Difference between revisions of "Part:BBa K3468089:Experience"
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===Applications of BBa_K3468089=== | ===Applications of BBa_K3468089=== | ||
During Pymol visual examination, it was found that the mutation site was far away from the inside of the protein, which met the disulfide bond geometric standard, but destroyed the existing salt bridge (E44-K252). DDG is 0.663kcal/mol evaluated by FoldX. | During Pymol visual examination, it was found that the mutation site was far away from the inside of the protein, which met the disulfide bond geometric standard, but destroyed the existing salt bridge (E44-K252). DDG is 0.663kcal/mol evaluated by FoldX. | ||
| + | [[File:Fig5.png|400px|thumb|left|Fig.5 Structure feature of L43C and K252C]] | ||
| + | |||
===User Reviews=== | ===User Reviews=== | ||
<!-- DON'T DELETE --><partinfo>BBa_K3468089 StartReviews</partinfo> | <!-- DON'T DELETE --><partinfo>BBa_K3468089 StartReviews</partinfo> | ||
Revision as of 07:16, 25 October 2020
This experience page is provided so that any user may enter their experience using this part.
Please enter
how you used this part and how it worked out.
Applications of BBa_K3468089
During Pymol visual examination, it was found that the mutation site was far away from the inside of the protein, which met the disulfide bond geometric standard, but destroyed the existing salt bridge (E44-K252). DDG is 0.663kcal/mol evaluated by FoldX.
User Reviews
UNIQ514382c2efadc081-partinfo-00000000-QINU UNIQ514382c2efadc081-partinfo-00000001-QINU