Group2016
Phospholamban WT
PLN-AFA Monomer
Phospholamban
(WT) Pentamer
Sarcolipin
(WT) Monomer
Oriented and Magic Angle Spinning Solid State NMR
PKA-motion
SE-PISEMA
Protein Kinase A
NMR Methodology
Molecular Dynamics Simulation

Gianluigi Veglia
5-132 Hasselmo Hall
+1-612-625-0758
Lab manager
+1-612-301-9691
Wet lab
+1-612-626-2089
Lab office
+1-612-625-0786
5-256 Hasselmo Hall
Mailing address
6-155 Jackson Hall
321 Church st. SE
Minneapolis, MN, 55455
MNMR phones
+1-612-625-2715 (Tata Gopinath)
+1-612-624-8892 (Spectrometers)
LAB NEWS________________________________________________________________

How about getting eight times what you invest in NMR time? 17 May 2016

MAeSTOSO
A new approach by Gopinath and Veglia enables simultaneous acquisition of up to eight different solid-state NMR spectra with one experiment with an incredible saving in time. The MAeSTOSO (Multiple Acquisitions via Sequential Transfer of Orphan Spin pOlarization) approach relies on residual polarization of both (13)C and (15)N pathways and combines low- and high-sensitivity experiments into a single pulse sequence using one receiver and commercial ssNMR probes. The acquisition of multiple experiments does not affect the sensitivity of the main experiment; rather it recovers the lost coherences that are discarded, resulting in a significant gain in experimental time! To read more click here.

Cysteine ethylation as an NMR probe 10 December 2015

13C ethyl cysteine and DARR spectrum
For the human heart to function properly, calcium ions in cardiac muscle need to be moved to and from calcium ion reservoirs. One of the key players in this task is membrane-embedded enzyme called "SERCA". The structural changes of SERCA along the enzymatic pathway are crucial to its function, but how can one see these conformational transitions?

While solid-state NMR is ideally suited for such task, it requires carbon-13 isotope enrichment of the protein. It is not an issue for proteins that can be readily expressed in bacteria, but is a major problem if the protein is isolated from a natural source.

In the paper published in ACS Chemical Biology we address this bottleneck by introducing post-translational chemical labeling of the enzyme. By using a 13C enriched compound, we have performed reductive alkylation of the cysteines in SERCA, generating an isotope probe for magic angle spinning NMR spectroscopy.

The paper is authored by Vitaly Vostrikov, Martin Gustavsson, Tata Gopinath, Dan Mullen, Alysha Dicke, Vincent Truong and Gianluigi Veglia.

ASBMB special symposium 08 December 2015

ASBMB logo
Jonggul Kim and Cristina Olivieri (visiting scientist) are representing the research group at the "Kinases and Pseudokinases: Spines, Scaffolds and Molecular Switches" symposium at University of California, San Diego. The conference is organized by the American Society for Biochemistry and Molecular Biology.

Jonggul gave a talk "Signaling in the catalytic subunit of protein kinase A via hydrophobic motifs", while Cristina presented a poster "Conformational landscape of protein kinase inhibitor with and without protein kinase A ".

Sarah wins AHA grant 07 December 2015

Veglia lab logo
Sarah Nelson received a pre-doctoral fellowship from the American Heart Association (16PRE27770056). Her research proposal entitled "Structural effects of arrhythmia mutations on the calmodulin-RyR complex" focuses on the regulation of a 2.3 MDa calcium channel ryanodine receptor by a small water soluble protein calmodulin. The latter harbors several naturally occurring mutations, that affect the interaction between the two proteins, rendering the regulation less efficient and ultimately resulting in pathologies.

American Heart Association offers funding opportunities for graduate students and postdocs interested in initiating careers in cardiovascular and stroke research. Current Veglia lab members sponsored by the American Heart Association are Kailey Soller and Vitaly Vostrikov.
 

News Archive