Cavity as a Source of Conformational Fluctuation and High-Energy State: High-Pressure NMR Study of a Cavity-Enlarged Mutant of T4Lysozyme

Although the structure, function, conformational dynamics, and controlled thermodynamics of proteins are manifested by their corresponding amino acid sequences, the natural rules for molecular design and their corresponding interplay remain obscure. In this study, we focused on the role of internal...

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Библиографические подробности
Опубликовано в: :Biophys J
Главные авторы: Maeno, Akihiro, Sindhikara, Daniel, Hirata, Fumio, Otten, Renee, Dahlquist, Frederick W., Yokoyama, Shigeyuki, Akasaka, Kazuyuki, Mulder, Frans A.A., Kitahara, Ryo
Формат: Artigo
Язык:Inglês
Опубликовано: The Biophysical Society 2015
Предметы:
Proteins and Nucleic Acids
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC4286597/
https://ncbi.nlm.nih.gov/pubmed/25564860
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpj.2014.11.012
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