ライフサイエンスコーパス: half-cystine

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1 fe, evidence suggests that it is a vestigial half-cystine.

2 imers, just like the single mutants at these half-cystines.

3 rs resides in only 90 residues, including 11 half-cystines.

4 cystines are covalently bound to which other half-cystines.

5 xpressed primarily monomers, suggesting that half-cystine 1199 in the D3-domain is involved in formin

6 hose with unmutated plasmid, suggesting that half-cystine 1276 is not involved in formation of disulf

7 By site-directed mutagenesis, the codon for half-cystine 95 in norrin was changed to one encoding al

8 tant was the size of dimers, indicating that half-cystine 95 is involved in oligomer formation.

9 structure preferences of free cysteines and half-cystines, and by promising preliminary results we o

10 architecture neural network to predict which half-cystines are covalently bound to which other half-c

11 al mutant vectors encoding serine instead of half-cystine at residues 13244 and 13246 in submaxillary

12 lanking regions of N-terminus and C-terminus half-cystines augmented with residue secondary structure

13 Since all 22 half-cystines can be modified with iodoacetamide without

14 Two of these half-cystines, Cys13244 and Cys13246, are in the highly

15 cysteine in 16 members and participates as a half-cystine in at least 3 (and perhaps as many as 6) ot

16 Support for the involvement of these half-cystines in formation of disulfide-bonded dimers of

17 The roles of the half-cystines in the CGLCG motifs in the assembly of dis

18 Cells with plasmids in which both half-cystines in the motif in the D1- or D3-domain of mu

19 teine is reduced (free in sulfhydryl state), half-cystine (involved in a disulfide bond) or bound to

20 Cys111 is the invariable third half-cystine of the second complement control protein mo

21 wo cysteines (Cys-158 and Cys-311) of eleven half-cystines of the N-terminal chromophore binding doma

22 While a structural role as a half-cystine provides a stability basis for possible sel

23 The corresponding half-cystine residue in human prepro-von Willebrand fact

24 These results suggest that three half-cystine residues (Cys13223, Cys13244, and Cys13246)

25 f-cystine residues in norrin and part of the half-cystine residues in a disulfide-rich domain of von

26 consistent with the sequence identity of the half-cystine residues in norrin and part of the half-cys

27 utagenesis to assess the roles of individual half-cystine residues in the assembly of disulfide-linke

28 Two half-cystine residues of one center (Cys345Cys348) align

29 Of the eight half-cystine residues that are conserved in mammalian J

30 etween Cys345 and Cys348; the two C-terminal half-cystine residues, Cys476 and Cys489, exist as free

31 change, one at a time, each codon for the 11 half-cystines to serine.

32 on Ala66, which is known to participate as a half-cystine with position 83 in FGF-8, FGF-19, and FGF-

33 zed by selective replacement of each pair of half-cystines with two alpha-amino-butyrate (Abu) residu

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