「ProLine」の共起表現(1語右で並び替え)

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共起表現

「ProLine」の共起表現一覧(1語右で並び替え)

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ns with high proportions of alanine, glycine,	proline, and glutamic acid.
DBP is a member of the PAR bZIP (	Proline and Acidic amino acid-Rich basic leucine ZIPp
ric repulsion due to the pyrrolidone rings of	proline and hydroxyproline residues.
nherited cause of excess urinary excretion of	proline and glycine, similar to that found in iminogl
transporters for monoamines, the amino acids	proline and glycine, GABA, and a group of orphan tran
e high-affinity renal transporter of glycine,	proline and hydroxyproline found to be defective in b
The pathways linking arginine, glutamine, and	proline are bidirectional.
only proteinogenic amino acid of this type is	proline) are sometimes named imino acids, though this
This enzyme begins the process of degrading	proline by starting the reaction that converts it to
somal dominant retinitis pigmentosa, in which	proline changed to alanine.
In enzymology, a	proline dehydrogenase (EC 1.5.99.8) is an enzyme that
I homing endonuclease / maturase and the PutA	proline dehydrogenase / transcription factor, have be
	Proline derivative 3d is prepared in a separate leg f
This boroxine reacts with the	proline derivative (3d) to form the basic oxazaboroli
Protegrin-5 substitutes a	proline for an arginine with one less positive charge
PELP-1 (	proline, glutamic acid and leucine rich protein 1) PE
ssue is collagen, which is made up of lysine,	proline, glycine, alanine, and other amino acids .
oradrenaline/adrenaline, dopamine, serotonin,	proline, glycine, choline, betaine and taurine.
Each residue of the protein (except	proline) has an amide proton attached to a nitrogen i
bromination, amidation of the C-terminus, and	proline hydroxylation.
although some AT-hooks contain only a single	proline in the core sequence.
ne altered ALDH4A1 gene have normal levels of	proline in their blood.
β-Casomorphin 8 that has histidine instead of	proline in position 8, depending on whether it is der
PRODH gene have moderately elevated levels of	proline in their blood, but these levels do not cause
	Proline is often seen immediately following the end o
Because	proline is cheaply available in high optical purity,
ct biosynthetical precursor to the amino acid	proline is the imino acid (S)-Δ1-pyrroline-5-carboxyl
n of codon 23 in the rhodopsin gene, in which	proline is changed to histidine, accounts for the lar
ain many Gly-X-Y sequences, where X and Y are	proline, isoleucine, or hydroxylysine; they, therefor
Hyperprolinemia type II results in	proline levels in the blood between 10 and 15 times h
This enzyme participates in arginine and	proline metabolism and aminoacyl-trna biosynthesis.
etabolism, glutamate metabolism, arginine and	proline metabolism, and nitrogen metabolism.
This enzyme participates in arginine and	proline metabolism.
ates in glutamate metabolism and arginine and	proline metabolism.
ipates in lysine degradation and arginine and	proline metabolism.
lucuronate interconversions, and arginine and	proline metabolism.
PROLINO" or "ProliNO") is the abbreviation of	proline nitric oxide or proline NO.
iad (where Xaa and Yaa are any amino acid), a	proline occupying the Yaa position is hydroxylated to
Other names in common use include	proline oxidase, L-proline oxidase, 1-pyrroline-5-car
in the PRODH gene, which codes for the enzyme	proline oxidase.
Hydroxyproline and	proline play key roles for collagen stability.
This modification of the	proline residue increases the stability of the collag
ween the thermostability of a protein and its	proline residue content.
he N-terminal amino acid from peptides with a	proline residue in the penultimate position.
) the site of cleavage is on either side of a	proline residue, (iii) the N-terminal residue is lysi
	Proline residues are known to be structure-breaking r
peptide bonds from trans form to cis form at	proline residues and facilitates protein folding.
nt DNA technology, the penultimate lysine and	proline residues on the C-terminal end of the B-chain
o peptidic bonds in protein (especially, like	proline residues) and that is why it can precipitate
eaves peptide bonds at the C-terminal side of	proline residues.
in folding chaperones for proteins containing	proline residues.
ch domain, a pleckstrin homology domain and a	proline rich region
m the N-terminal region of the protein PROL1 (	proline rich, lacrimal 1).
d, glycine, histidine, lysine, phenylalanine,	proline, serine, and threonine belong to class-II syn
deficiency patients is caused by a leucine to	proline substitution.
N-terminal domain is also found in the PROSC (	proline synthetase co-transcribed bacterial homolog)
ntaining tandem repeats rich in threonine and	proline that varies between 50 and 115 copies in diff
ed structure suggests that it is derived from	proline, the results from the experiments indicated t
ver, these atoms are both H-bond acceptors in	proline; there is no H-bond donor due to the cyclic s
A change in codon 102 from	proline to leucine on chromosome 20, has been found i
ase, prolyl-transfer ribonucleate synthetase,	proline translase, prolyl-transfer ribonucleic acid s
	Proline U100 in South Africa.
ol is obtained by reduction of the amino acid	proline using lithium aluminium hydride.

共起表現

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「ProLine」の共起表現一覧(1語右で並び替え)