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| [[Image:1mqv.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1mqv| PDB=1mqv | SCENE= }} | | {{STRUCTURE_1mqv| PDB=1mqv | SCENE= }} |
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| '''Crystal Structure of the Q1A/F32W/W72F mutant of Rhodopseudomonas palustris cytochrome c' (prime) expressed in E. coli'''
| | ===Crystal Structure of the Q1A/F32W/W72F mutant of Rhodopseudomonas palustris cytochrome c' (prime) expressed in E. coli=== |
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| ==Overview==
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| We employed fluorescence energy-transfer probes to investigate the polypeptide dynamics accompanying cytochrome c' folding. Analysis of fluorescence energy-transfer kinetics from wild-type Trp-72 or Trp-32 in a crystallographically characterized (1.78 A) Q1A/F32W/W72F mutant shows that there is structural heterogeneity in denatured cytochrome c'. Even at guanidine hydrochloride concentrations well beyond the unfolding transition, a substantial fraction of the polypeptides ( approximately 50%) adopts compact conformations (tryptophan-to-heme distance, approximately 25 A) in both pseudo-wild-type (Q1A) and mutant proteins. A burst phase (< or =5 ms) is revealed when stopped flow-triggered refolding is probed by tryptophan intensity: measurements on the Q1A protein show that approximately 75% of the Trp-72 fluorescence (83% for Trp-32) is quenched within the mixing deadtime, suggesting that most of the polypeptides have collapsed.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12407175}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12407175 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12407175}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Winkler, J R.]] | | [[Category: Winkler, J R.]] |
| [[Category: Four-helix bundle]] | | [[Category: Four-helix bundle]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:36:44 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:33:37 2008'' |