Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding
- PMID: 8876184
- PMCID: PMC38106
- DOI: 10.1073/pnas.93.21.11615
Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding
Abstract
How fast can a protein fold? The rate of polypeptide collapse to a compact state sets an upper limit to the rate of folding. Collapse may in turn be limited by the rate of intrachain diffusion. To address this question, we have determined the rate at which two regions of an unfolded protein are brought into contact by diffusion. Our nanosecond-resolved spectroscopy shows that under strongly denaturing conditions, regions of unfolded cytochrome separated by approximately 50 residues diffuse together in 35-40 microseconds. This result leads to an estimate of approximately (1 microsecond)-1 as the upper limit for the rate of protein folding.
Comment on
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A speed limit for protein folding.Proc Natl Acad Sci U S A. 1996 Oct 15;93(21):11426-7. doi: 10.1073/pnas.93.21.11426. Proc Natl Acad Sci U S A. 1996. PMID: 8876151 Free PMC article. Review. No abstract available.
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