Examples of 'n-glycosylation' in a sentence
Meaning of "n-glycosylation"
n-glycosylation (noun): A type of glycosylation process in biochemistry where a sugar molecule is attached to a nitrogen atom in a protein structure. This phrase is commonly used in the context of molecular biology and biochemistry
How to use "n-glycosylation" in a sentence
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n-glycosylation
N-glycosylation signals and the stop codon are indicated by asterisks.
A potential site of N-glycosylation is present in this loop.
N-glycosylation in various host cells has been also addressed in further studies.
The five putative N-glycosylation sites are squared.
N-glycosylation signals are indicated by asterisks and the polyadenylation signal is double underlined.
It also contains four predicted N-glycosylation sites.
The putative N-glycosylation sites are indicated by asterisks.
They all have four potential N-glycosylation sites.
The potential N-glycosylation sites are underlined twice.
There are no apparent sites for N-glycosylation.
The potential N-glycosylation sites are underlined in each sequence.
Other fragments include a cysteine residue or an N-glycosylation site.
One additional N-glycosylation site was introduced in each case.
The introduced glycosylation site is in particular an in vivo N-glycosylation site.
Attachment of glycans at N-glycosylation sites is shown.
See also
N-glycosylation of the glycopeptide was determined after separation on preparative HPLC.
The asparagines of the N-glycosylation sites are double underlined.
No N-glycosylation of the human type has been found so far in this microorganism.
Another option is inactivation of N-glycosylation sites by site-specific mutagenesis.
Potential N-glycosylation sites are underlined and putative transmembrane segments are overlined.
We note that the protein contains six potential N-glycosylation sites.
The potential N-glycosylation sites are shown as green balls.
We note that the protein contains seven potential N-glycosylation sites.
The potential N-glycosylation sites are in bold.
The modification of proinsulin gene is preferred by creating N-glycosylation site AsnXSer.
Ten potential N-glycosylation sites are marked by closed circles.
The glycosylation site that is deleted can include an N-glycosylation site.
Engineering of protein N-glycosylation in yeast - towards production of therapeutic antibodies.
Furthermore, the immunoglobulins of the invention also have a particular N-glycosylation profile.
Four potential N-glycosylation sites are located in the extracelluar region.
Further, the linkers may be modified by incorporation of N-glycosylation motifs as described above.
Four potential N-glycosylation sites are located in the extracellular region.
Exemplary derivatives of hedgehog proteins include polypeptides which lack N-glycosylation sites e . g.
Twelve consensus N-glycosylation motifs are indicated with filled triangles.
The study of the glycoproteins revealed a modification of N-glycosylation linked to a convulsante dose of MSO.
Canonical N-glycosylation sites do not appear within the sequence.
Putative transmembrane domains are shaded, and predicted N-glycosylation sites are marked with circles.
There are 6 possible N-glycosylation sites present in the presumed extracellular domain.
Typically, glycosylation occurs in the Fc region of the antibody at a highly conserved N-glycosylation site.
Particular N-glycosylation sites are not required for activity, whereas others are.
Awamori achieved by the introduction of a N-glycosylation consensus site into a coding sequence.
Potential N-glycosylation sites should be conserved if mannosylation of the protein is desired.
Attachment of glycans at each of the N-glycosylation sites accounts for the observed mass.
The primary sequence of these fusión proteins contains four possible N-glycosylation sites.
Such one or more additional N-glycosylation sites are not always glycosylated.
The deleted repeat also contains one of the 5 consensus sequences for N-glycosylation.
Moreover, we show how defects in N-glycosylation will primarily affect cell adhesion.
Also, the results show that these differences are not explained by differential N-glycosylation patterns.
The loss of the N-glycosylation site alters the characteristics of the protein.
Such linkage can allow for easier purification following the N-glycosylation modifications.
