Explaining that baleen is composed of keratin#the same protein that makes hair and fingernails#Werth also describes how the protein forms large continually growing plates each with an internal fibrous core sandwiched between smooth outer plates.
Whales usually carry 300 of these structures on each side of their mouths#arranged perpendicular to the direction of water flowing into the mouth
#Untangling lifes originsresearchers in the Evolutionary Bioinformatics Laboratory at the University of Illinois in collaboration with German scientists have been using bioinformatics techniques to probe the world of proteins for answers to questions about the origins of life.
Proteins are formed from chains of amino acids and fold into three-dimensional structures that determine their function.
and molecular dynamics looking back to when proteins first appeared approximately 3. 8 billion years ago to determine changes in folding speed over time.
To do this they looked at all known protein structures as defined in the Structural Classification of Proteins (SCOP) database
In a previous study researchers in Caetano-Anoll s's group used SCOP and genomic information to reconstruct phylogenomic trees that describe the history of the protein world.
In contrast the leaves of these new trees are protein domains which are compact evolutionary units of structure and function.
Proteins are usually complex combinations of several domains. We have a world of about 90000 of these structures
or folds because they are determined by the way the protein chains fold on themselves. To date approximately 1300 folds have been characterized.
For the current study the researchers identified protein sequences in the genomes that had the same folding structure as known proteins.
when proteins became part of a particular organism. This allowed them to map protein structures and organisms onto a timeline.
Directly calculating the folding speed for all of these proteins would be impossible with today's technology so the researchers took advantage of the fact that a protein always folds at the same points
and used a measure called Size Modified Contact Order (SMCO). Contact order is the ability of a protein to establish links between segments of the polypeptide chain.
When points that are close together on the chain come together they generally form helical structures; when distant points come together they form beta strands that interact with each other
The measure is normalized (size modified) to take protein length which affects folding speed into account.
What we see is said an hourglass Caetano-Anoll s. At the beginning proteins seem not to be folding so fast.
what he calls the Big bang in protein evolution. Approximately 1. 5 billion years ago more complex domain structures and multi-domain proteins emerged with the appearance of multicellular organisms.
Amino acid chains which make up proteins also became shorter at this point in time. Why does speed folding matter?
If the protein does not fold in the vast majority of cases it will not have a function.
So folding implies functionality. And speed of folding implies speed of achieving that functionality he explained.
For a cell that's very important because if proteins are very slow folders there is a time lag to
Moreover proteins that fold rapidly are more likely to fold correctly. Protein misfolding has been linked with diseases such as Alzheimer's.
Caetano-Anoll s said however that this research makes an important contribution to understanding how molecules work.
when you look at the level of cells proteins and genes human and bee brains function very similarly.
Transcripts are often like a recipe for making proteins and a collection of all the transcripts in a cell is called a transcriptome.
#Stressed proteins can cause blood clots for hoursnew research from Rice university Baylor College of Medicine (BCM)
and brain could cause a common protein to change shape and form dangerous blood clots. The scientists were surprised to find that the proteins could remain in the dangerous clot-initiating shape for up to five hours before returning to their normal healthy shape.
The study--the first of its kind--focused on a protein called von Willebrand factor or VWF a key player in clot formation.
A team led by Rice physicist Ching-Hwa Kiang found that shear forces like those found in small arteries of patients with atherosclerosis cause snippets of nonclotting VWF to change into a clot-forming shape for hours at a time.
Kiang associate professor of physics and astronomy and of bioengineering studies the forces involved in protein folding.
Proteins are the workhorses of biology. Tens of thousands are produced each second in every living cell and each of these folds into a characteristic shape within moments of its creation.
Despite its ubiquity protein folding is an immensely complex process that is shrouded in mystery. Kiang is a pioneer in the use of atomic force microscopes (AFM) to shed light on the fundamental physical processes involved in protein folding.
The AFM has a tiny needle with a tip measuring just a few atoms across. The needle is suspended from a tiny arm that bobs up and down over a surface.
and pull apart individual protein molecules. By stretching these like rubber bands her team has shown it can measure the precise physical forces that hold them in their folded shape.
It's a long protein and one end remains anchored to the cell while the rest unfurls from the wall like a streamer.
