Computational Design of Four-Helix Bundle Proteins That Bind Nonbiological Cofactors
β Scribed by Andreas Lehmann; Jeffery G. Saven
- Book ID
- 109387676
- Publisher
- American Institute of Chemical Engineers
- Year
- 2008
- Tongue
- English
- Weight
- 171 KB
- Volume
- 24
- Category
- Article
- ISSN
- 8756-7938
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## Abstract The introduction of disulfide crosslinks is a generally useful method by which to identify regions of a protein that are close together in space. Here we describe the use of disulfide crosslinks to investigate the structure and flexibility of a family of designed 4βhelix bundle proteins
## Abstract Fourβ, fiveβ, and sixβhelix bundle template assembled synthetic proteins (TASPs) have been synthesized using disulfide bonds between cavitand templates and peptides, and characterized in terms of stability and structural specificity. The peptide sequence (CGGGEELLKKLEE LLKKG) used was o