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Structure of the Hydrophobic Core Determines the 3D Protein Structure—Verification by Single Mutation Proteins
Four de novo proteins differing in single mutation positions, with a chain length of 56 amino acids, represent diverse 3D structures: monomeric 3α and 4β + α folds. The reason for this diversity is seen in the different structure of the hydrophobic core as a result of synergy leading to the generati...
Tallennettuna:
| Julkaisussa: | Biomolecules |
|---|---|
| Päätekijät: | , , , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
MDPI
2020
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7281683/ https://ncbi.nlm.nih.gov/pubmed/32423068 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.3390/biom10050767 |
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