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#structuralbiology

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What determines the folding and stability of protein structures? In his fourth lecture, Dr. Ali Hassanali from the Abdus Salam International Centre for Theoretical Physics (ICTP) explores the intricate world of protein secondary structures, focusing specifically on alpha helices and beta sheets. Dr. Hassanali explains how these structures are stabilized through a variety of interactions, including hydrogen bonding and electrostatic effects, and the critical role of dihedral angles as illustrated by the Ramachandran plot.

This lecture also highlights the essential contributions of cysteine in forming disulfide bonds, which enhance protein stability in challenging environments. By examining the interplay of molecular interactions, Dr. Hassanali provides insights into the architectural and functional significance of these secondary structures as well as their evolutionary adaptations.

🎥 Join us for this #OpenAccess lecture and engage in discussions with Dr. Hassanali himself and other members of the Enabla community: enabla.com/pub/606/about

New Presidential executive order on proteins:

All amino acids now to be right w̶i̶n̶g̶ handed.

Leftist amino acids to be outlawed.

(Also, Z-DNA is deemed to be Communist, and is prohibited.)

Trans- and cis- peptide bonds to be banned.

Non-binary amino acid Glycine to be banned.

Proline is not a real amino acid and will be banned immediately.

Phenylalanine looks and sounds a bit like Fentanyl, banned immediately.

@strucbio #StructuralBiology #PDB

This study investigates the surprising limitations of AlphaFold 2 (AF2) in predicting protein structures—specifically its tendency to confidently predict β-solenoid folds for repeat proteins, even when the structures are unrealistic or unstable.

🔗 AlphaFold 2, but not AlphaFold 3, predicts confident but unrealistic β-solenoid structures for repeat proteins. DOI: doi.org/10.1016/j.csbj.2025.01

📚 CSBJ: csbj.org/

There is an Associate Professor Position in #Bioinformatics with a Focus on #AI Applications in Integrated #StructuralBiology available in our Institute in Marseilles (France) @afmblab.bsky.social
@afmblab.bsky.social
@strucbio @bioinformatics

The successful candidate will create his/her own team for developing and implementing innovative AI-based approaches to address key challenges in structural biology, including but not limited to:
1. Designing synthetic proteins with novel or enhanced enzymatic properties.
2. Developing synthetic protein or biomolecule binders for therapeutic or biotechnological applications.
3. Performing molecular docking of small molecules on therapeutic targets.
4. Modelling macromolecular complexes in silico.

* Contact : For more information, please contact Juan Reguera, Unit Director, including a brief CV.
Formal applications should include:
• A detailed CV with a summary of past and present research and teaching activities.
• A short description of research project and implementation plan.
• A motivation letter.