Examples of 'cysteines' in a sentence
Meaning of "cysteines"
cysteine (noun) - an amino acid that is important for protein synthesis and the overall functioning of the body, commonly found in many foods like poultry, eggs, and dairy products
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- plural of cysteine
How to use "cysteines" in a sentence
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cysteines
Four conserved cysteines are involved in disulfide bonds.
The domain usually contains six conserved cysteines.
Two crosslinked cysteines form a cystine molecule.
Cysteines can be placed anywhere within the target.
As a common feature no cysteines residues are present in this channel.
Mutagenic oligonucleotides are used to mutate single pairs of cysteines.
Positions of cysteines are indicated with black dots.
Subdomains between the conserved cysteines vary in length.
The conserved cysteines are also indicated by asterisks.
The codons encoding the mutated cysteines are highlighted.
The two cysteines are introduced by amino acid substitution.
Most suitably all three reactive groups are cysteines.
It is assumed that all cysteines are engaged in disulfide bonds.
Asterisks indicate positions of conserved cysteines.
These cysteines may generate interchain disulphide bonds.
See also
No glycosylation sites or unpaired cysteines were found in the humanized sequences.
Such cysteines are preferably located in a dimerization domain of a monomer.
Another characteristic is that two cysteines are present as sandwiching tryptophan.
Only cysteines perfectly conserved within each consensus are reported.
Vasopressin is a nonapeptide with a disulphide bridge between two cysteines.
All of the cysteines are likely be to involved in disulfide bonding.
Glycosylation sites are boxed and the preserved cysteines are underlined.
N is the number of cysteines present in the protein molecule.
Cysteines can be engineered into these positions by known techniques.
Eotaxin has four cysteines forming two disulfide bridges.
Cysteines are depicted by black boxes.
The reference is focused on cysteines involved in intramolecular disulfide bonds.
Cysteines are shown in bold letters.
Peptides can introduce the thiol function by incorporation of cysteines.
The introduced cysteines are shown in bold and underlined.
The asterisks mark the first two conserved cysteines.
Conserved cysteines are indicated by bold lettering.
Each motif contains four to six cysteines in conserved positions.
Native cysteines were replaced by alanines.
Only one of these clones contain two or more cysteines.
The cysteines remain protected.
Sulfonation was used to provide protecting groups for the cysteines.
It contains five cysteines which are not involved in disulfide bonds.
Terns for their cysteines.
The cysteines are also highlighted.
It is probable that disulphide bridges between cysteines are involved in a correct conformation.
The two cysteines are selectively deprotected before addition of the maleimide.
Typically these occupy all the cysteines present in the molecule.
Cysteines were assigned to the positions where no specific amino acid was identified.
Are highlighted by adjacent cysteines looping out the intervening sequence regions.
Cysteines are highlighted red.
This calculation assumes that all cysteines pair into cystines.
The conserved cysteines are marked with asterisks under the alignment.
The zinc ion is chelated by one histidine and three cysteines.
Reversibly blocked cysteines in a protein may be converted to irreversibly blocked cysteines.
