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Sequence, structure, and cooperativity in folding of elementary protein structural motifs
Residue-level unfolding of two helix-turn-helix proteins—one naturally occurring and one de novo designed—is reconstructed from multiple sets of site-specific (13)C isotopically edited infrared (IR) and circular dichroism (CD) data using Ising-like statistical-mechanical models. Several model varian...
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| 出版年: | Proc Natl Acad Sci U S A |
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| 主要な著者: | , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
National Academy of Sciences
2015
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4538684/ https://ncbi.nlm.nih.gov/pubmed/26216963 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1506309112 |
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