We didn't know how the conformation of the PVWF protein changed. That is why Dr. Kiang's research is so important
They also determined how long the protein remained partially unfurled before relaxing into its natural shape. The next step will be to design new experiments that allow us to monitor the proteins as they bind to platelets
and initiate clot formation Kiang said. That will tell us even more about the physical properties of the proteins
and provide more clues about potential therapies. The research was supported by the National institutes of health the National Science Foundation the Alliance for Nanohealth the Welch Foundation the Mary R. Gibson Foundation and the Everett Hinkson Fund.
and dispatching proteins into the nucleus and the cytoplasm. These police proteins are armed with police sketches of the parasites in the form of small RNA transcripts.
The new plot twistit struck Reenan and lead author Selena Gell that this policing system
This was characterized by elevations in plasma urea and protein in the urine. The researchers found increased deposits of triglycerides (TG)( especially saturated fatty acids) increased signs of oxidative stress and depleted copper levels in the kidneys.
Coprolites also showed that fish mostly anchovies did provide the primary protein in the diet but not the calories.
and sizes of lesions due to colorectal cancer and an increased number of cells that express the protein IL-10 which acts to regulate the body's inflammatory response Resistant starch may also have implications for the prevention
Advantages of using plants to produce therapeutic proteins include the ability to produce large quantities quickly and cheaply the absence of human pathogens the stability of the proteins and the ease with
Another was establishing good manufacturing practices for biologically active proteins expressed in transgenic plants. Story Source:
According to the researchers STAT3 is activated frequently in various types of human cancers and when activated STAT3 increases IKBKE overexpression and protein levels.
and animal studies that a protein lures zinc into key cells that are first-responders against infection.
because it stops the action of a protein ultimately preventing excess inflammation. While this study and previous work linking zinc deficiency to inflammation might suggest that supplementation could help very sick ICU patients it's still too early to make that leap.
and interacts with thousands of proteins to sustain human life. Of all the zinc contained in our bodies only about 10 percent of it is readily accessible to help fight off an infection said Knoell also an investigator in Ohio State's Davis Heart and Lung Research Institute.
A major part of this process involves the NF-Î B pathway named for a highly active protein that is known to play an important role in the immune response to infection.
After cell entry zinc is directed then to and binds to a different protein in the NF-Î B pathway.
In the current study collaborators who specialize in computational modeling of protein interactions helped identify the likely target of zinc once it enters the cell:
specific binding sites on a protein called IKKB. When researchers allowed this protein to function unchecked in mice with zinc deficiency the animals developed excessive inflammation in response to sepsis--confirmation that IKKB was zinc's target to turn off the inflammatory pathway.
There are certainly other zinc targets in the cell but we found evidence that zinc is brought in by ZIP8 to turn the pathway off by interacting with this protein at a specific region Knoell said.
The recommended daily allowance for zinc ranges from 8 to 11 milligrams for most adults.
and microbiology focused their attention on a class of essential virulence proteins produced by a broad range of pathogens including Phytophthora called effectors.
Its effectors are the first example of proteins produced by eukaryotic pathogens--nucleated single -or multicellular organisms--that promote infection by suppressing the host RNA silencing process.
Many RNAS are used to make proteins. However these RNAS can be regulated by small RNA (snippets of RNA) that bind to them.
or signature--a specific protein code--that allows the proteins to be delivered into host cells Ma said.
when gluten a protein in wheat barley and rye damages the lining of the small intestine causing a variety of symptoms.
As a society Americans'consumption of fish especially fish that contributes to these omega-3 fats is quite low compared to other proteins Drouillard said.
whose protein is mutated but still partly functional--it is possible as Jackson postulated to increase meristem size
Choosing low-fat milk or yogurt over cream can increase intake of protein calcium and Vitamin d while limiting intake of saturated fats.
The latest frontier in basic biomedical research is to better understand the molecular machines called proteins and enzymes.
They also imaged tubulin a protein essential for building various structures within cells. In that case they were able to drop the time from nine days to under three and a half hours.
and characterized with regards to its protein and sugar composition. The antibody was shown also to be active in neutralizing a broad panel of rabies viruses
and several of his undergraduate research assistants compared the protein quality of red oak and sugar maple leaves from trees on the Diag.
which states that protein quality in leaves differs significantly from species to species . Instead Barbehenn and his students found that the amino acid composition of the proteins in red oak
and sugar maple leaves is strikingly similar--so similar in fact that they could not be distinguished during the spring
However the researchers found that protein is more abundant in oak leaves than in maple leaves.
