Biomolecular NMR

Preprints related to the application and development of biomolecular NMR spectroscopy

List by Reid Alderson

Preprints:

Dynamic Aha1 Co-Chaperone Binding to Human Hsp90

Javier Oroz, Laura J Blair, Markus Zweckstetter

https://www.biorxiv.org/content/10.1101/550228v1

Atomic-level details about the interaction between Hsp90 and its co-chaperone Aha1

Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex

Diego Gauto, Leandro Estrozi, Charles Schwieters, Gregory Effantin, Pavel Macek, remy sounier, Astrid C. Sivertsen, Elena Schmidt, Rime Kerfah, Guillaume Mas, Jacques-Philippe Colletier, Peter Guntert, Adrien Favier, Guy Schoehn, Jerome Boisbouvier, Paul Schanda

https://www.biorxiv.org/content/10.1101/498287v1

Combines limited data from cryo-EM and solution- and solid-state NMR to determine structural models of a 500 kDa protein

Dynamics and interactions of ADP/ATP transporter AAC3 in DPC detergent are not functionally relevant

Vilius Kurauskas, Audrey Hessel, François Dehez, Chris Chipot, Beate Bersch, Paul Schanda

https://www.biorxiv.org/content/10.1101/317669v2

Data from NMR show that the the membrane protein AAC3 reconstituted in detergent is partially unfolded and inactive

Conformational Priming of RepA-WH1 for Functional Amyloid Conversion Detected by NMR Spectroscopy

David Pantoja-Uceda, Javier Oroz, Cristina Fernández, Eva de Alba, Rafael Giraldo, Douglas V. Laurents

https://www.biorxiv.org/content/10.1101/612135v1

Application of 15N spin relaxation and H/D exchange to investigate the structural and dynamical features of an amyloidogenic protein

Tuning site-specific dynamics to drive allosteric activation in a pneumococcal zinc uptake regulator

Daiana A. Capdevila, Fidel Huerta, Katherine A. Edmonds, My T. Le, Hongwei Wu, David P. Giedroc

https://www.biorxiv.org/content/10.1101/301853v1

Spin relaxation experiments characterize changes to backbone and methyl side-chain dynamics in the presence and absence of DNA. Allosteric changes upon zinc binding are identified through NMR. Now published in eLife https://elifesciences.org/articles/37268

Structural basis and mechanism of the unfolding-induced activation of an acid response chaperone HdeA

Xing-Chi Yu, Yunfei Hu, Jienv Ding, Hongwei Li, Changwen Jin

https://www.biorxiv.org/content/10.1101/390104v1

Residual structure and dynamics of the acid-unfolded chaperone HdeA are determined, and chemical exchange saturation transfer (CEST) and 19F NMR provide additional insight into the mechanism of HdeA. Now published in J. Biol. Chem. http://www.jbc.org/content/294/9/3192

Structural basis for terminal loop recognition and processing of pri-miRNA-18a by hnRNP A1

Hamed Kooshapur, Nila Roy Choudhury, Bernd Simon, Max Mühlbauer, Alexander Jussupow, Noemi Fernandez, Andre Dallmann, Frank Gabel, Carlo Camilloni, Gracjan Michlewski, Javier F. Caceres, Michael Sattler

https://www.biorxiv.org/content/10.1101/178855v3

NMR used in combination with other biophysical methods to determine the structure of a protein-RNA complex. Now published in Nat. Commun. https://www.nature.com/articles/s41467-018-04871-9

Rescue of Conformational Dynamics in Enzyme Catalysis by Directed Evolution

Renee Otten, Lin Liu, Lillian R. Kenner, Michael W. Clarkson, David Mavor, Dan S. Tawfik, Dorothee Kern, James S. Fraser

https://www.biorxiv.org/content/10.1101/185009v1

Usage of relaxation dispersion to characterize millisecond dynamics in the enzyme CypA and variants thereof obtained through directed evolution. Now published in Nat. Commun. https://www.nature.com/articles/s41467-018-03562-9

Systematic mapping of the free energy landscapes of a growing immunoglobulin domain identifies a kinetic intermediate associated with co-translational proline isomerization

Christopher A. Waudby, Maria-Evangelia Karyadi, Tomasz Wlodarski, Anaïs M. E. Cassaignau, Sammy Chan, Julian M. Schmidt-Engler, Anne S. Wentink, Carlo Camilloni, Michele Vendruscolo, Lisa D. Cabrita, John Christodoulou

https://www.biorxiv.org/content/10.1101/189050v1

Protein folding on the ribosome studied by NMR. Now published in Proc. Natl. Acad. Sci. USA https://www.pnas.org/content/115/39/9744.long

Categories: biophysics

Posted on: 21 May 2019

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