Tuesday 26th of September 2023

life force: ATP....

of protein

Fighting obesity may be as easy as ATP, says UH researcher

NIH, NSF funds biosensors that would track metabolic activity, diagnose unhealthy conditions

HOUSTON, Oct. 22, 2007 – Wearing a portable instrument to monitor metabolism in the fight against obesity and its related health consequences may be on the horizon thanks to collaborative research being performed at the University of Houston and The Methodist Hospital.

Physics Professor John Miller, director of the High-Temperature Superconducting Device Applications and Nano-Biophysics Laboratory in the Texas Center for Superconductivity at the University of Houston (TcSUH), recently received a three-year, $623,425 exploratory research grant from the National Institutes of Health (NIH) in a joint program with the National Science Foundation (NSF) on biosensors for energy balance and obesity.

In particular, Miller is targeting metabolic syndrome, a pernicious complication of obesity that affects about 20 percent of obese individuals and greatly increases the likelihood of diabetes, heart disease and cancer. His long-term goal is to develop innovative technologies that detect metabolic activity for research and clinical applications.

“Although drug treatments for metabolic syndrome exist, the cost of drugs to treat all obese individuals is prohibitive,” Miller said. “Therefore, there is a critical public health need to develop technologies that can provide early diagnosis of metabolic syndrome and enable cost-effective treatment, as well as to measure metabolic activity and other components of energy balance in obese patients.”

The chemical currency of energy and metabolism that is used by the cellular machinery of all living organisms is adenosine triphosphate (ATP) – a molecule involved in more chemical reactions than any other on Earth except water. In animals, plants and fungi, ATP is produced by enzyme complexes in mitochondria that live and reproduce inside the cell. ATP molecules can be thought of as packets of “fuel” that power biological molecular motors. If one were to suddenly run out of ATP, death would be instantaneous. However, ATP that goes unused eventually gets converted into fat – hence the growing obesity epidemic at a time when high-calorie food is plentiful.



Adenosine-5'-triphosphate (ATP) is a multifunctional nucleotide used in cells as a coenzyme. It is often called the "molecular unit of currency" of intracellular energy transfer.[1] ATP transports chemical energy within cells for metabolism. It is produced by photophosphorylation and cellular respiration and used by enzymes and structural proteins in many cellular processes, including biosynthetic reactions, motility, and cell division.[2] One molecule of ATP contains three phosphate groups, and it is produced by ATP synthase from inorganic phosphate and adenosine diphosphate (ADP) or adenosine monophosphate (AMP).
Metabolic processes that use ATP as an energy source convert it back into its precursors. ATP is therefore continuously recycled in organisms: the human body, which on average contains only 250 grams (8.8 oz) of ATP,[3] turns over its own body weight in ATP each day.[4]


The ATP concentration inside the cell is typically 1–10 mM.[21] ATP can be produced by redox reactions using simple and complex sugars (carbohydrates) or lipids [fats] as an energy source. For ATP to be synthesized from complex fuels, they first need to be broken down into their basic components. Carbohydrates are hydrolysed into simple sugars, such as glucose and fructose. Fats (triglycerides) are metabolised to give fatty acids and glycerol.
The overall process of oxidizing glucose to carbon dioxide is known as cellular respiration and can produce about 30 molecules of ATP from a single molecule of glucose.[22] ATP can be produced by a number of distinct cellular processes; the three main pathways used to generate energy in eukaryotic organisms are glycolysis and the citric acid cycle/oxidative phosphorylation, both components of cellular respiration; and beta-oxidation. The majority of this ATP production by a non-photosynthetic aerobic eukaryote takes place in the mitochondria, which can make up nearly 25% of the total volume of a typical cell.[23]



There you have it... and as anyone who knows about ppms would tell you, it does not take much to change a system one way or the other... 250 grams of ATP... (3000 ppms approx in an average 75 kgs body). Imagine a dose of headache tablet: 0.5 gram (60 ppm approx, in an average 75 kgs body, of which about 5ppm is used efficiently). A spider bite: ±0.001 part per million (ppm) enough to do some damage including death should the spider venom be highly toxic (necrotic or paralysing).

