Postdoctoral positions available
Veglia Group, May 2014
Phospholamban WT
PLN-AFA Monomer
(WT) Pentamer
(WT) Monomer
Oriented and Magic Angle Spinning Solid State NMR
Protein Kinase A
NMR Methodology
Molecular Dynamics Simulation

Gianluigi Veglia
5-132 Hasselmo Hall
Lab manager
Wet lab
Lab office
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________________________________________________________________

Biophysical Society meeting 21 January 2015

Biophysical SocietyAt the 59-th annual meeting of the Biophysical Society in Baltimore the Veglia lab will be presenting the following topics:

  • Feb 8, Sunday
    Alysha: Mapping of sarcolipin conformational states along the enzymatic pathway of SERCA (poster).
    Geoffrey: Probing multiple timescale dynamics of protein kinase A-inhibitor complexes (poster).
    Gianluigi: Allosteric regulation of the sarcoplasmic reticulum Ca2+-ATPase by phospholamban and sarcolipin using solid-state NMR spectroscopy (talk).
    Leanna: Phospholamban phosphorylation alters its conformational equilibrium to regulate SERCA activity (poster).

  • Feb 9, Monday
    Kailey: Sequence-independent ssDNA relieves phospholamban inhibition of SERCA in a length dependent manner (poster).

  • Feb 11, Wednesday
    Jonggul: Dysfunctional conformational dynamics of protein kinase A from R14 deletion of phospholamban (poster).
    Sarah: Characterization of calmodulin binding to the ryanodine receptor by solution and solid-state NMR (poster).
    Vitaly: Role of phospholamban mutations in protein-protein interactions (talk).

  • PISAmist: PISEMA calculation from pdb 12 December 2014

    SE-PISEMA spectrum
    Working with mechanically or magnetically aligned lipid bilayers one often faces the need to back-calculate the separated local field observables for a given structure. PISAmist, a program written by Vitaly, provides a fast and efficient way to extract the anisotropic chemical shifts and dipolar couplings from a pdb file. PISAmist allows one to change the Euler rotations of the structure, change the chemical shift tensor components and order parameter, select an amino acid type and to calculate the spectra with the lipid bilayer membrane normal either parallel, or perpendicular to the applied magnetic field. PISAmist provides both graphical and tabulated output, and returns the rotation matrix for the applied coordinate transformations.
    We hope the academic community will find PISAmist useful in their research.

    GPCR activation by TLQP-21 peptide 13 November 2014

    Phospholamban, R14del mutant
    A short water soluble peptide TLQP-21 has been shown to be an effective remedy against obesity. Our collaboration with several research groups from University of Minnesota, University of North Carolina at Chapel Hill and University of Rome Tor Vergata focused on elucidating the molecular target of this peptide. Solid-state NMR of TLQP-21 incubated with cell lines lacking the C3aR1 receptor showed that the peptide was unstructured. However, TLQP-21 adopted a folded conformation with the cells expressing C3aR1, revealing the folding-upon-binding mechanism of GPCR activation. The results published in Structure are co-authored by Vitaly, Raffaello and Gopinath.

    R14del lethal mutant of phospholamban 22 September 2014

    Phospholamban, R14del mutant
    Naturally occurring deletion of residue 14 (arginine) in cardiac phospholamban has been linked to the progression of heart disease. To understand the basis of this, Vitaly, Kailey, Gopinath and Kim Ha (Veglia group alumna) undertook biophysical studies of this membrane protein, the results of which have been published in Biochimica et Biophysica Acta. We have established that the regulatory domain of R14del is primarily unfolded, is more dynamic, and has weaker interactions with phospholipid bilayer, the qualities that affect its interaction with other proteins in the heart muscle.

    ICMRBS conference 25 August 2014

    ICMRBS 2014
    At the 26-th International Conference on Magnetic Resonance in Biological Systems (ICMRBS), Veglia group will present the following posters:

  • "Phosphorylation at adjacent sites affects phospholamban conformational equilibria to regulate SERCA activity" (Leanna, Vitaly, Gianluigi);

  • "Probing multiple timescale dynamics of a protein kinase A - inhibitor complex" (Geoffrey, Jonggul, Frank, Leanna, Gianluigi);

  • "Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour" (Giuliana Fusco, Alfonso De Simone, Gopinath, Vitaly, Michele Vendruscolo, Christopher Dobson, Gianluigi);

  • "Allosteric regulation of the sarcoplasmic reticulum Ca2+-ATPase by phospholamban and sarcolipin using solid-state NMR spectroscopy" (talk by Gianluigi).

  • MNMR workshop 03 June 2014

    MNMR workshopMinnesota NMR center is conducting a workshop on the theoretical and practical aspects of nuclear magnetic resonance with an emphasis on protein NMR. The detailed schedule can be found here. Members of the Veglia group will be giving the following lectures:

  • Gianluigi Veglia: Product operator formalism.
  • Tata Gopinath: Pulse sequence engineering.
  • Leanna McDonald: Sequential assignment and protein dynamics.
  • Jonggul Kim: Assignment of methyl groups of large proteins.
  • Vitaly Vostrikov: Structure calculation, analysis and validation using XPLOR-NIH.

    Workshop photos are available on the MNMR Facebook page.


  • α-synuclein interaction with synaptic vesicles models 29 May 2014

    α-synuclein domainsα-synuclein is a 140 residue protein, implicated in the progression of Parkinson's disease. Due to its dynamic nature, it has not been amenable to conventional methods like solution NMR or X-ray crystallography. Members of the Veglia group (Gopinath and Vitaly) in collaboration with scientists from the University of Cambridge and Imperial College London (UK) employed solid-state magic angle spinning NMR in combination with CEST technique to probe the dynamic regimes of physiologically relevant, non-aggregated form of α-synuclein.
    The results published in Nature Communications allowed us to propose a model for α-synuclein binding to the synaptic vesicles mimicks, reconciling the results of a range of previous studies.


    Veglia group, May 2014 23 May 2014

    Veglia group, May 2014
    Back, left to right:
    Gopinath, Gianluigi, Jonggul, Alessandro, Alysha, Geoffrey, Adak, Atul, Manu.
    Front, left to right:
    Vitaly, Sarah, Kailey, Chelsea, Leanna, Callahan.

    Awards in the Veglia lab 07 May 2014

    Veglia lab logo
    Leanna McDonald was awarded a three-year Ruth L. Kirschstein Postdoctoral fellowship, supported by the National Institute of Dental and Craniofacial Research.
    Sarah Nelson was a recipient of a Thomas S. Reid Award for Biochemistry, awarded to "a graduate student whose research has applications beyond the academic community".
    Vitaly Vostrikov's poster at the Biomolecular Structure, Dynamics, and Function: Membrane Proteins symposium was picked as a session winner.

    Vitaly also received the Paul D. Boyer-James B. Peter Award, recognizing "a postdoctoral fellow (up to 5 years post-Ph.D.) who has made significant research contributions in any area of biochemistry under the direction of a BMBB faculty member". Previous lab members honored include Nate Traaseth (2008), Larry Masterson (2010), Tata Gopinath (2011) and Raffaello Verardi (2012).

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