Status:Closed

Opening date: 4 April 2023

Closing date: 12 May 2023

Master's internship

Objective of the call for proposals

By supporting technological or methodological development within leading technology platforms, this call for proposals offers the opportunity to train Master's students in the latest technologies, and promotes the scientific community's access to a cutting-edge technological offering for its research work.

Given IM2B's twofold objective of enhancing the value of its technology platforms and strengthening its Master's training programs by developing interdisciplinarity and professionalization, this call for tenders aims to fund 4 to 6 Master's 2 internships at IM2B's technology platforms in the 2023-2024 academic year.

These internships must meet the highest standards of quality and innovation.

Tender process

This call for proposals is divided into two stages:

  1. Call for internship projects open to staff from technology platforms within the IM2B perimeter.

    The Training Committee selects 4 to 6 internship projects.

  2. Call for applications and submission of one to three applications by internship supervisors.

    Validation of applications by the Training Committee.

     

Eligibility requirements

  • The project must involve technological and/or methodological development(s) to be implemented by an IM2B technology platform;
  • The internship is supervised by a technology platform staff member;

  • The application must comply with the IM2B timetable and framework.

     

Selection criteria

After checking the eligibility of the projects submitted, the IM2B Training Committee will evaluate the projects and select 4 to 6 internship projects, according to the following selection criteria:

  • Project quality;
  • Added value of the technological/methodological development for the platform, in particular its "transferability" to the scientific community;
  • Professionalization of the internship (its value in developing the employability of future graduates);

  • Suitability of the internship topic for the profile of students enrolled in the IM2B2 Master's program.
     

    The interdisciplinary nature of the internship will be considered a bonus.

Documents

Agnès
Kammoun
Project manager, Deputy Co-Director Technology platforms and value enhancement
IMM
agnes.kammoun@univ-amu.fr

Testimonials

Maxime Bizet

IM2B financed my M2 chemistry internship, which I carried out between the "Protein Expression Facility" (PEF) technology platform and the "Bioenergetics and Protein Engineering" Laboratory (BIP). This work enabled me to acquire interdisciplinary skills that are in line with my professional project at the chemistry-biology interface, in particular as part of my PhD at BIP.

See all testimonials

Awardees

  • Awardees

    2023
    Master's internship

    From nanobodies to megabodies

    Project leader(s)
    Anaïs GAUBERT (AFMB)
    Laboratory(s)
    Architecture and function of biological macromolecules (AFMB)
    Master's internship

    From nanobodies to megabodies

    Project leader(s)
    Anaïs GAUBERT (AFMB)
    Laboratory(s)
    Architecture and function of biological macromolecules (AFMB)

    A new tool coming from nanobodiesR has emerged: MegabodiesR.

    Megabodies R are constructed by grafting a nanobody to a scaffold protein, enhancing the molecular weight while retaining the affinity and specificity of binding towards the target.

    The purpose of those megabodies is to overcome two major obstacles that limit cryo-EM resolution: size particles and preferential orientation at the water-air interface (Uchański et al., 2021).

    This project aims at developing a methodology to design R megabodies from existingR nanobodies.

    See the associated call for project

  • Awardees

    2023
    Master's internship

    Characterization of inclusion bodies

    Project leader(s)
    Deborah BYRNE (IMM) & Yasmina BOUZARIOUH (IMM)
    Laboratory(s)
    Biomass & Protein Engineering - Meditarannean Institute of Microbiology (IMM)
    Master's internship

    Characterization of inclusion bodies

    Project leader(s)
    Deborah BYRNE (IMM) & Yasmina BOUZARIOUH (IMM)
    Laboratory(s)
    Biomass & Protein Engineering - Meditarannean Institute of Microbiology (IMM)

    Recombinant protein expression in cells often leads to the Training of inclusion bodies (IBs), aggregates traditionally viewed as containing denatured, inactive proteins (Mayer & Buchner, 2003). However, recent studies have challenged this perception by revealing that IBs can harbor a significant portion of the cell's total protein content, with up to 95% purity. This dichotomy in IB composition distinguishes classical inclusion bodies (IBsC), characterized by compact, amorphous structures, from non-classical inclusion bodies (ncIBs), which exhibit a higher proportion of correctly folded proteins, facilitating their extraction and solubilization (Bucciantini et al., 2002); (Upadhyay et al., 2012).

    This study focuses on delineating the parameters distinguishing classical IBs from ncIBs and optimizing production methods for proteins prone to aggregation. Through microscopic analysis, dynamic light scattering (DLS), and thermodynamic studies, we elucidated the distinct characteristics of these inclusion bodies. Our findings reveal that classical IBs form dense structures within bacteria, impacting cell division and localization, whereas ncIBs exhibit diffuse morphology in the cytoplasm. Moreover, while classical IBs necessitate denaturing agents for solubilization, hindering protein yields, ncIBs offer a promising alternative with their porous, less dense assembly, facilitating extraction using non-denaturing agents. By exploiting this distinction, we demonstrate the transformation of classical IB production into ncIB thereby enhancing yields of recalcitrant proteins.

    Our results, supported by molecular, structural and biophysical techniques, underscore the potential of ncIBs as a platform for diverse protein production, offering avenues for enhancing yields and addressing challenges associated with hydrophobic and disordered proteins.

    Biomass & Protein Engineering platform

    Classical Inclusion Bodies (Credits Yasmina Bouzariouh & Hugo Le Guenno)

    See the associated call for project