Examples of 'cys' in a sentence
Meaning of "cys"
Cys (verb) - To move swiftly and gracefully, like a cat stealthily navigating its way through terrain
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- plural of CY
How to use "cys" in a sentence
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cys
Cys can form disulfide bridges.
The genes required for the synthesis of cysteine are coded for on the cys regulon.
Cys residues can not be identified by protein microsequencing.
This is the only possibility of encoding Cys.
Cys can form a disulfide bridge.
Disulfide linkages connecting a pair of Cys are shown by lines.
Cys participates in formation of disulfide bonds.
The positions of the four Cys residues are shown.
Cys in place of cysteinyl.
This generated free Cys residues in half of the molecules.
Cys residues were included in the linear peptides to enable their cyclization.
A chemically reactive handle is preserved by inclusion of a protected Cys residue.
Cys is the amino acid cysteine in its three letter code.
This treatment removes the protecting group from Cys.
Cys may be present in the peptide as a disulfide in the form of cystine.
See also
Further preferred is a binding domain devoid of a free Cys residue.
Maleimide Cys labeling or unnatural amino acids.
It is almost always preceded by a Cys.
The conserved Cys residues are enclosed in yellow boxes.
The substitution of at least one of the Cys residues by a Ser residue.
The two Cys residues are joined by a disulfide bond.
The protection of at least one of the Cys residues by an acetamidomethyl group.
Several Cys residues have been identified as being sensitive to redox changes.
The sulfur atoms of each Cys residue forms a disulfide bridge.
A free Cys residue is not involved in the formation of a disulfide bond.
The substitution of at least one of the Cys residues by an Ala residue.
Four of the six Cys residues in spHAS are conserved with seHAs.
A preferred label is oregon green that may be attached to a Cys residue.
The two Cys residues are joined by a disulfide bond in the active compounds.
Even more preferred is a binding domain free of any Cys residue.
The Cys residues were used to assist in coupling to a protein carrier as described below.
The next peak of similar area is the free Cys moiety.
The substitution of at least one of the Cys residues by a gamma aminobutyric acid residue.
Further preferred is a binding protein or binding domain devoid of a free Cys residue.
Four His and Cys residues are used to bind a metal ion in a tetrahedral geometry.
Even more preferred is a binding protein or binding domain free of any Cys residue.
Disulfide bonds between Cys residues can be formed using dimethyl sulfoxide Tam et al.
The two regions of similarity are centered around a Cys and two His residues.
Even free internal Cys residues may be present in either of the reacting segments.
Chimeras with other conotoxins may include additional Cys residues and additional disulphide bonds.
This may be an essential Cys whose modification by sulfhydryl poisons partially inhibits enzyme activity.
The term octreotide derivatives includes those including the moiety having a bridge between the Cys residues.
There are numerous ways to modify Hcy and Cys to make them immunologically distinct.
Such Cys residues are spaced apart from each other by a number of intermittent amino acids.
The residues that can be changed to Cys for preferred interchain disulfide bonds are boxed.
The Cys residues are bold and underlined and the predicted transmembrane region is boxed.
Preferably cyclic conotoxin peptides will retain the Cys residues and characteristic disulphide bonding pattern.
Cys indicates the identification of the PTH derivative of carboxymethyl cysteine in the alkylated protein.
The residues separating the second Cys and the first His are mainly polar and basic.
Cys and Trp not reported.
