Leucine
Leucine questions and answers
Learn more about Leucine at Diet & Health.net.
Q: My evaluation of paper chromatography in a mixture of Leucine, Lysine and Aspartic acid?
All three mixtures in the experiment. Aspartic acid is purple, yellow shadow colour, Leucine is dark purple and Lysine is yellow and purple
A: When i have done paper chromatography with mixtures of amino acids, I use a solvent of 880 ammonia, water and another organic, would have to look it up! Once separated out, with a line drawn for the solvent front, remove, allow to dry and spray with ninhydrin, in a fume cabinet. After a few hours purple spots materialize and the spots can be assigned to amino acids by their Rf values.
Q: Is there a protein which lacks leucine residue?
Where can I find the list of proteins that lacks leucine residue?
A: I'm not sure about this but with my simple understanding about protein that it sould only be found on meat but as it is, I guess you should try soya beans and aloe vera...
Q: What are some important proteins that contain leucine zippers?
A: Well leucine zipper is a common motif for transcription factors. Because I'm a neuroscientist, the big one that sticks in my mind is Cyclic AMP Response Element-Binding Protein, i.e. CREB.
Some immediate early genes, like AP-1, c-fos are bZIPs too.
Q: What are the differences of functions between leucine serine and cysteine?
A: Leucine: Essential amino acid; builds body muscles
Serine: Serine is important in metabolism in that it participates in the biosynthesis of purines and pyrimidines. It is also the precursor to several amino acids, including glycine, cysteine, and, in bacteria, tryptophan. It is also the precursor to numerous of other metabolites, including sphingolipids. Serine is also a precursor to folate, which is the principal donor of one carbon fragments in biosynthesis.
Cysteine: Non-essential amino acid.
Q: what is the difference between deuterated and undeuterated leucine amino acid structurally and chemically?
what is the chemical structure of deuterated and undeuterated leucine amino acid? how many hydrogens and what positions of hydrogen are replaced by deuterons? is there any difference between the 2? can any1 help plzz..
A: Deuterated just means the amino acid has been make with deuterium in place of hydrogen. Deuterium is an radioisotope of hydrogen with 1 neutron, 1 proton and 1 electron (H atom only has 1 proton and 1 electron). There is no structural or chemical difference to the amino acid when a neutron is added and the isotope is stable, and deuterium is a stable radiolabel of H. Adding deuterium is done to make the amino acid traceable through the body using a radioactivity detector, but besides that there is no difference, which is why we deuterate things.
Q: What forces that keep the zipper zipped up in leucine zipper protein?
A: The main feature of the leucine zipper domain is the predominance of the common amino acid leucine at the interlink position of the heptad repeat. Leucine zippers were first identified by sequence alignment of certain transcription factors which identified a common pattern of leucines every seven amino acids. These leucines were later shown to form the hydrophobic core of a coiled coil.
Each half of a leucine zipper consists of a short alpha-helix with a leucine residue at every seventh position. The standard 3.6 residues per turn alpha-helix structure changes slightly to become a 3.5 residues per turn alpha-helix. Known also as the heptat repeat, one leucine comes in direct contact with another leucine on the other strand every second turn.
Q: what is leucine, isoleucine, and valine, and how do they help with workouts?
what is leucine, isoleucine, and valine, and how do they help with workouts?
A: They are amino acids of which there are 20. They are, however, also essential amino acids(EAA) of which there are 9. Your body does not make EAA, therefore you must intake EAA by eating proteins that contain EAA (amino acids make protein), which are called complete proteins.
If you fail to obtain even 1 EAA, this will cause your body's protein to degenerate, meaning your muscle will be broken down. This will effect your workouts in that, you won't be gaining and muscle mass or strength.
Unless you're a vegetarian, you can attain all EAA fairly easily.
Q: I read an article about getting more leucine in your diet will aid in weight loss?
Also does anybody know if amino acid supplements work to help lose weight.
A: Ameno Acids are good for the body, but I have not heard of any link between them ad weight loss.
Q: In what ways are the leucine zipper and beta sandwich protein similar? In what ways are they different?
A: Both rely on hydrophobic packing.
Beta sandwich, by definition, has a level of ordered secondary structure (beta sheet).
Q: How are leucine, serine and cysteine amino acids similar and different?
how do funtional groups in these amino acids contribute to their differences in properties?
A: First, they all have an alpha carbon, amino group, and carboxyl group. Serine and cysteine have a similarly structured side chain.
However, where serine has an OH, serine has an SH. This allows for cysteine to form disulfide bridges with other cysteines. Serine and cysteine both have polar side chains, while leucine has a nonpolar hydrophobic side chain.
Q: Is there any drug or way that will precipitate/crystalize LEUCINE in a urine sample?
A: Try Mountain Dew. That works better than any drug.
Q: Out of 64 possible codons, leucine has 6 codons. Is there any specific reason for this condition?
Is leucine the most prevalent amino acid in the universe?
Is leucine more favoured than any other amino acid?
A: Leucine is, as some say, one of the most abundantly found amino acid in proteins. Why so??
Leucine is a hydrophobic amino acid. The way I see the structure, it has hydrophobic groups at one extremity and an OH group on the other hand. It is highly used for hydrophobic interactions.
Leucine is a non-polar amino acid. Non-polar amino acids dominate in proteins because the surface only is made-up of polar amino-acids while non-polar amino acids occupy the core of the protein which is away from water.
Also, leucine forms a structural motif in proteins called Leucine zippers which are a heptad of amino acids arranged in a zig-zag formation. This helps proteins having this motif to bind to DNA.
Transcription factors are known to have a leu-zipper motif.
Q: give the structure of the reaction between leucine and serine in two different ways.?
A: first leu-ser
(i-Pr-CH2)-CH(NH2)-CONH-CH(CH2OH)-COOH
second, ser-leu
HOCH2-CH(NH2)-CONH-CH(CH2-i-Pr)-COOH
i-Pr = isopropyl or 2-propyl = (CH3)2-CH-
Q: Hi, can anyone tell me the general functions of leucine-rich motifs?
also is leucine rich motifs synonymous with leucine rich repeats?
thanks.
A: Attachment of transcription modulator and initiator.
Well at least from what I remember.
Q: Why is the amino acid leucine found in interior of a protein?
A: http://www.chembio.uoguelph.ca/educmat/phy456/456lec02.htm