What happens when a diatomic molecule loses an electron Does the bond weaken?
No, it is not correct to say that the bond energy always decreases when a diatomic molecule loses an electron. F2 and O2 are counterexamples to this point. When a molecule loses an electron, it will come from the highest occupied molecular orbital. In both O2 and F2, this MO is an antibonding MO. Removing an electron from an antibonding MO *increases* the bond energy.
The polyamines are organic compounds having two or more primary amino groups - such as putrescine, cadaverine, spermidine, and spermine - that are essential molecules in both eukaryotic and prokaryotic cells. Cyclen is the main representative of a class of cyclic polyamines. Polyethylene amine is a polymer based on aziridine monomer.
Why are lipids described as non-polymeric?
Unlike the proteins,nucleic acid and polysaccharides, lipids are not polymers.
It is because it do not contain any fixed monomeric units instead it has a long chain of methylene groups (-CH2-CH2-CH2-CH2-)and has a general formula :
CH3-(CH2)n-COOH
How does induction by IPTG differ from induction by lactose via allolactose?
Lactose is eventually metabolized in the cell to allolactose, which binds to the lacI repressor, leading to the induction of the lac promoter (or derivatives of the lac promoters). The allolactose is also eventually metabolised. IPTG does essentially the same as allolactose, however, it does not get metabolized. Moreover, since lactose gets transported in the cell by the lacY gene product and metabolized to allolactose by the lacZ gene product, lactose cannot be used in lacZY- strains for induction. IPTG, however, can be used since it does not require the two genes.
Mixing rubidium gunpowder with silver nitrate and capping it would likely produce a chemical reaction resulting in a flash of light, making it more of a flare rather than a decent explosive. The reaction between the two compounds may release a significant amount of light and heat but may not produce a large explosion typically associated with high-explosive materials. Additionally, using these chemicals in a confined space could be dangerous and should be avoided.
Why there are 4 D-aldopentoses but only two D-ketopentoses?
This is my understanding.... though I am no expert by any means...
Aldopentoses have 3 chiral centers (assymetrical carbon atoms) which allows for 8 stereoisomers (4D and 4L) while ketopentoses have 2 chiral centers which makes 4 stereoisomers .
Gene silencing is a process by which the expression of a specific gene is suppressed, leading to a reduction or elimination of the gene's protein product. This can occur through various mechanisms, such as RNA interference or epigenetic modifications, which can silence gene expression at the transcriptional or post-transcriptional level. Gene silencing plays a crucial role in regulating gene expression and can be used in research and therapeutic applications.
Anton van Leeuwenhoek
What is another name for hydrolysis?
Another name for hydrolysis is reaction. Hydrolysis is a chemical reaction where water reacts with a compound. This produces other compounds.
Why breathed-out air turns time water cloudy quicker than breathed-in air?
breathed out air turns lime water cloudy than breathed out air cuz the carbon dioxide content present in breathed out air(0.04% approximately) as compared to breathed out air(4% approximately)so as CO2 passes through lime water it turns lime water cloudy:)
Somatodendritic refers to the part of a neuron that includes the cell body (soma) and dendrites. This region of the neuron is involved in receiving and integrating incoming signals from other neurons.
Why does acid clot appear pink or white with a pink band at the top?
Litmus milk is an undefined medium consisting of skim milk and the pH indicator azolitmin.
Azolitmin is purple between pH of 4.6 and 8.2. It turns pink when pH reaches 4.5 and blue at a pH of 8.3.
Lactose ferminatation turns the litmus pink due to acidity. If litmus is reduced during lactose fermentation it will turn the medium white. Acid may cause an acid clot this is due to the casein precipitating. Heavy gas production can cause stormy fermentation, this is due to the breaking up of the clot.
FAD co enzyme participates in which type of reactions?
FAD (flavin adenine dinucleotide) participates in oxidation-reduction reactions as a cofactor, primarily in enzymes that catalyze reactions involving the transfer of electrons. It accepts two electrons and two protons to form FADH2, which can then donate these electrons to other molecules in the cell.
response to varying light intensities. By measuring the rate of oxygen production in the alga under different colors of light, Engelmann was able to determine that red and blue light were the most effective in driving photosynthesis. This led to the conclusion that chlorophyll absorbs light most efficiently in these two regions of the spectrum.
Indicate whether each of the following pairs represent constitutional isomers, the same compound, or different compounds 2-methoxybutane and 3-methyl-2-butanol
Does your body contain more neutrons than protons?
Short Answer:
There are more protons than neutrons in the human body.
