pH-Jump Induced Leucine Zipper Folding beyond the Diffusion Limit

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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

@article{Donten2015pH-Ju-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:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/30859"> <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:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2015-05-04T08:45:37Z</dc:date> <dc:contributor>Hassan, Shabir</dc:contributor> <dc:contributor>Hamm, Peter</dc:contributor> <dc:creator>Popp, Alexander</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2015-05-04T08:45:37Z</dcterms:available> <dcterms:title>pH-Jump Induced Leucine Zipper Folding beyond the Diffusion Limit</dcterms:title> <dc:creator>Hauser, Karin</dc:creator> <dc:creator>Donten, Mateusz L.</dc:creator> <dc:creator>Hassan, Shabir</dc:creator> <dc:creator>Hamm, Peter</dc:creator> <dc:language>eng</dc:language> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/30859"/> <dc:contributor>Donten, Mateusz L.</dc:contributor> <dc:contributor>Hauser, Karin</dc:contributor> <dcterms:issued>2015</dcterms:issued> </rdf:Description> </rdf:RDF>

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