Anagram & Information om | Engelska ordet CYSTEINES

Exempel på hur man kan använda CYSTEINES i en mening

• The chemokines are characterized by the presence of 4 conserved cysteines that form 2 disulfide bonds.
• After washing, the hair is treated with a mild solution of hydrogen peroxide, which oxidizes the cysteines back to cystine.
• Substrate-binding strategies are similar to MetH, although in the case of MetE the zinc atom is instead coordinated to two cysteines, a histidine and a glutamate, for which an example is shown on the right.
• POFUT-1 responsible for adding fucose sugars in O linkage to serine or threonine residues between the second and third conserved cysteines in EGF-like repeats on the Notch protein.
• Rab27 is post translationally modified by the addition of two geranylgeranyl groups on the two C-terminal cysteines.
• However, since 2-mercaptoethanol forms adducts with free cysteines and is somewhat more toxic, dithiothreitol (DTT) is generally more used especially in SDS-PAGE.
• Class C methylase has homologous sequence with the RS enzyme, coproporphyrinogen III oxidase (HemN), which also catalyzes the methylation of sp2-hybridized carbon centers yet it lacks the 2 cysteines required for methylation in mechanism of Class A.
• The loops have functional sites, including two cysteines amino acids for a disulfide bridge, Asp-Arg-Tyr, which is responsible for association with arrestin and, Lys/Arg-Lys/Arg-X-X-Lys/Arg, which interacts with G-proteins.
• For example, the spacing of the characteristic N-terminal cysteines differs; there are three amino acids separating the initial pair of cysteines in CX3CL1, with none in CC chemokines and only one intervening amino acid in CXC chemokines.
• TCEP can keep the cysteines from forming di-sulfide bonds and, unlike dithiothreitol and β-mercaptoethanol, it will not react as readily with the maleimide.
• It is a 42-residue-long protein containing 11 basic residues (nine lysines, two arginines) and six cysteines.
• The loops have functional sites, including two cysteines for a disulfide bridge, Asp-Arg-Tyr, responsible for association with arrestin, and Lys/Arg-Lys/Arg-X-X-Lys/Arg, which interacts with G-proteins.
• When the thioredoxin is detected by the enzyme, the C-terminal tail moves over the active site and forms a closed position within the enzyme itself, allowing for the cysteines that are catalytically necessary to move in and make sufficient contact with the thioredoxin.
• The PTX3 carboxy-terminal domain contains a canonical pentraxin signature (HxCxS/TWxS) and two conserved cysteines (Cys-210 and Cys-271), and shares 57% conserved and 17% identical amino acids with short pentraxins.
• Chemokines are divided into 2 major subfamilies, CXC and CC, based on the arrangement of the first 2 of the 4 conserved cysteine residues; the 2 cysteines are separated by a single amino acid in CXC chemokines and are adjacent in CC chemokines.
• The N-terminal Broad complex, Tramtrack and Bric-à-Brac (BTB) domain contains the Cys151 residue, which is one of the important cysteines in stress sensing.
• KLF13 belongs to a family of transcription factors that contain 3 classical zinc finger DNA-binding domains consisting of a zinc atom tetrahedrally coordinated by 2 cysteines and 2 histidines (C2H2 motif).
• N-terminal cysteines of MAP6 domain-containing protein 1 (MAP6d1), a postnatally expressed isoform in the mouse central nervous system, are palmitoylated by DHHC-type palmitoylating enzymes.
• The staining and destaining of gels is often followed by the reduction and alkylation (r&a) of the cystines or cysteines in the proteins.
• In acidic solution, the sulfenic acid is isolated before reaction with one or more cysteines accessible from the luminar surface of the enzyme, a tetracyclic sulfenamide.

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