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Cambridge) was an English biochemist who was awarded the Nobel Prize in Physiology or Medicine in
1929, with Christiaan Eijkman, for the discovery of vitamins. He also discovered the amino acid
tryptophan, in 1901. He was President of the Royal Society from 1930-1935.
tryptophan (trĭp`təfăn), organic compound, one of the 20 amino acids amino acid (əmē`nō)
..... Click the link for more information. commonly found in animal proteins. Only the L-stereoisomer
appears in mammalian protein. It is one of several essential amino acids needed in the diet; human
beings cannot synthesize it from simpler metabolites. Young adults require about 7 mg of this amino
acid per day per kg (3 mg per lb) of body weight. Nicotinic acid (niacin), a vitamin vitamin, group of
organic substances that are required in the diet of humans and animals for normal growth, maintenance
of life, and normal reproduction. Vitamins act as catalysts; very often either the vitamins themselves are
coenzymes , or they form integral parts
..... Click the link for more information. of the B complex, can be made from tryptophan in the body,
but evidently the rate of transformation is insufficient for the demands of normal growth and
maintenance, and hence nicotinic acid must be supplied in the diet. Deficiency of tryptophan in the diet
enhances the progress of the vitamin-deficiency disease pellagra pellagra (pəlăg`rə)
..... Click the link for more information. , which is treated by restoring nicotinic acid to the diet, usually
supplemented with tryptophan. Bacteria in the intestine break tryptophan down to compounds such as
skatole and indole, which to a great extent are responsible for the unpleasant odor of feces. Tryptophan
contributes to the structure of proteins into which it has been incorporated by the tendency of its side
chain to participate in hydrophobic interactions (see isoleucine isoleucine (ī'səl
..... Click the link for more information. ). The amino acid was isolated from casein (milk protein) in
1901, and its structure was established in 1907.
The amino acid was isolated from casein (milk protein) in 1901, and its structure was established in
1907.
Tryptophan adalah asam amino esensial. This means that it must be obtained through the diet in
adequate quantities to meet the body's needs. Ini berarti bahwa hal itu harus diperoleh dari makanan
dalam jumlah yang memadai untuk memenuhi kebutuhan tubuh.
Tryptophan is a precursor in the central nervous system of the neurotransmitter serotonin. Triptofan
adalah prekursor di dalam sistem saraf pusat dari neurotransmitter serotonin. Serotonin modulates
mood and sleep patterns. Memodulasi serotonin suasana hati dan pola tidur.
Tryptophan is also converted in the body to niacin (vitamin B-3) and picolinic acid. Triptofan juga
dikonversi dalam tubuh untuk niasin (vitamin B-3) dan asam picolinic. Giving high doses of vitamin B-
6 along with tryptophan increases its conversion to niacin and decreases its uptake into the nervous
system. Pemberian dosis tinggi vitamin B-6 bersama dengan triptofan meningkatkan konversi untuk
niasin dan berkurang dengan penyerapan ke dalam sistem saraf. One standard test for vitamin B-6
deficiency is to supplement an individual with tryptophan and then look at the spill of xanthurenic acid
in his or her urine. Satu standar tes untuk vitamin B-6 adalah untuk melengkapi kekurangan individu
dengan triptofan dan kemudian melihat tumpahan asam xanthurenic dalam air seni nya. High levels of
xanthurenic acid in the urine are indicative of the need for vitamin B-6. Tinggi asam xanthurenic dalam
urin adalah indikasi dari kebutuhan akan vitamin B-6. Low blood tryptophan levels have been reported
in depressed patients and are corrected with tryptophan supplementation. Tingkat triptofan darah
rendah telah dilaporkan terjadi pada pasien depresi dan triptofan diperbaiki dengan suplemen.
Tryptophan has clinical impact on depression, particularly endogenous (unipolar) depression. Triptofan
memiliki dampak klinis depresi, terutama endogen (unipolar) depresi. Doses of 1,000 to 3,000 mg
divided throughout the day and taken on an empty stomach have been employed. Dosis 1.000 hingga
3.000 mg dibagi sepanjang hari dan diambil pada waktu perut kosong telah digunakan.
