期刊
PROTEIN SCIENCE
卷 11, 期 9, 页码 2179-2183出版社
COLD SPRING HARBOR LAB PRESS
DOI: 10.1110/ps.0212702
关键词
AFM; titin; polyprotein; mutant; linker; force
资金
- Wellcome Trust Funding Source: Medline
This manuscript introduces a versatile system for construction of multimeric proteins to be used as substrates for atomic force microscopy. The construction makes use of a cassette system that allows modules to be cut and ligated in any combination in eight different positions. The modules can be sequenced in situ after construction. A three-module fragment can be produced that is of a size amenable to structural and biophysical analysis to check the effect of placing a protein into a multimeric construct. We show that if the parent titin modules are retained in a construct, they can act both as linkers and as an internal standard for the force measurements. Proteins that cannot be expressed solubly in an eight-module homopolymer have been expressed and subject to force measurements using this system.
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