Instead of differences in protein quality we showed that maple trees have lower quantities of protein than oak partly explaining why they are less nutritious than oak leaves said Barbehenn an associate research scientist in the Department of Molecular Cellular and Developmental
She said her work studying protein metabolism in gypsy moth caterpillars shaped her decision to pursue a doctorate in nutrition.
and quantify the amino acids that make up proteins. The whole-body essential amino acid composition of gypsy moth caterpillars was measured to estimate their optimum dietary protein composition which was compared with the EAA compositions of oak and maple leaves.
The protein study showed that gypsy moths would have to devour more maple leaves than oak leaves to achieve the same amount of nourishment.
##Zoomable map of poplar proteins offers new view of bioenergy cropresearchers seeking to improve production of ethanol from woody crops have a new resource in the form of an extensive molecular map
of poplar tree proteins published by a team from the Department of energy's Oak ridge National Laboratory. Populus a fast-growing perennial tree holds potential as a bioenergy crop due to its ability to produce large amounts of biomass on nonagricultural land.
Now a study by ORNL scientists with the Department of energy's Bioenergy Science Center has provided the most comprehensive look to date at poplar's proteome the suite of proteins produced by a plant's cells.
The ability to comprehensively measure genes and proteins helps us understand the range of molecular machinery that a plant uses to do its life functions said ORNL's Robert Hettich.
The ORNL research team measured more than 11000 proteins in different parts of poplar including mature leaves young leaves roots and stems.
which maps out the proteins present in the various tissue types at a given point in time.
and also the ability to zoom in on specific biological features such as pathways and individual proteins.
considering a plant such as poplar can potentially manufacture more than 40000 different proteins. Unlike an organism's genome which is the same for every cell
The analytical techniques we've demonstrated allow us to measure the range of proteins very deeply
and specifically so we can start to figure out for instance how the protein machinery in a leaf differs from the ones in the trunk Hettich said.
versus one that's very old thus enabling us to understand how all these proteins are changing as a function of the tree growing older.
and adapt to environmental surroundings by altering their proteins could help bioenergy researchers develop poplar trees better suited to biofuel production.
It's the proteins that directly alter the morphology anatomy and function of a plant cell Abraham said.
If we can identify the proteins that create a favorable trait such as fast growth then we can incorporate that protein
and often the goat is the only source of animal protein in their diet explains Rosa Garcã a. The team led by Koldo Osoro Otaduy manager of the Animal Production Systems Area at SERIDA
albeit in opposite directions suggests that the protein the gene called SLC30A4 codes for may play a crucial role in the disease.
Indeed that protein is relatively abundant in insulin-producing islet cells of the pancreas where it aids the transport of zinc into those cells.
It also may throw light on precisely how these substances affect the production or performance of the protein for which the implicated gene codes.
The study reveals that voles liked these larvae (rich in proteins) and feed on them decreasing the harm produced by these worms over the acorns.
#Using lysine estimates to detect heat damage in distillers dried grains with solublesdistillers dried grains with solubles (DDGS) are a good source of energy and protein in swine diets.
pigs can use it for protein synthesis. Some sources of DDGS are heat damaged. And therefore the digestibility of the lysine in particular is said poor animal sciences professor Hans Stein.
total crude protein concentration total analyzed lysine concentration reactive lysine concentration as determined using the furosine procedure and lysine to crude protein ratio.
Using the lysine to crude protein ratio as a second independent variable in the regression equation improved the predictions.
Researchers could not accurately predict lysine digestibility using the concentration of crude protein alone. The practical outcome of this is that you can't analyze only for crude protein.
You will need to have some kind of an estimate of lysine or furosine to know if your source of DDGS is heat damaged Stein said.
and fosmid clones technologies yielding 343 Mb draft genome with 18071 predicted protein-coding genes.
Abnormal proteins from buttock fat linked to metabolic syndromepeople who are shaped apple--with fat more concentrated around the abdomen--have long been considered more at risk for conditions such as heart disease
and omentin-1 proteins that can lead to inflammation and a prediabetic condition know as insulin resistance in individuals with early metabolic syndrome.
