Dynamic design: manipulation of millisecond timescale motions on the energy landscape of cyclophilin A
Proteins need to interconvert between many conformations in order to function, many of which are formed transiently, and sparsely populated. Particularly when the lifetimes of these states approach the millisecond timescale, identifying the relevant structures and the mechanism by which they interco...
Principais autores: | , , , , , , , , , , , |
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Formato: | Journal article |
Idioma: | English |
Publicado em: |
Royal Society of Chemistry
2020
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