Tryptophan has been shown in double-blind trials to also be very helpful in treatment of insomnia when
given in doses between 1,000 and 2,000 mg per day one hour before bed. Triptofan telah ditunjukkan
dalam double blind cobaan untuk juga akan sangat membantu dalam pengobatan insomnia ketika
diberikan dalam dosis antara 1.000 dan 2.000 mg per hari satu jam sebelum tidur.
It has been found best to administer this amino acid along with a carbohydrate source such as fruit juice
because insulin, which is secreted after the carbohydrate load, has been found to help tryptophan
absorption into the nervous system. Telah ditemukan terbaik untuk memberikan asam amino ini
bersama dengan sumber karbohidrat seperti jus buah karena insulin, yang dikeluarkan setelah beban
karbohidrat, telah ditemukan untuk membantu penyerapan triptofan ke dalam sistem saraf. Giving
tryptophan along with other neutral amino acids blocks its absorption and prevents therapeutic results.
Memberikan triptofan bersama dengan asam amino netral lainnya blok dengan penyerapan dan
mencegah hasil terapeutik. Generally, tryptophan should be given away from a meal on an empty
stomach along with a carbohydrate source for optimal therapeutic results. Secara umum, triptofan harus
diberikan jauh dari makan perut kosong bersama dengan sumber karbohidrat hasil terapeutik yang
optimal.
Nutrisi bisa didapat dari berbagai macam sumber, antara lainnya dari makanan sehari-hari. Tetapi tubuh
balita yang sedang berkembang membutuhkan tambahan dari susu. Susu telah dikenal mempunyai nilai
nutrisi yang sangat baik, karena mengandung kalsium, protein, dan berbagai macam vitamin seperti A,
D, dan B12 (Riboflavin). Karena itulah, anak-anak dianjurkan untuk meminum susu setiap hari agar
mereka mendapat nutrisi yang lebih lengkap dan lebih baik.
Untuk menyediakan nutrisi yang terbaik bagi balita Anda yang sedang bertumbuh, Frisian Flag 123 &
456 telah diformulasi dengan DHA, AA, SA, Sphingomyelin dan T+T (Tyrosine dan Tryptophan). Jika
anak Anda tidak menyukai susu putih, ada pilihan rasa madu dan coklat. Nutrisi penting apa yang
terkandung dalam Frisian Flag 123 dan 456? Mari kita kenali lebih dekat lagi.
L-Tryptophan
IUPAC name
[show]
Trtptophan
Other names 2-Amino-3-(1H-indol-3-yl)propanoic acid Identifiers CAS number 73-22-3 Y PubChem
6305 SMILES
[show]
N[C@@H](Cc1c2ccccc2n([H])c1)C(O)=O
Properties Molecular formula C11H12N2O2 Molar mass 204.23 g mol−1 Supplementary data page
Structure and
properties n, εr, etc. Thermodynamic
data Phase behaviour
Solid, liquid, gas Spectral data UV, IR, NMR, MS
Proline
Prolina Nama sistematik Asam S-pirolidin-
2-karboksilat Singkatan Pro
P Kode genetik CCx (x = semua basa N) Rumus kimia C5H9NO2 Massa molekul 115,13 g mol-1 Titik
lebur 221°C Massa jenis ? g cm-3 Titik isoelektrik 6,30 pKa 1,95
10,47 Nomor CAS [147-85-3] SMILES C1CCNC1C(=O)O
Research work
Fischer's early discovery of phenylhydrazine and its influence on his later work have already been
mentioned. While he was at Munich, Fischer continued to work on the hydrazines and, working there
with his cousin Otto Fischer, who had followed him to Munich, he and Otto worked out a new theory
of the constitution of the dyes derived from triphenylmethane, proving this by experimental work to be
correct.
At Erlangen Fischer studied the active principles of tea, coffee and cocoa, namely, caffeine and
theobromine, and established the constitution of a series of compounds in this field, eventually
synthesizing them.
The work, however, on which Fischer's fame chiefly rests, was his studies of the purines and the sugars.
This work, carried out between 1882 and 1906 showed that various substances, little known at that
time, such as adenine, xanthine, in vegetable substances, caffeine and, in animal excrement, uric acid
and guanine, all belonged to one homogeneous family and could be derived from one another and that
they corresponded to different hydroxyl and amino derivatives of the same fundamental system formed
by a bicyclic nitrogenous structure into which the characteristic urea group entered. This parent
substance, which at first he regarded as being hypothetical, he called purine in 1884, and he
synthesized it in 1898. Numerous artificial derivatives, more or less analogous to the naturally-
occurring substances, came from his laboratory between 1882 and 1896.
