaves tell stems to grow when a plant is caught in a shady place.

photo of a forest

Hole in the Wall trail, Olympic National Park, Washington, USA by John Hunter

The researchers discovered that a protein known as phytochrome interacting factor 7 (PIF7) serves as the key messenger between a plant’s cellular light sensors and the production of auxins, hormones that stimulate stem growth.

“We knew how leaves sensed light and that auxins drove growth, but we didn’t understand the pathway that connected these two fundamental systems,” says Joanne Chory, professor and director of the Salk’s Plant Biology Laboratory and a Howard Hughes Medical Institute investigator (HHMI provides huge amounts of funding for scientific research). “Now that we know PIF7 is the relay, we have a new tool to develop crops that optimize field space and thus produce more food or feedstock for biofuels and biorenewable chemicals.”

Plants gather intelligence about their light situation—including whether they are surrounded by other light-thieving plants—through photosensitive molecules in their leaves. These sensors determine whether a plant is in full sunlight or in the shade of other plants, based on the wavelength of red light striking the leaves. This is pretty cool; I love to learn about the brilliant strategies that have evolved.

If a sun-loving plant, such as thale cress (Arabidopsis thaliana), the species Chory studies, finds itself in a shady place, the sensors will tell cells in the stem to elongate, causing the plant to grow upwards towards sunlight.

When a plant remains in the shade for a prolonged period, however, it may flower early and produce fewer seeds in a last ditch effort to help its offspring spread to sunnier real estate. In agriculture, this response, known as shade avoidance syndrome, results in loss of crop yield due to closely planted rows of plants that block each other’s light.

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Exploring Eukaryotic Cells

Posted on March 4, 2012  Comments (3)

This webcast is packed with information on the makeup and function of eukaryotic cells, which are the type of cells found in animals. It is part of a interesting series of science webcasts by Crash Course. The webcast style might be a bit too hyperactive and flippant for some but the content is quite interesting and the videos they are are of similar style and quality so if you like this one you can subscribe to their channel. They offer quite a few webcasts on science but they also offer webcasts on history.

Related: Plants, Unikonts, Excavates and SARs – How Cells Age – Midichloria mitochondrii