1YYX
The solution structure of a redesigned apocytochrome B562 (Rd-apocyt b562) at 2.8M urea
Summary for 1YYX
| Entry DOI | 10.2210/pdb1yyx/pdb |
| Related | 1RAC 1YYJ |
| NMR Information | BMRB: 6560 |
| Descriptor | Redesigned apo-cytochrome b562 (1 entity in total) |
| Functional Keywords | rd-apocyt b562, intermediates, hydrophobic interactions, structural genomics, psi, protein structure initiative, berkeley structural genomics center, bsgc, de novo protein |
| Total number of polymer chains | 1 |
| Total formula weight | 11729.12 |
| Authors | Feng, H.,Vu, N.,Bai, Y.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2005-02-25, release date: 2005-08-25, Last modification date: 2024-05-29) |
| Primary citation | Feng, H.,Vu, N.,Bai, Y. Detection and structure determination of an equilibrium unfolding intermediates of Rd-apocytochrome b562: native fold with non-native hydrophobic interactions J.Mol.Biol., 343:1477-1485, 2004 Cited by PubMed Abstract: The absence of detectable kinetic and equilibrium folding intermediates by optical probes is commonly taken to indicate that protein folding is a two-state process. However, for some small proteins with apparent two-state behavior, unfolding intermediates have been identified in native-state hydrogen exchange or kinetic unfolding experiments monitored by nuclear magnetic resonance. Rd-apocytochrome b(562), a four-helix bundle, is one such protein. Here, we found another unfolding intermediate for Rd-apocytochrome b(562). It is based on a cooperative transition of (15)N chemical shifts of amide protons as a function of urea concentrations before the global unfolding. We have solved the high-resolution structure of the protein at 2.8 M urea, which is after this cooperative transition but before the global unfolding. All four helices remained intact, but a number of hydrophobic core residues repacked. This intermediate provides a possible structural interpretation for the kinetic unfolding intermediates observed using nuclear magnetic resonance methods for several proteins and has important implications for theoretical studies of protein folding. PubMed: 15491625DOI: 10.1016/j.jmb.2004.08.099 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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