This is primarily because we are mostly water and H2O is mostly hydrogen. Hydrogen is a single proton and is 25% of all the atoms in the body.
Of the six elements that make up 99% of the mass of the human body (oxygen 65%, carbon 18%, hydrogen 10%, nitrogen 3%, calcium 1.4%, phosphorous 1.1%), all but hydrogen and phosphorous have an equal number protons and neutrons in the dominant isotope and hydrogen, be 25% of all atoms, overwhelms the balance giving more protons than neutrons.
Long Answer:
The human body (and other living things) contains a much greater number of protons than neutrons. Consider the data from the "related links" below which describe the elemental composition of the human body. This data allows one to calculate the number of neutrons and protons for each element and determine that there are about 4.15*10^27 protons more than the number of neutrons.
Perform the following calculations for each of the elements on the list: determine the difference between number of neutrons and protons in the atomic nucleus and call it N-P ('N' minus 'P') for each element; divide the mass in grams of the element in the human body by the atomic mass of the element to get the moles of the element in the human body; multiply the moles by Avagadro's constant (~6.022*10^23) to get the number of atoms; multiply the number of atoms with N-P to get the net neutrons for the element.
The list at the cited webpage is conveniently in order of most abundant to least abundant. If we look at only the first fifteen elements at the ones that have N-P not equal to zero we find that the net neutrons is on the order of -(10^27). This is due to the fact that Hydrogen has 1 proton and 0 neutrons (N-P = -1), and with a mass contribution of 7 kilograms to the human body, adds nearly 7000 moles of protons. Note, I'm ignoring the rest of the elements on the list after Cadmiun (the fifteenth with N-P != 0) since the mass contribution after Cadmium is less than 0.050 grams, none of the remaining elements should be able to contribute enough neutrons to increase the net neutrons into positive range. (The trend is much more clear if you perform the calculations and list the elements.)
Additionally, although Carbon makes up ~16 kilograms of the body, the amount of isotopic carbon is only about 1% of that value at most, so the contribution from isotopic carbon would be only about 160 grams, which if it were all C14, would only add 1.38*10^25 neutrons.
Insects use chitin for movement. Chitin is a tough, flexible substance that makes up the exoskeleton of insects, providing support and protection for their bodies. Muscles attached to the inner surface of the exoskeleton allow insects to move by contracting and relaxing.
Titin is the common name for a protein whose full name is over 189,000 letters [base pairs] long. Its 'formula' follows:
Methionylthreonylthreonylglutaminylal...- ylglutaminylprolylleucylglutaminylser...- lserylthreonylalanylthreonylphenylala...- rylglycylphenylalanylprolylvalylproly...- lanylarginylaspartylglycylglutaminylv...- nylleucylprolylglycylvalylglutaminyli...- ylglycylarginylalanyllysylleucylthreo...- llysylalanylasparaginylserylglycylarg...- eonylasparaginylglycylserylglycylglut...- nylglutamylleucylleucylvalyllysylalan...- asparaginylphenylalanylvalylglutaminy...- ylthreonylvalylarginylglutaminylglycy...- utaminylvalylarginylvalylthreonylglyc...- lylvalyllysylphenylalanyltyrosylargin...- cylglutaminylserylserylleucylaspartyl...- glutaminylglutamylglycylaspartylleucy...- anylglutamylalanyltyrosylprolylglutam...- serylvalylasparaginylalanylthreonylas...- ylthreonylserylthreonylalanylglutamyl...- tamylglutamylglutamylvalylprolylalany...- eucylvalylserylthreonylalanylglutamin...- glutaminylthreonylarginylisoleucylglu...- ylhistidylphenylalanylaspartylalanyla...- lylglutamylmethionylvalylisoleucylasp...- nylglutaminylleucylprolylhistidyllysy...- lprolylprolyllysylprolyllysylserylarg...- erylisoleucylalanylalanyllysylalanylg...- ylglutaminylserylprolylserylprolyliso...- lprolylvalylarginylhistidylvalylargin...- lylvalylarginylserylvalylserylprolyla...- onylserylprolylisoleucylarginylserylv...- thionylarginyllysylthreonylglutaminyl...- ylglycylprolylglutamylvalylprolylprol...- tamylglycyltyrosylvalylalanylserylser...- ylarginylglutamylthreonylthreonylleuc...- minylisoleucylarginylthreonylglutamyl...- cylarginyltyrosylglycylvalylglutaminy...- eucylserylglycylalanylalanylglycylala...