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| [[Image:1lfm.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1lfm| PDB=1lfm | SCENE= }} | | {{STRUCTURE_1lfm| PDB=1lfm | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF COBALT(III)-SUBSTITUTED CYTOCHROME C (TUNA)'''
| | ===CRYSTAL STRUCTURE OF COBALT(III)-SUBSTITUTED CYTOCHROME C (TUNA)=== |
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| ==Overview==
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| Replacement of iron with cobalt(III) selectively introduces a deep trap in the folding-energy landscape of the heme protein cytochrome c. Remarkably, neither the protein structure nor the folding thermodynamics is perturbed by this metal-ion substitution, as shown by data from spectroscopic and x-ray diffraction experiments. Through kinetics measurements, we have found parallel folding pathways involving several different misligated Co(III) species, and, as these folding intermediates persist for several hours under certain conditions, we have been able to elucidate fully their spectroscopic properties. The results, along with an analysis of the fluorescence energy-transfer kinetics during refolding, show that rapidly equilibrating populations of compact and extended polypeptide conformations are present until all molecules have reached the native structure. These measurements provide direct evidence that collapsed denatured structures are not substantially more stable than extended conformations of cytochrome c.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12084923}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12084923 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12084923}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Folding]] | | [[Category: Folding]] |
| [[Category: Intermediate]] | | [[Category: Intermediate]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:52:35 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 20:24:02 2008'' |