'It also suggests that abnormal protein levels may be an early indicator to identify those at risk for developing metabolic syndrome.
and low levels of omentin-1--proteins that correlate with other factors known to increase the risk for heart disease and diabetes.
High chemerin levels for example correlated with high blood pressure elevated levels of C reactive-protein protein (a sign of inflammation) and triglycerides insulin resistance and low levels of HDL cholesterol.
Complete blood counts lipid profiles and blood glucose blood pressure and C reactive-protein protein levels were measured in all participants. Levels of four proteins secreted by adipose tissue--chemerin resistin visfatin
and omentin-1--were measured also in plasma and in subcutaneous fat samples from gluteal tissue.
The abnormal levels of these two proteins were also independent of age body mass index and waist circumference.
Unlike peas beans are attacked not by pea weevils as they contain a protein called Î-amylase inhibitor (Î AI) that causes the weevils feeding on beans to starve before they cause any damage.
Coronaviruses have a spike protein that is activated by a protease and mediates membrane fusion and entry into a host cell.
The location on the spike protein where a protease activates this process is called a cleavage site.
This is the first characterization of a natural coronavirus with a spike protein containing two furin cleavage sites said Millet the paper's first author.
Fungi get around this plant immunity by injecting proteins into the host plant cells. These'effector proteins'enable the fungi to escape the plant's immune system
and allow the fungal cells to enter the plant unrecognised. Exeter scientists have shown now that signalling organelles known as'early endosomes'act as long distance messengers in the fungi.
This rapid communication between the point of invasion and the fungal cell nucleus enables the fungus to produce the effector proteins that help evade the plant's immune response from the moment the fungus enters the host tissue.
Quality is measured by the concentration of proteins in the plants. Bradford says the experiment differed from earlier research in two important ways:
many single polypeptide (protein) chains actually contained two enzymes one of which was embedded in the other.
Further analysis of the most important protein revealed that the embedded component was a carbohydrate-binding module (CBM)
This bending action may bring the fiber close to the other enzyme in the protein so it can get to work breaking the bonds between the sugars.
The groups had comparable scores on intakes of whole grains refined grain total dairy total protein fatty acid and sodium.
The external organ support system is designed to perform critical functions of a normal liver including protein synthesis and the processing and cleaning of a patient's blood.
The 3-pound organ that sits to the right of the stomach performs many functions including detoxification regulation of glucose levels and the making of vital proteins.
#whether by blade of a mower or jaws of a predatory insect â#by producing defensive proteins
and proteins account for tolerance. When Kim returned in July for his second three-month stay he brought seeds from two Korean lines--Sukang
Looking at both lines he identified 33 proteins that are expressed differentially in the tolerant cultivar.
and compare those results with the list of differentially expressed proteins from the Korean cultivars.
If the same proteins are expressed differentially in Glover's varieties Kim will validate the genes he identified as important to tolerance in his Korean varieties.
and recommended for a healthy diet are those that have a high amount of nutrients per serving including fruits and vegetables nonfat milk whole grains and fish and other lean proteins.
One serving is the equivalent to eight grams of protein: a cup of milk or 45 grams of cheese.
Like a watchful sentry JA takes action at the first sign of plant distress producing proteins that prepare the plant to combat excess heat lack of water or attack by disease organisms.
#New superfoods could help key protein keep bodies healthya new generation of new superfoods that tackle heart disease
and diabetes could be developed following research into a protein that helps keep cells in our bodies healthy.
Researchers at the University of Warwick found that the protein called Nrf2 continually moves in
The research team are the first to record the continual movement cycle of Nrf2 which sees the protein oscillate in and out of the cell nucleus once every 129 minutes.
In an attempt to target healing stem cells to the site of the injury researchers coated iron nanoparticles with two kinds of antibodies proteins that recognize
At this cleavage site the protein segment covering part of the enzyme active site is removed and the substrates (tyrosine and other monophenols) can be accessed
which produced well formed protein crystals. This was only possible with the use of a relatively unusual co-crystallization reagent a polyoxometalate of the Anderson type.
and was a key proponent of its usage as an additive for protein crystallization. The research project was continued then as FWF Initiative.
Glycine soja used to improve protein content in soybean; and Vitis amurensis a wild relative of grape which has been used to improve cold tolerance.
