Examples of 'glycosylation site' in a sentence
Meaning of "glycosylation site"
glycosylation site: In biochemistry, a glycosylation site refers to a specific location on a protein where a carbohydrate molecule can be attached. This process plays a crucial role in protein folding, stability, and function
How to use "glycosylation site" in a sentence
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glycosylation site
A putative glycosylation site has been described.
The double line indicates a putative glycosylation site.
A potential glycosylation site is italicized.
The combination of the two mutations creates a glycosylation site.
The glycosylation site was introduced during the process of humanization.
Removal of a glycosylation site.
Other candidates for substitution are residues creating a potential glycosylation site.
This is a potential glycosylation site and this residue can be mutated to a glutamine.
Suitable methods for removing or introduction of a glycosylation site are described above.
Glycosylation site Length Amino acid position of glycosylation site.
Preferably the humanized antibody comprises no more than one glycosylation site.
Most of SCR contain one possible glycosylation site and four cysteines.
The presence of either of these tripeptide sequences in a polypeptide creates a potential glycosylation site.
All three proteins contain a conserved potential glycosylation site in the eighth IRR domain.
Other framework residues that are candidates for substitution are residues creating a potential glycosylation site.
See also
In an example, the glycosylation site is added by shuffling polynucleotides.
Glycosylation of antibodies may also be modified or eliminated by mutation of glycosylation site sequences.
In an exemplary embodiment, the glycosylation site is added by shuffling polynucleotides.
Any other substitution at this site also destroys the glycosylation site.
Similar modifications at the glycosylation site at position 78 are also preferred.
Any other substitution at this site will also destroy the glycosylation site.
Alternatively, an existing glycosylation site can be mutated to preclude carbohydrate attachment.
Glycosylating the mutant human growth hormone at the newly introduced glycosylation site.
The glycosylation site can be altered by amino acid insertions, deletions and / or substitutions.
The isolated antibody or antibody fragment of the invention may additionally contain a glycosylation site.
The potential asparagine-linked glycosylation site is overlined.
The native glycosylation site in the protein is bold, the signal sequence underlined.
The FGF mutein has had introduced at least one glycosylation site.
Each glycosylation site probably contains several closely related, non-identical structures.
The DNA sequence defined by CHO encodes a glycosylation site.
More preferably, the glycosylation site is introduced into the framework regions of a variable region.
Such replacements can introduce a non-native glycosylation site.
As another example, a glycosylation site and altering a disulfide bond can be combined into a single variant.
In such a case, the carbonyl group may be located at a protein glycosylation site.
Example 13 sets forth additional multiple glycosylation site leptin proteins and in vitro biological activity data.
In a preferred embodiment of the invention, more than one additional glycosylation site is introduced.
A potential N-linked glycosylation site is double underlined.
Thus, preferably a scaffold protein according to the present invention has no glycosylation site.
In some embodiments, the dPEG is linked to a glycosylation site of the targeting molecule.
Thus, the presence of either of these peptide sequences in a polypeptide creates a potential glycosylation site.
A single potential N-linked glycosylation site is marked by an asterisk.
Thus, the presence of either of these tripeptide sequences in a glycoprotein creates a potential glycosylation site.
The N-linked glycosylation site is marked with a dot.
Thus, the presence of either of these tripeptide sequences in a polypeptide creates a potential glycosylation site.
The antibody may bind to a glycosylation site on CCRL2.
In both, the glycosylation site motif NYT was successfully modified.
The asterisk indicates the possible N-linked glycosylation site.
The introduced glycosylation site is in particular an in vivo N-glycosylation site.
A mucin domain comprises or alternatively consists of an O-linked glycosylation site.
The glycosylation site that is deleted can include an N-glycosylation site.
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Examples of using Glycosylation
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Further glycosylation of specific hydroxylysine residues occurs
Several methods of modulating glycosylation of proteins are known
Protein glycosylation may be analyzed in a number of ways