So "if a tiny gram of ATP is not processed", my guess is this can lead to an increase in fat of 300 grams in an average 75 kgs body per day... I know it's not as clear cut as this, but who knows... The complex relationship of ATP with EXTRA carbon dioxide is not quite clear (carbon dioxide could reduce the amount of ATP being processed since the body already has extra CO2 — blocking the process of energy-producing CO2 since the body would be "saturated" with CO2). Obese people tend to have problem in expelling CO2, leading to sleep apnea and putting on more weight. The extra CO2 could also lead to a tendency towards less activity... Less activity plus food equals more fat.

Which comes first is difficult to know, but my guess is that "fat" people should eat less, abstain from carbonated drinks (with either sugars or sweeteners) should exercise (without consuming more food), shit more and fart more.

Now it's the role of advertisers and product manufacturers to become responsible citizens to make sure their products and promotional push ARE NOT ADDICTIVE. That will be the day.


Some proteins that bind ATP do so in a characteristic protein fold known as the Rossmann fold, which is a general nucleotide-binding structural domain that can also bind the coenzyme NAD.[41] The most common ATP-binding proteins, known as kinases, share a small number of common folds; the protein kinases, the largest kinase superfamily, all share common structural features specialized for ATP binding and phosphate transfer.[42]
ATP in complexes with proteins, in general, requires the presence of a divalent cation, almost always magnesium, which binds to the ATP phosphate groups. The presence of magnesium greatly decreases the dissociation constant of ATP from its protein binding partner without affecting the ability of the enzyme to catalyze its reaction once the ATP has bound.[43] The presence of magnesium ions can serve as a mechanism for kinase regulation.[44]




As an over-simplification — and as I have said many times on this site — let me repeat here that in order to live (acquire ATP and life constructing blocks), we need to "steal" something else's protein...

eat less, shit more...

Dieting is harder than you think. If you cut out a chocolate bar each day you will lose only one-third of the weight that experts had thought. For decades, doctors have based their advice to those who want to lose weight on the assumption that cutting 500 calories a day will see the weight fall off at the rate of 1lb a week.

"This is wrong," Kevin Hill, of the National Institutes of Health in the United States, said. "It does not happen." The error has arisen because the calculation did not take account of changes in metabolism as weight falls. The body adjusts to reductions in energy intake (calories eaten) by slowing its energy output (calories expended). The result is that forgoing that daily chocolate bar containing 250 calories will lead to about 25lb of weight loss if it is sustained for three years, much less than the 78lb predicted by the old dieting assumption....




Gus: the only diet that works is to eat less, eat small portions more often, drink no fizzy"energy drink" while being active and expell more.... In order to reduce "hunger pains" should one need to, the only solution is water, lettuce and "just bear it"... Hunger pains usually only last no more than two hours, even if one skips a meal... Moderation and balance (a bit of everything) is the relative key. See story at top...

fat kids...

SPECIALIST child obesity clinics are so overwhelmed by demand that patients wait up to a year to get into a program.

Doctors report a dramatic increase in the number and severity of childhood obesity cases they are treating but say resources are failing to keep pace with the epidemic.

''From the short period of time we've been doing this, we're seeing more and more severely affected children at a younger age,'' said Shirley Alexander, who has run the weight management program at The Children's Hospital at Westmead since 2008, and whose youngest patient is just 18 months old.

''When we first started, it was unusual to see a nine- or 10-year-old with co-morbidities like diabetes or obstructive sleep apnoea.

''Now they seem to be younger, heavier and having more concerning complications.''

Read more: http://www.smh.com.au/national/health/the-wait-grows-at-child-clinics-20111217-1ozs2.html#ixzz1gqV88chr

more fat pigs...

There is an issue in France about obesity and kids... Suddenly, the culprit has become embroilled in a pot of yogurt... Some brands of the stuff have been adding "probiotic" supplements for many years (20) ... These supplements are designed to help build the "immune system"... But one should know that these supplements are the SAME ones used in "helping" cattle, pigs and chickens grow faster, fatter, bigger... Some studies have found that "obese" kids have far more "probiotic" substances in their intestinal flora than the normal kids. Are we in the same boat here? Are "probiotic" supplements added in food without our knowledge? 

Keep you posted...

the complex machinery of life...

