ENGINEERING A UNIQUELY REACTIVE THIOL INTO A CYSTEINE-RICH PEPTIDE
被引:23
作者:
SHIMONY, E
论文数: 0引用数: 0
h-index: 0
机构:Howard Hughes Medical Institute, Graduate Department of Biochemistry, Brandeis University, Waltham, MA
SHIMONY, E
SUN, TY
论文数: 0引用数: 0
h-index: 0
机构:Howard Hughes Medical Institute, Graduate Department of Biochemistry, Brandeis University, Waltham, MA
SUN, TY
KOLMAKOVAPARTENSKY, L
论文数: 0引用数: 0
h-index: 0
机构:Howard Hughes Medical Institute, Graduate Department of Biochemistry, Brandeis University, Waltham, MA
KOLMAKOVAPARTENSKY, L
MILLER, C
论文数: 0引用数: 0
h-index: 0
机构:Howard Hughes Medical Institute, Graduate Department of Biochemistry, Brandeis University, Waltham, MA
MILLER, C
机构:
[1] Howard Hughes Medical Institute, Graduate Department of Biochemistry, Brandeis University, Waltham, MA
来源:
PROTEIN ENGINEERING
|
1994年
/
7卷
/
04期
关键词:
CHARYBDOTOXIN;
LABELING;
POTASSIUM CHANNEL;
D O I:
10.1093/protein/7.4.503
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
Cysteine mutagenesis for the purpose of chemical labelling was applied to the K+ channel neurotoxin charybdotoxin, a 37-residue peptide with six functionally essential cysteines. An additional 'spinster cysteine' was introduced at a position far away in space from the toxin's known interaction surface where it contacts its K+ channel receptor. Despite the presence of the extra unpaired cysteine residue, the toxin still folds efficiently and may be labelled by fluorescent and radioactive reagents to give a functionally competent toxin.