Hamed Kooshapur

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NMR Analysis of Apo Glutamine‐Binding Protein Exposes Challenges in the Study of Interdomain Dynamics

Hamed Kooshapur, Junhe Ma, Nico Tjandra, Guillermo A. Bermejo

Angewandte Chemie International Edition > 58 > 47 > 16899 - 16902

Glutamine‐binding protein (GlnBP) displays an apo, “open” and a holo, “closed” crystal form, mutually related by a rigid‐body reorientation of its domains. A fundamental question about such large‐scale conformational transitions, whether the closed state exists in the absence of ligand, is controversial in the case of GlnBP. NMR observations have indicated no evidence of the closed form, whereas experimentally...

article

NMR Analysis of Apo Glutamine‐Binding Protein Exposes Challenges in the Study of Interdomain Dynamics

Hamed Kooshapur, Junhe Ma, Nico Tjandra, Guillermo A. Bermejo

Angewandte Chemie > 131 > 47 > 17055 - 17058

Glutamine‐binding protein (GlnBP) displays an apo, “open” and a holo, “closed” crystal form, mutually related by a rigid‐body reorientation of its domains. A fundamental question about such large‐scale conformational transitions, whether the closed state exists in the absence of ligand, is controversial in the case of GlnBP. NMR observations have indicated no evidence of the closed form, whereas experimentally...

article

Conformational Ensemble of Disordered Proteins Probed by Solvent Paramagnetic Relaxation Enhancement (sPRE)

Hamed Kooshapur, Charles D. Schwieters, Nico Tjandra

Angewandte Chemie International Edition > 57 > 41 > 13519 - 13522

Characterization of the conformational ensemble of disordered proteins is highly important for understanding protein folding and aggregation mechanisms, but remains a computational and experimental challenge owing to the dynamic nature of these proteins. New observables that can provide unique insights into transient residual structures in disordered proteins are needed. Here using denatured ubiquitin...

article

Conformational Ensemble of Disordered Proteins Probed by Solvent Paramagnetic Relaxation Enhancement (sPRE)

Hamed Kooshapur, Charles D. Schwieters, Nico Tjandra

Angewandte Chemie > 130 > 41 > 13707 - 13710

Characterization of the conformational ensemble of disordered proteins is highly important for understanding protein folding and aggregation mechanisms, but remains a computational and experimental challenge owing to the dynamic nature of these proteins. New observables that can provide unique insights into transient residual structures in disordered proteins are needed. Here using denatured ubiquitin...

article

Efficient Detection of Hydrogen Bonds in Dynamic Regions of RNA by Sensitivity‐Optimized NMR Pulse Sequences

Andre Dallmann, Bernd Simon, Malgorzata M. Duszczyk, Hamed Kooshapur, more

Angewandte Chemie > 125 > 40 > 10681 - 10684

Verbesserte Empfindlichkeit: Mit effizienten NMR‐Experimenten, die auf der J‐Kopplung entlang von Wasserstoffbrücken basieren, wird die Sekundärstruktur von großen und dynamischen RNA‐Molekülen bestimmt (siehe Bild). Die Experimente liefern eine bis zu 8fach verbesserte Empfindlichkeit und ermöglichen so die Detektion von Basenpaaren in den dynamischen Bereichen großer RNA‐Moleküle.

article

Efficient Detection of Hydrogen Bonds in Dynamic Regions of RNA by Sensitivity‐Optimized NMR Pulse Sequences

Andre Dallmann, Bernd Simon, Malgorzata M. Duszczyk, Hamed Kooshapur, more

Angewandte Chemie International Edition > 52 > 40 > 10487 - 10490

Improved Sensitivity: Efficient NMR experiments are presented for determining the secondary structure in large and dynamic RNAs using J‐couplings across hydrogen bonds (see picture). The experiments provide up to eight‐fold improved sensitivity and thus enable detection of base pairs in dynamic regions even in large RNAs.

article

hnRNP A1 Proofreads 3′ Splice Site Recognition by U2AF

Joao Paulo Tavanez, Tobias Madl, Hamed Kooshapur, Michael Sattler, more

Molecular Cell > 2012 > 45 > 3 > 314-329

One of the earliest steps in metazoan pre-mRNA splicing involves binding of U2 snRNP auxiliary factor (U2AF) 65 KDa subunit to the polypyrimidine (Py) tract and of the 35 KDa subunit to the invariant AG dinucleotide at the intron 3′ end. Here we use in vitro and in vivo depletion, as well as reconstitution assays using purified components, to identify hnRNP A1 as an RNA binding protein that allows...

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Search results for: Hamed Kooshapur

NMR Analysis of Apo Glutamine‐Binding Protein Exposes Challenges in the Study of Interdomain Dynamics

NMR Analysis of Apo Glutamine‐Binding Protein Exposes Challenges in the Study of Interdomain Dynamics

Conformational Ensemble of Disordered Proteins Probed by Solvent Paramagnetic Relaxation Enhancement (sPRE)

Conformational Ensemble of Disordered Proteins Probed by Solvent Paramagnetic Relaxation Enhancement (sPRE)

Efficient Detection of Hydrogen Bonds in Dynamic Regions of RNA by Sensitivity‐Optimized NMR Pulse Sequences

Efficient Detection of Hydrogen Bonds in Dynamic Regions of RNA by Sensitivity‐Optimized NMR Pulse Sequences

hnRNP A1 Proofreads 3′ Splice Site Recognition by U2AF

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INFONA - science communication portal

Search results for: Hamed Kooshapur

NMR Analysis of Apo Glutamine‐Binding Protein Exposes Challenges in the Study of Interdomain Dynamics

NMR Analysis of Apo Glutamine‐Binding Protein Exposes Challenges in the Study of Interdomain Dynamics

Conformational Ensemble of Disordered Proteins Probed by Solvent Paramagnetic Relaxation Enhancement (sPRE)

Conformational Ensemble of Disordered Proteins Probed by Solvent Paramagnetic Relaxation Enhancement (sPRE)

Efficient Detection of Hydrogen Bonds in Dynamic Regions of RNA by Sensitivity‐Optimized NMR Pulse Sequences

Efficient Detection of Hydrogen Bonds in Dynamic Regions of RNA by Sensitivity‐Optimized NMR Pulse Sequences

hnRNP A1 Proofreads 3′ Splice Site Recognition by U2AF

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