A Journal of Postdoctoral Research.
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Title : Ms.
First Name : SOUMYA
University/Institution : Lawrence Berkeley National lab
Email ID : sgremesh@lbl.gov
City : Berkeley
Country : United States
State : California
Zipcode : 94720
Department : Molecular Biophysics and Integrated Bioimaging
Company Name :
Area of Research
Protein-DNA complexes, DNA binding proteins, Nucleoid associated proteins, antibodies, MHC I, T-cell receptors
Area of Expertise
Biochemistry, Structural biology, Biophysics, Molecular biology, Protein chemistry, X-ray crystallography, Small-angle X-ray scattering, Molecular modeling, soft X-ray tomography
Brief Description of Research Interest :


2016-2017: During the first year of my training at Lawrence Berkeley National lab as aBiochemist Postdoctoral Fellow, I was involved in expanding BILBOMD (SAXS validatedmolecular dynamics approach for atomic modeling) developed by Dr. Michal Hammel at SIBYLSfor conformational sampling of glycosylated proteins such as therapeutic antibodies. Manuscript describing the work was published in STRUCTURE (Cell Press).

2016-2018: A second area of interest is in structurally and mechanistically characterizing therole of bacterial nucleoid associated proteins (NAPs) in maintaining bacterial DNA topology. Weemploy X-ray crystallography and SAXS to understand the role of NAPs at nanoscale. We also use a novel imaging technique called Soft X-ray tomography (SXM) to image bacterial cells innear-native state and correlate changes in gene expression to changes in DNA topology.

2015-2016: As a Visiting Scientist at the La Jolla Institute of Allergy and Immunology, Idetermined the crystal structures of Major Histocompatibility Complex I (MHCI) with non-canonical peptides important in mediating host immunity. This work is published in two journalarticles (in 2016 and 2017) that introduced a novel mode of binding of extended peptides toMHCI. The results have led to the development of novel bioinformatics prediction algorithms toaid prediction of allergy causing peptides. A patent based on the work is pending at USPTO.

2010-2014: For my doctoral thesis, I characterized the mammalian DNA-binding protein, IRF4(Interferon Regulatory Factor 4) using MX, Small-angle X-ray scattering (SAXS) and analyticalultra-centrifugation (AUC). IRF4 is a member of the Interferon Regulatory family of proteinsregulating the human immune system. By combining results from various biophysicaltechniques, we showed that the molecular mechanism of activation of IRF4 is different thanother members of the family. This work was published in 2015.

2008-2010: For my master’s thesis, I characterized a biocatalyst enzyme, threonine aldolase (e-TA) from E. coli that catalyzes diastereoselective carbon-carbon bond formation. Through use ofX-ray crystallography (MX) and other biochemical techniques we determined the molecularmechanism of enzyme catalysis. The work aids development of e-TA for quick and efficientgeneration of pharmaceutical intermediates. This work has been published in two separatejournal articles published in 2014 and 2015

Representative Publications :

o  di Salvo ML, RemeshSG, Vivoli M, Ghatge MS, Paiardini A, D'Aguanno S, Safo MK, Contestabile R.FEBS J., 281, 129-145 (2014)

o  Remesh SG, Ghatge MS, Ahmed MH, Musayev FN, Gandhi A, Chowdhury N, di Salvo ML,Kellogg GE, Contestabile R, et al. Biochimica et Biophysica Acta, 1854, 278-283(2015)

o  Remesh SG, Santosh V, Escalante CR.  J. Biol. Chem., 290, 27779-27790 (2015)

o  McMurtrey C, TrolleT, Sansom T, Remesh SG, Kaever T, Bardet W, Jackson K, McLeod R, etal. eLife 2016;10.7554/eLife.12556 (2016)

o  Hammel M, Yu Y,Radhakrishnan SK, Chokshi C, Tsai MS, Matsumoto Y, Kuzdovich M, RemeshSG, et al. J. Biol. Chem., 291, 26987-27006 (2016)

o  Remesh SG, Andreatta M, Ying G, Kaever T, Nielsen M, McMurtrey C,Hildebrand W, Peters B, Zajonc DM. J. Biol. Chem., 292, 5262-5270 (2017)

o  Guillaume J, WangJ, Janssens J, Remesh SG, Risseeuw MDP, Decruy T, Froeyen M,Elewaut D, et al. Sci. Rep., 7, 4276-4294 (2017)

o  Remesh SG et al Conformational plasticity of theImmunoglobulin Fc domain in solution. Structure (Cell Press), 26, 1007–1014 (2018)

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