In 1884 Fischer began his great work on the sugars, which transformed the knowledge of these
compounds and welded the new knowledge obtained into a coherent whole. Even before 1880 the
aldehyde formula of glucose had been indicated, but Fischer established it by a series of
transformations such as oxidation into aldonic acid and the action of phenylhydrazine which he had
discovered and which made possible the formation of the phenylhydrazones and the osazones. By
passage to a common osazone, he established the relation between glucose, fructose and mannose,
which he discovered in 1888. In 1890, by epimerization between gluconic and mannonic acids, he
established the stereochemical and isomeric nature of the sugars, and between 1891 and 1894 he
established the stereochemical configuration of all the known sugars and exactly foretold the possible
isomers, by an ingenious application of the theory of the asymmetrical carbon atom of Van't Hoff and
Le Bel, published in 1874. Reciprocal syntheses between different hexoses by isomerization and then
between pentoses, hexoses, and heptoses by reaction of degradation and synthesis proved the value of
the systematics he had established. His greatest success was his synthesis of glucose, fructose and
mannose in 1890, starting from glycerol.
This monumental work on the sugars, carried out between 1884 and 1894, was extended by other work,
the most important being his studies of the glucosides.
Between 1899 and 1908 Fischer made his great contributions to knowledge of the proteins. He sought
effective analytical methods of separating and identifying the individual amino acids, discovering a
new type, the cyclic amino acids: proline and oxyproline. He also studied the synthesis of proteins by
obtaining the various amino acids in an optically active form in order to unite them. He was able to
establish the type of bond that would connect them together in chains, namely, the peptide bond, and by
means of this he obtained the dipeptides and later the tripeptides and polypeptides. In 1901 he
discovered, in collaboration with Fourneau, the synthesis of the dipeptide, glycyl-glycine and in that
year he also published his work on the hydrolysis of casein. Amino acids occurring in nature were
prepared in the laboratory and new ones were discovered. His synthesis of the oligopeptides culminated
in an octodecapeptide, which had many characteristics of natural proteins. This and his subsequent
work led to a better understanding of the proteins and laid the foundations for later studies of them.
In addition to his work in the fields already mentioned, Fischer also studied the enzymes and the
chemical substances in the lichens which he found during his frequent holidays in the Black Forest, and
also substances used in tanning and, during the final years of his life, the fats. In 1890, he also proposed
a "Lock and Key Model" to visualize the substrate and enzyme interaction. Though, later studies did
not support this model in all enzymatic reactions.
Fischer is noted for his work on sugars among other work the organic synthesis of (+) glucose[1] and
purines (including the first synthesis of caffeine).
Proline P (Pro)
Chemical Properties: Physical
Properties:
Cyclic Nonpolar
Biosynthesis of Proline
Proline shares many properties with the aliphatic group.
Proline is formally NOT an amino acid, but an imino acid. Nonetheless, it is called an amino acid.
The primary amine on the α carbon of glutamate semialdehyde forms a Schiff base with the aldehyde
which is then reduced, yielding proline.
When proline is in a peptide bond, it does not have a hydrogen on the α amino group, so it cannot
donate a hydrogen bond to stabilize an α helix or a β sheet. It is often said, inaccurately, that proline
cannot exist in an α helix. When proline is found in an α helix, the helix will have a slight bend due to
the lack of the hydrogen bond.
Proline is often found at the end of α helix or in turns or loops. Unlike other amino acids which exist
almost exclusively in the trans- form in polypeptides, proline can exist in the cis-configuration in
peptides. The cis and trans forms are nearly isoenergetic. The cis/trans isomerization can play an
important role in the folding of proteins and will be discussed more in that context.
Biosynthesis of Proline
Glutamic acid is easily converted into proline. First, the γcarboxyl group is reduced to the aldehyde,
yielding glutamate semialdehyde. The aldehyde then reacts with the α-amino group, eliminating water
as it forms the Schiff base. In a second reduction step, the Schiff base is reduced, yielding proline.