The J-810 Series Circular Dichroism spectrophotometer is commonly used in the UV region of the spectrum to obtain information about protein secondary structure, in a wavelength range from 163nm to 900 nm. This instrument is equipped with a computer-controlled Peltier device and offers confidence in the data from characterization studies of biomolecule structure, function and stability under a wide variety of experimental conditions. Quantitative multivariate analysis program for the estimation of protein secondary structures from the CD spectra is also provided. Spectra Manager™ software is a comprehensive lab companion for capturing and processing data, eliminating the need to learn multiple software programs and allowing data from more than one instrument to be manipulated and displayed together on the same platform.
Light source: 150 W Xenon arc lamp (air cooled), Sample chamber: small or large - designed for various experimental techniques, Wavelength range: ~163 to ~900 nm (standard), Four Channel Simultaneous Data Acquisition: Input channels: 2 internal plus 2 external signals can be acquired simultaneously.
EDUCATION
2019: PhD in Structural Biology and Protein Biomaterials (UoC, IMBB-FORTH - Greece)
2012: M.Sc. in Protein Biotechnology (UoC-Greece)
2009: Diploma Degree in Biology (UoC-Greece)
WORKING EXPERIENCE
Oct 2019 – Now: Post-Doctoral Researcher at I.M.B.B.-F.O.R.TH, Greece
(Laboratory of Structural Biology)
Sep 2020 – Now: Autonomous teaching and exam organizing of the under-graduate courses
"Enzymatic Biotechnology" and “Protein Engineering” at the Dept. of
Biology of the Uni. of Crete
2014 – 2020: Experienced scientist position at I.M.B.B.-F.O.R.TH, Greece (InnovCrete project /FP7-Regpot program) and at University of Crete
Oct. 2010 –Jan. 2011: Laboratory Teaching Assistant of Microbiology Teaching Lab
at the Dept. of Biology, Uni. of Crete
SELECTED PUBLICATIONS
*Kefala K., Kotsifaki D., Providaki M., Kapetaniou E., Rahme L. and Kokkinidis M. Purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal fragment of the MvfR protein of Pseudomonas aeruginosa. (2012). Acta. Cryst F, 68, 695-697
*Kefala A., Kotsifaki D., Providaki M., Amprazi M. and Kokkinidis M. Expression, purification and crystallization of a protein resulting from the inversion of the aminoacid sequence of a helical bundle. (2017). ). Acta. Cryst F, 73, 51-53
Dimovasili C., Fadouloglou V.E., Kefala A., Providaki M., Kotsifaki D, Sarrou I., Plaitakis A., Zaganas I. and Kokkinidis M. Crystal structure of glutamate dehydrogenase 2, a positively selected novel human enzyme involved in brain biology and cancer pathophysiology. Journal of Neurochemistry (accepted)
RESEARCH PROFILE
Being in a Structural Biology group since 2011, Dr. Kefala A. has studied deeply the protein folding problem, elucidating the relation between amino acid sequence and structural properties of α-helical bundles. The knowledge obtained was used for protein design leading to bio-derived materials for bio-medical applications and basic research through structural studies of protein folding through reverse sequences.
Notable achievements include:
The elucidation of the protein folding of mutants of the α-helical protein Rop that is used as a canonical paradigm of this structural motif.
Protein design of novel protein-based biomaterials with specific engineered properties.
EDUCATION
2019: International Diploma in Business Administration (ELKEDIM. Lifelong LC, Greece)
2012: PhD in Structural Biology and Protein Biomaterials (UoC, IMBB-FORTH - Greece)
2007: M.Sc. in Protein Biotechnology (UoC-Greece)
2005: Diploma Degree in Biochemistry and Biotechnology (UoT-Greece)
WORKING EXPERIENCE
May 2016 – Now: Post-Doctoral Researcher at I.M.B.B.-F.O.R.TH, Greece
(Laboratory of Structural Biology)
Nov. 2012 – Apr. 2016: Experienced scientist position at I.M.B.B.-F.O.R.TH, Greece
(InnovCrete project /FP7-Regpot program)
Sept 2019 – Now: Autonomous teaching and exam organizing of the under-graduate courses
"Enzymatic Biotechnology" and “Protein Engineering” at the Dept. of
Biology of the Uni. of Crete
Oct. 2006 –Jan. 2007: Laboratory Teaching Assistant of Microbiology Teaching Lab
at the Dept. of Biology, Uni. of Crete
SELECTED PUBLICATIONS
Mermigka G, Amprazi M, Mentzelopoulou A, Amartolou A, Sarris PF (2020) Plant and Animal Innate Immunity Complexes: Fighting Different Enemies with Similar Weapons. Trends Plant Sci. 2020 Jan;25(1):80-91
Kefala K., Kotsifaki D., Providaki M., Amprazi M. and Kokkinidis M. (2017) Expression, purification and crystallization of a protein resulting from the inversion of the amino-acid sequence of a helical bundle. Acta. Cryst F, 73(1), 51-53
Amprazi M., Kotsifaki D., Providaki M., Kapetaniou EG., Fellas G., Kyriazidis I.,Perez J.and Kokkinidis M. (2014) Structural plasticity of 4-α-helical bundles exemplified by the puzzle-like molecular assembly of the Rop protein. PNAS. 111(30): 11049-54
Ambrazi M., Fellas G., Kapetaniou EG., Kotsifaki D., Providaki M. and Kokkinidis M. (2008) Purification, crystallization and preliminary X-ray diffraction analysis of a variant of the ColE1 Rop protein. Acta Cryst. F 64: 432–434
SCΗOLARSHIPS, AWARDS and GRANTS
Grant "Support for Researchers, with Emphasis on Young Researchers" of the Ministry of Education's Education and Lifelong Learning Program (40.600 euro) (2018)
Short-Term Fellowship by FEBS (2.000 euro) (2012) and Short-Term Fellowship by EMBO (9.000 euro)(2011)
Scholarship “HRAKLEITOS II” for perusing a PhD of the Hellenic Ministry of Education, co-funded by (ESF) & National Source (45.000 euro) (2009-2012)
RESEARCH PROFILE
Being in a Structural Biology group since 2006, Maria Amprazi has studied deeply the protein folding problem, elucidating the relation between amino acid sequence and structural properties of α-helical bundles. The knowledge obtained was used for protein design leading to bio-derived materials for bio-medical applications.
Notable achievements include:
The elucidation of the protein folding pathway of the α-helical protein Rop that is used as a canonical paradigm of this structural motif.
Protein design of novel protein-based biomaterials with specific engineered properties.
Design and production of protein scaffolds that lead to restriction enzymes with new specificities, finding great application in gene therapy.
Light source: 150 W Xenon arc lamp (air cooled), Sample chamber: small or large - designed for various experimental techniques, Wavelength range: ~163 to ~900 nm (standard), Four Channel Simultaneous Data Acquisition: Input channels: 2 internal plus 2 external signals can be acquired simultaneously.