pH-Jump Induced Leucine Zipper Folding beyond the Diffusion Limit

Cite This

Files in this item

Files Size Format View

There are no files associated with this item.

DONTEN, Mateusz L., Shabir HASSAN, Alexander POPP, Jonathan HALTER, Karin HAUSER, Peter HAMM, 2015. pH-Jump Induced Leucine Zipper Folding beyond the Diffusion Limit. In: The Journal of Physical Chemistry B. 119(4), pp. 1425-1432. ISSN 1520-6106. eISSN 1520-5207. Available under: doi: 10.1021/jp511539c

@article{Donten2015pHJum-30859, title={pH-Jump Induced Leucine Zipper Folding beyond the Diffusion Limit}, year={2015}, doi={10.1021/jp511539c}, number={4}, volume={119}, issn={1520-6106}, journal={The Journal of Physical Chemistry B}, pages={1425--1432}, author={Donten, Mateusz L. and Hassan, Shabir and Popp, Alexander and Halter, Jonathan and Hauser, Karin and Hamm, Peter} }

<rdf:RDF xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <dc:contributor>Halter, Jonathan</dc:contributor> <dcterms:abstract xml:lang="eng">The folding of a pH-sensitive leucine zipper, that is, a GCN4 mutant containing eight glutamic acid residues, has been investigated. A pH-jump induced by a caged proton (o-nitrobenzaldehyde, oNBA) is employed to initiate the process, and time-resolved IR spectroscopy of the amide I band is used to probe it. The experiment has been carefully designed to minimize the buffer capacity of the sample solution so that a large pH jump can be achieved, leading to a transition from a completely unfolded to a completely folded state with a single laser shot. In order to eliminate the otherwise rate-limiting diffusion-controlled step of the association of two peptides, they have been covalently linked. The results for the folding kinetics of the cross-linked peptide are compared with those of an unlinked peptide, which reveals a detailed picture of the folding mechanism. That is, folding occurs in two steps, one on an ∼1-2 μs time scale leading to a partially folded α-helix even in the monomeric case and a second one leading to the final coiled-coil structure on distinctively different time scales of ∼30 μs for the cross-linked peptide and ∼200 μs for the unlinked peptide. By varying the initial pH, it is found that the folding mechanism is consistent with a thermodynamic two-state model, despite the fact that a transient intermediate is observed in the kinetic experiment.</dcterms:abstract> <dc:creator>Halter, Jonathan</dc:creator> <dc:contributor>Popp, Alexander</dc:contributor> <dc:contributor>Hassan, Shabir</dc:contributor> <dc:date rdf:datatype="">2015-05-04T08:45:37Z</dc:date> <dc:contributor>Hamm, Peter</dc:contributor> <dc:creator>Popp, Alexander</dc:creator> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dcterms:available rdf:datatype="">2015-05-04T08:45:37Z</dcterms:available> <dcterms:title>pH-Jump Induced Leucine Zipper Folding beyond the Diffusion Limit</dcterms:title> <dc:creator>Donten, Mateusz L.</dc:creator> <dc:creator>Hauser, Karin</dc:creator> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:creator>Hassan, Shabir</dc:creator> <dc:creator>Hamm, Peter</dc:creator> <dc:language>eng</dc:language> <dc:contributor>Donten, Mateusz L.</dc:contributor> <bibo:uri rdf:resource=""/> <dspace:isPartOfCollection rdf:resource=""/> <dc:contributor>Hauser, Karin</dc:contributor> <dcterms:issued>2015</dcterms:issued> <dcterms:isPartOf rdf:resource=""/> </rdf:Description> </rdf:RDF>

This item appears in the following Collection(s)

Search KOPS


My Account