Ontology highlight
ABSTRACT:
SUBMITTER: Uzawa T
PROVIDER: S-EPMC337025 | biostudies-literature | 2004 Feb
REPOSITORIES: biostudies-literature
Uzawa Takanori T Akiyama Shuji S Kimura Tetsunari T Takahashi Satoshi S Ishimori Koichiro K Morishima Isao I Fujisawa Tetsuro T
Proceedings of the National Academy of Sciences of the United States of America 20040107 5
The characterization of protein folding dynamics in terms of secondary and tertiary structures is important in elucidating the features of intraprotein interactions that lead to specific folded structures. Apomyoglobin (apoMb), possessing seven helices termed A-E, G, and H in the native state, has a folding intermediate composed of the A, G, and H helices, whose formation in the submillisecond time domain has not been clearly characterized. In this study, we used a rapid-mixing device combined w ...[more]