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Literature DB >> 8876184

Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding.

S J Hagen¹, J Hofrichter, A Szabo, W A Eaton.

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.

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Year: 1996 PMID： 8876184 PMCID： PMC38106 DOI： 10.1073/pnas.93.21.11615

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

31 in total

1. Theoretical predictions of folding pathways by using the proximity rule, with applications to bovine pancreatic trypsin inhibitor.

Authors: C J Camacho; D Thirumalai
Journal: Proc Natl Acad Sci U S A Date: 1995-02-28 Impact factor: 11.205

Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding.

1. Theoretical predictions of folding pathways by using the proximity rule, with applications to bovine pancreatic trypsin inhibitor.

2. Direct observation of fast protein folding: the initial collapse of apomyoglobin.

3. Extremely rapid protein folding in the absence of intermediates.

4. Submillisecond folding of monomeric lambda repressor.

5. Ultrafast thermally induced unfolding of RNase A.

6. Folding of a four-helix bundle: studies of acyl-coenzyme A binding protein.

7. Funnels, pathways, and the energy landscape of protein folding: a synthesis.

8. Fast folding of a prototypic polypeptide: the immunoglobulin binding domain of streptococcal protein G.

9. The barriers in protein folding.

Review 10. Ligand binding and conformational changes measured by time-resolved absorption spectroscopy.

1. The speed limit for protein folding measured by triplet-triplet energy transfer.

2. Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering.

3. Cytochrome c folds through a smooth funnel.

4. Investigation of routes and funnels in protein folding by free energy functional methods.

5. The topomer-sampling model of protein folding.

6. Multiple pathways on a protein-folding energy landscape: kinetic evidence.

7. Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation.

Review 8. From discrete protein kinetics to continuous Brownian dynamics: a new perspective.

9. How the folding rate constant of simple, single-domain proteins depends on the number of native contacts.

Review 10. Searching for "downhill scenarios" in protein folding.