- serylalanylseryltyrosylalanylalanylgl...- lalanyllysylglutamylvalyllysylglutami...- lanylalanylvalylalanylthreonylvalylva...- lalanylarginylvalylarginylglutamylpro...- tamylglutaminylthreonylalanylglutamin...- eonylalanylvalylhistidylisoleucylglut...- glutaminylvalylarginyllysylglutamylal...- threonyllysylvalylvalylvalylalanylala...- lutaminylglutamylleucyllysylserylargi...- leucylthreonylthreonyllysylglutaminyl...- alylthreonylhistidylglutamylglutaminy...- ylglutamyllysylthreonylphenylalanylva...- ylalanylalanyllysylalanyllysylglutamy...- oleucylserylglutamylglutamylisoleucyl...- taminylvalylthreonylglutaminylglutamy...- ylthreonylarginyllysylthreonylvalylva...- nylthreonylprolyllysylvalyllysylgluta...- larginylglycylarginylglutamylglycylis...- lutamylglutaminylvalylglutaminylisole...- ethionylarginyllysylglutamylalanylglu...- hreonylisoleucylalanylvalylalanylthre...- utaminylglutamylthreonylisoleucylleuc...- onylmethionylalanylthreonylarginylglu...- utaminylvalylthreonylhistidylglycylly...- lalanylglutamylalanylvalylalanylthreo...- ylglutaminylalanylarginylvalylarginyl...- lycylhistidylleucylglutamylglutamylse...- threonylthreonylleucylglutamyltyrosyl...- leucylserylalanylalanyllysylvalylalan...- nylprolylalanylserylglutamylprolylhis...- llysylprolylarginylvalylisoleucylglut...- nylhistidylisoleucyllysylthreonylthre...- hionylhistidylisoleucylserylserylglut...- eonylaspartylleucylthreonylthreonylgl...- laspartyllysylarginylprolylarginylthr...- alanylthreonylvalylseryllysylisoleucy...- ylhistidylglycyltyrosylglutamylalanyl...- lisoleucylalanylthreonylleucylglutami...- eonylserylserylalanylglutaminyllysyli...- alanylprolylthreonylvalyllysylprolyls...- nylalanylglutamylprolylthreonylprolyl...- olylphenylalanylalanylaspartylthreony...- erylglutamylalanylglycylvalylglutamyl...- lylserylisoleucylthreonylglycylthreon...- ylarginylphenylalanylglutamylvalylleu...- yllysylvalylthreonylglutamylthreonyla...- alylglutamylisoleucylprolylvalylthreo...- rylglycylleucyllysylasparaginylvalylt...- lutamylserylvalylthreonylleucylglutam...- cyltyrosylprolylserylprolylthreonylva...- lutamylaspartyltyrosylglutaminylisole...- tylphenylalanylglutaminylisoleucylthr...- ylisoleucylalanylarginylleucylmethion...- ylalanylalanylglutamylaspartylserylgl...- inylserylalanylvalylasparaginylglutam...- onylserylcysteinyltyrosylleucylalanyl...- tamylphenylalanylglutamyllysylglutamy...- glutamyllysylphenylalanylthreonylthre...- ylalanylvalylglutamylserylarginylaspa...- tylthreonylserylleucylthreonylglutamy...- lglycylglutamylprolylalanylalanylprol...- yllysylprolylvalylvalylglutaminyllysy...- lvalylvalylphenylalanylglycylcysteiny...- nylprolyllysylprolylhistidylvalyltyro...- lylprolylleucylthreonylthreonylglycyl...- tyrosylasparaginyllysylglutaminylthre...- ylvalylisoleucylserylmethionylthreony...- lanylglycylglutamyltyrosylthreonyliso...- sylhistidylglycylglutamylthreonylsery...- lutamylglutamylalanylaspartyltyrosylg...- ylglutaminylglutaminylglutamylmethion...- taminylvalylthreonylalanylphenylalany...- ylvalylglycylglutamylthreonylalanylpr...- rylglutamyltyrosylglutamyllysylglutam...- inylalanylleucylisoleucylarginyllysyl...- eonylvalylvalylvalylarginylthreonylty...- glutamylphenylalanylhistidylisoleucyl...- ylarginylleucylisoleucyllysylglutamyl...- ucylisoleucyllysylthreonylthreonylleu...- mylglutamylaspartylglycylglutamylglut...- lisoleucylserylglutamylserylglutamyla...- lanylaspartylleucylarginylisoleucylly...- lleucylglutamylglycylmethionylglycylv...- einyllysylmethionylserylglycyltyrosyl...- yltryptophyltyrosyllysylaspartylglycy...- lycylglutamylarginyltyrosylglutaminyl...- lutaminylaspartylglycylarginylalanyls...- lvalylleucylprolylglutamylaspartylglu...- lanylphenylalanylalanylserylasparagin...- nylisoleucylcysteinylserylglycyllysyl...- ylalanylprolylleucylglycylalanylproly...- nylleucylglutamylprolylvalylserylargi...- rolylarginylserylvalylserylarginylser...- ylprolylalanylarginylmethionylserylpr...- lalanylarginylmethionylserylprolylala...- arginylarginylleucylglutamylglutamylt...- ylleucylglutamylarginylleucyltyrosyll...- yllysylprolylvalylserylphenylalanylly...- ylasparaginylcysteinylarginylphenylal...- cylarginylprolylmethionylprolylglutam...- ylalanylhistidylaspartylglycylglutami...- ylaspartyltyrosylthreonylhistidyllysy...- artylglycylthreonylglutaminylserylleu...- ylthreonylprolylserylaspartylserylgly...- lylalanylglutaminylasparaginylarginylylserylvalylisoleucylleucylthreonylvaylglutaminylvalyllysylprolylmethionyllysylasparaginylvalylasparaginylisoleeucylglutamylmethionyllysylvalylarginlylasparaginylprolylaspartylisoleucyllserylaspartylisoleucylisoleuc
