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]

http://en.wikipedia.org/wiki/Adenosine_triphosphate

-------------------------

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...

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....

http://www.independent.co.uk/life-style/health-and-families/health-news/scientists-debunk-decadesold-theories-on-losing-weight-2344151.html

---------------------

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...

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.''

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...

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:

Abstract

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:

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

Read from top.

https://www.youtube.com/watch?v=vBiIDwBOqQA

For decades, biology has been dominated by information – the power of genes. Yet there is no difference in the information content between a living cell and one that died a moment ago.

Nick Lane takes us on a journey which turns the standard view upside down, capturing an extraordinary scientific renaissance that is hiding in plain sight.

At its core is an amazing cycle of reactions that uses energy to transform inorganic molecules into the building blocks of life – and the reverse.

To understand this cycle is to fathom the deep coherence of the living world. It connects the origin of life with the devastation of cancer, the first photosynthetic bacteria with our own mitochondria, sulfurous sludges with the emergence of consciousness, and the trivial differences between ourselves with the large-scale history of our planet.

This talk was recorded at the Royal Institution on 20 May 2022.

READ FROM TOP

FREE JULIAN ASSANGE NOW....