「cysteines」の共起表現一覧(1語右で並び替え)
該当件数 : 25件
ce 2-mercaptoethanol forms adducts with free | cysteines and is somewhat more toxic, dithiothreitol ( |
of replacing the nitrosyl from the modified | cysteines and thus can serve in research of the redox |
ntributions include conversion of serines to | cysteines, and involvement with energy transfer studie |
stabilized by interactions between conserved | cysteines and other charged amino acids. |
nds of these metal ions are probably the six | cysteines and two histidines that are conserved in thi |
Two of these | cysteines are clustered in the C-terminal section of t |
f TGF-beta-2, it is known that all the other | cysteines are involved in intrachain disulfide bonds. |
protein, merely their location (i.e., which | cysteines are bonded). |
The side chains of the four disulfide-bonded | cysteines are shown in yellow, with their sulfur atoms |
N-terminal cysteine as well as the internal | cysteines are able to form the thioester, but only the |
yclized through a disulfide bond between two | cysteines, as in somatostatin and oxytocin. |
ion of hydrogen peroxide, which oxidizes the | cysteines back to cystine. |
TCEP can keep the | cysteines from forming di-sulfide bonds and unlike dit |
The absence of | cysteines in the scaffold enables engineering of site- |
, Rabs are anchored via prenyl groups on two | cysteines in the C-terminus. |
iplasmic protein DsbA which in turn oxidizes | cysteines in other periplasmic proteins in order to ma |
idues between the second and third conserved | cysteines in EGF-like repeats on the Notch protein. |
The two | cysteines in the first periplasmic domain are in a Cys |
forty residues long, contains four conserved | cysteines involved in disulfide bonds and is part of t |
It is suspected that the | cysteines of individual or separate claudins form disu |
This domain contains ten conserved | cysteines that form five disulphide bridges. |
well conserved and includes three conserved | cysteines that coordinate the zinc ion. |
cally localized protein with highly reactive | cysteines that respond quickly to changes in the redox |
from both domains and contains two conserved | cysteines thought to function as the acid and base in |
served cysteine residues instead of the four | cysteines typical to chemokines), exodus-2, and second |
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