Paraquat is one of the most widely used herbicides in the world. It is a viologen, killing plant tissue just by contact. It is toxic to humans if ingested.
It is also an inhibitor of photosystem I, which causes formation of ROS(Reactive Oxygen Species).
Positive work done on the surroundings by the system (q>0) and negative heat transferred from the system to the surroundings (w<0).
The primary structure of DNA, its sequence of nucleotides, encodes the genetic information in the form of genes. These genes control the production of proteins, enzymes, and other molecules that determine an organism's traits. The secondary structure of DNA, its double helix shape, ensures stability and integrity of the genetic code, allowing for accurate replication and transmission of genetic information.
What is the amino acid structure of tubulin?
That'll vary depending on which tubulin protein you look at, as there are different types, and variation between species as well.
If you don't know which one to look for, take a bovine (cow) or porcine (pig) alpha/beta tubulin.
For the most complete set of data on its structure, find a pdb file (search Google for "pdb" and use the search functions of one of those websites to find tubulin).
For less detailed structure, you can find its "FASTA" sequence. RCSB (find it on Google) will allow you to download the pdb file and the FASTA sequence for any known protein.
You can also find the original paper that described the amino acid sequence - just search Google. If you don't find it on Google, chances are you'll have to pay for it!
If you really don't mind which tubulin you get the structure of, use this one to save some time. It is the bovine (cow/cattle) alpha and beta tubulin monomers. The structure was derived as a dimer, so there are two sequences here. The first one is the beta chain, the second one is the alpha chain.
>1JFF:B|PDBID|CHAIN|SEQUENCE
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSY HGDSDLQLERINVYYNEAAGNKYVPRAILVDLEPGTM DSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTE GAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTG SGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEP YNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTP TYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNM VPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQM FDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDE QMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMS ATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGE GMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEF EEEGEEDEA
>1JFF:A|PDBID|CHAIN|SEQUENCE
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQM PSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPT VIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIG KEIIDLVLDRIRKLADQCTGLQGFSVFHSFGGGTGSGF TSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNS ILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTN LNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRG HFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMV KCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTI QFVDWCPTGFKVGINYEPPTVVPGGDLAKVQRAVCML SNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGME EGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
Why metal nitrogen bond is stronger than metal oxygen bond in bio-inorganic compound?
Metal-nitrogen bonds are typically stronger than metal-oxygen bonds in bio-inorganic compounds because nitrogen is a smaller atom than oxygen, which allows for stronger overlap between the metal and nitrogen orbitals. Additionally, nitrogen has a higher electronegativity than oxygen, resulting in a greater degree of covalency in the metal-nitrogen bond compared to the metal-oxygen bond. These factors lead to a stronger bond between the metal and nitrogen atoms in bio-inorganic compounds.
What is the number on the upper right hand corner of every element on the Periodic Chart?
The number in the upper right corner of each element on the Periodic Table is its atomic number. This number represents the number of protons in the nucleus of an atom of that element.
What does the symbol dPa stand for?
Probably decipascals. The pascal is a unit of pressure, newtons per square meter. 1 dPa would be one tenth of a pascal.