Fats and proteins tend to increase with the economic development of emerging countries he said.
and found that the contents of protein fat vitamins and minerals are the same as that of commercial yeast.
and there were many more changes in the non-coding part of the genome than in the parts of the genome that codes for protein.
The Joslin nutritional guidelines for diabetes recommend a diet with relatively high amounts of healthy fats and protein but moderately low amounts of carbohydrates.
The gene called OSCA1 encodes a protein in the cell membrane of plants that senses changes in water availability
Pei and Duke colleagues Fang Yuan James Siedow and others identified a gene that encodes a protein in the cell membranes of plant leaves
and may not realize that lupin has the same protein that causes allergic reactions to peanuts and soybeans.
It is high in protein and in dietary fiber --which helps lower cholesterol --and is low in fat.
A specific protein in milk known as beta-lactoglobulin is able to initiate an allergy only when being devoid of iron.
Loaded with iron the protein is harmless. The scientists discovered the same mechanism recently with regard to birch pollen allergy.
Lack of iron load transforms milk protein into allergenone of the most important milk allergens the so-called beta-lactoglobulin belongs to the protein family of lipocalins.
Iron is bound to the protein by so-called siderophores. The first author Franziska Roth-Walter and her colleagues now show that an empty milk protein one without iron
and hummingbirds--a three-year process--Baldwin needed to test what the proteins expressed by these genes were responding to.
and are capable of activating genes that change the protein composition in the cell. A team of scientists--headed by Prof.
Brigitte Poppenberger at TUM's Institute of Biotechnology of Horticultural Crops--has been able to show for the first time that the concentration of CES protein increases in certain nuclear regions following brassinosteroid activation.
The cell seems to bundle key resources to rapidly trigger the production of certain proteins.
The molecules have a binding site for SUMO protein. As soon as this attaches CES moves to nuclear bodies.
what happens in the animal world where the SUMO protein is known to repress effects conferred by transcription factors.
or donor human milk as well as a fortifier consisting of protein and minerals made from the donor milk.
Because infants are already receiving enough protein from the fortifier another way to help them grow is by giving them fat.
which actions to take such as which proteins to code. It was thought that mrna was very fragile and short-lived so transferring it between species was unimaginable.
or better able to assimilate protein and other useful nutrients from the limited forage. Tolerant animals might invest energy in gut repair
and breastfeeding--Implementing a breastfeeding peer support group in a children's hospital--Considerations in meeting protein needs of the human milk-fed preterm infant--Environmental factors affecting breastfeeding duration within a NICUSUPPORTING the use of human milk is one
or displace animal protein as well as bad fats such as trans fat in a dish or meal.
and refined grains and alcohol and increase consumption of fruits vegetables whole grains low fat unsweetened dairy products and low cholesterol protein.
Three decades ago while a postdoctoral researcher at UW-Madison Vierstra was the first to purify the phytochrome protein.
Scientists analyze how influenza-related proteins help infect cellsa flu virus acts like a Trojan horse as it attacks
The Rice-Baylor team applied protein-folding algorithms developed by Onuchic and his colleagues to analyze how hemagglutinin reconfigures itself as it infects a cell.
It may be the only case known to human beings where a protein starts at a fixed point
Proteins are the molecular motors that spring from DNA and perform tasks essential to life and they are the prime focus of study for Onuchic and his colleagues at Rice's Center for Theoretical Biological Physics (CTBP).
The researchers use their energy landscape theory to determine the path an unfolded strand of amino acids takes as it collapses into a final functional protein.
Energy landscape theory predicts how a protein will fold no matter how fast it happens. In the case of hemagglutinin the unfolding and refolding happens in seconds.
During the process part of the protein cracks and releases fusion peptides. The fusion peptides are the most important part of the molecule said Rice postdoctoral researcher
Initially part of the protein forms a cap that protects the segments inside. Acidic conditions cause the cap to fall off
and the protein begins to reconfigure itself. The release of the fusion peptide which is hidden initially inside hemagglutinin is triggered by that giant conformational change Ma said.
When the cap is on the whole protein is said stable Noel. What we see in the simulation is that the hydrophobic pocket where the fusion peptides are buried is very unstable
But he suspects the inner part of the protein is conserved more highly. We're targeting the part that the virus cannot afford to change.
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