1BLV
SOLUTION STRUCTURE OF OXIDIZED RAT MICROSOMAL CYTOCHROME B5 IN THE PRESENCE OF 2 M GUANIDINIUM CHLORIDE: MONITORING THE EARLY STEPS IN PROTEIN UNFOLDING
Summary for 1BLV
| Entry DOI | 10.2210/pdb1blv/pdb |
| Descriptor | PROTEIN (CYTOCHROME B5), PROTOPORPHYRIN IX CONTAINING FE (2 entities in total) |
| Functional Keywords | protein unfolding, nmr solution structure, cytochrome b5, electron transport |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side: P00173 |
| Total number of polymer chains | 1 |
| Total formula weight | 11430.39 |
| Authors | Arnesano, F.,Banci, L.,Bertini, I.,Koulougliotis, D. (deposition date: 1998-07-21, release date: 1998-07-29, Last modification date: 2024-05-22) |
| Primary citation | Arnesano, F.,Banci, L.,Bertini, I.,Koulougliotis, D. Solution structure of oxidized rat microsomal cytochrome b5 in the presence of 2 M guanidinium chloride: monitoring the early steps in protein unfolding. Biochemistry, 37:17082-17092, 1998 Cited by PubMed Abstract: One- and two-dimensional proton NMR spectroscopy has been employed in order to study the denaturation effect of guanidinium chloride (GdmCl) on the oxidized state of the A-form of rat microsomal cytochrome b5 (cyt b5). The protein rapidly starts losing the heme at denaturant concentrations larger than approximately 2.0 M and a largely unfolded protein is eventually obtained. An estimate of the unfolding kinetics is obtained and, by use of a two-state model (folded left and right arrow unfolded), a value for DeltaG degrees. Below this concentration, small (PubMed: 9836603 DOI: 10.1021/bi981546p PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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