As we fart around about killing each others or not, rob thy neighbour's wife, make a Sunday roast (which is an assemblage of cooking dead proteins) and enjoy a free sample of the daily Telegraph like an enema, life — below the surface — is a marvel of automated complex chemical reactions, the precision of which may let us live or die. For example:



Mitochondrial ribosomes (mitoribosomes) are large ribonucleoprotein complexes that synthesize proteins encoded by the mitochondrial genome. An extensive cellular machinery responsible for ribosome assembly has been described only for eukaryotic cytosolic ribosomes. Here we report that the assembly of the small mitoribosomal subunit in Trypanosoma brucei involves a large number of factors and proceeds through the formation of assembly intermediates, which we analyzed by using cryo–electron microscopy. One of them is a 4-megadalton complex, referred to as the small subunit assemblosome, in which we identified 34 factors that interact with immature ribosomal RNA (rRNA) and recognize its functionally important regions. The assembly proceeds through large-scale conformational changes in rRNA coupled with successive incorporation of mitoribosomal proteins, providing an example for the complexity of the ribosomal assembly process in mitochondria.

Although they share a common ancestor, mitochondrial ribosomes (mitoribosomes) are substantially different in composition and structure from bacterial ribosomes, with an increased number of proteins and ribosomal RNA (rRNA) that varies considerably in length (1). An extreme example of a mitoribosome with an unusually large number of proteins and highly reduced rRNAs is found in Trypanosoma brucei, a parasitic protozoan that causes sleeping sickness in humans (2). Due to the complexity of mitoribosomes, it is conceivable that a dedicated machinery comprising assembly factors evolved for mitoribosomal maturation. Ribosome biogenesis is a multistep process in which rRNA folds, often cotranscriptionally, and ribosomal proteins are recruited (3–5). Assembly and maturation of eukaryotic cytosolic ribosomes are facilitated by numerous factors that form large complexes together with ribosomal proteins and immature rRNA (5). For mitoribosomes, structures of mammalian late assembly intermediates of the large subunit (LSU), to which three assembly factors are bound, have been described (6). Although it has been suggested that some proteins detected in purified mitoribosomal small subunits (mt-SSUs) from T. brucei may be involved in mitoribosomal maturation (7) and several mitochondrial assembly factors in yeast and human have been described, it is not clear whether mitoribosomal assembly involves formation of large assembly complexes, and there is currently no structural information that would provide a more comprehensive overview of mitoribosomal biogenesis in any organism.

To better understand mitoribosome biogenesis, we analyzed three assembly intermediates of the mt-SSU from T. brucei by using single-particle cryo–electron microscopy (cryo-EM). We were able to determine the atomic structure of the earliest and largest of the analyzed intermediates, which we termed the mt-SSU assemblosome, and this allowed us to identify 34 assembly factors that participate in the maturation of the trypanosomal mt-SSU. Comparison of the assemblosome with the two other assembly intermediates and the mature trypanosomal mt-SSU (2), together with RNA interference (RNAi) experiments for selected assembly factors, provides insights into the complex mechanisms of mitoribosomal assembly.


Read more:

Science  13 Sep 2019:
Vol. 365, Issue 6458, pp. 1144-1149





Meanwhile we could also investigate some other structures that have nothing to do whether we're clever or not:


Structured Abstract



The eukaryotic genome is hierarchically organized in the cell nucleus into DNA loops, chromatin domains, compartments, and, ultimately, chromosomes. Many of the most prominent organizational features of genomes are highly reproducible on the population level and are evolutionarily conserved, suggesting functional relevance. Numerous organizational features, such as the location of a gene or promoter-enhancer loops, have been implicated in the regulation of genome processes including transcription, replication, and repair. At the same time, single-cell analysis has revealed extensive stochasticity of gene expression, with individual genes undergoing cycles of bursts in activity and periods of inactivity. Because gene activity is closely linked to features of genome organization, the extent of variability of genome organization at the single-cell level has arisen as a question of interest. We review new findings that document extensive cell- and allele-specific variability of genome organization and discuss potential mechanisms of structural variability and its implications for genome function.


Recent advances in genome mapping using single-cell biochemical and imaging methods have enabled systematic probing of higher-order genome organization at the level of individual cells. Results from these approaches validate observations from traditional population-based methods but also reveal that genome organization is considerably more variable than anticipated. In particular, specific chromatin-chromatin interactions appear to be present in only a relatively small fraction of cells in a population, and the genome organization at individual alleles in the same nucleus differs considerably. Furthermore, the internal shapes of structural features such as chromatin domains are fluid, and the genomic positions of the boundaries between chromatin domains vary from allele to allele. The highly variable nature of genome architecture points to a high degree of intrinsic noise in genome organization, in line with the observed stochasticity in gene expression.


Read more:


Science  06 Sep 2019:

Vol. 365, Issue 6457, eaaw9498




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