BEGIN:VCALENDAR VERSION:2.0 PRODID:icalendar-ruby CALSCALE:GREGORIAN BEGIN:VEVENT DTSTAMP:20260711T172351Z UID:c14d907a-a774-405a-b435-069b4388d8d1 DTSTART:20220628T090000Z DTEND:20220628T170000Z DESCRIPTION:This is the third and last webinar of the series about [the imp act of AlphaFold on training and research in life sciences](https://www.eb i.ac.uk/training/events/impact-of-alphafold-on-training-and-research-in-li fe-sciences/). This webinar will focus on the impact of AlphaFold on resea rch and development in life sciences by highlighting a variety of case stu dies from academia as well as industries.\n\nIn this webinar we had the fo llowing panel of speakers:\n\n**Jan Kosinski -** AlphaFold has revolutioni sed structural biology by enabling the modelling of monomeric proteins and small complexes at accuracy similar to experimental structures. However\, to model large complexes\, it still needs to be integrated with experimen tal data such as cryo-electron microscopy maps. I presented how such an in tegrative combination enabled us to model the human nuclear pore complex a t unprecedented completeness and precision. I used this example to highlig ht the new opportunities for integrative structural biology. \n\n**Juan C arlos Mobarec -** Methods and software to obtain information about protein structures from amino-acid sequences have been applied in the pharmaceuti cal industry over the span of decades. Hence\, what can deliver the AI-con taining modelling workflows such as AlphaFold to early stage R&\;D? We have pioneered the application of AlphaFold in R&\;D on multiple cases. Here\, we reviewed use case examples of the latest automated workflow for protein structure prediction.\n\n**Juri Rappsilber -** Crosslinking mass spectrometry is now a well-established experimental technique for investig ating protein interactions\, structure and function. Crosslinking MS also remains unparalleled in its ability to provide structural information in c omplex systems. This is particularly relevant in the light of the most rec ent revolutionary advancement in structural biology. Artificial intelligen ce program-based predictions of protein structure (e.g. by AlphaFold) are having a wide-ranging impact on our ability to model protein structures bu t also to study protein interactions that are yet to be fully understood. Crosslinking mass spectrometry offers here highly relevant experimental da ta. Using a crosslinking mass spectrometry study of _Bacillus subtilis_ we have investigated different aspects of joining AlphaFold and crosslinking . Particularly\, the validity of the ipTM score was probed by crosslinking mass spectrometry\, and we present the possibility of assembling larger c omplexes based on the pairwise data resulting from crosslinking mass spect rometry and the AlphaFold prediction of two-protein interactions. Ultimate ly\, our structural understanding of biology stands to gain much from comb ining AlphaFold and crosslinking data\, particularly in our drive towards building a structural and functional understanding of the cell.\n\n**Katja Luck -** AlphaFold’s ability to predict the structure of folded regions of proteins and to identify disordered regions of proteins with unprecede nted accuracy transforms experimental design in molecular biology. First\, I discussed how AlphaFold can advance the design of functional and well-e xpressed protein constructs for the study of protein interactions and prot ein binding regions. Second\, I highlighted the potential\, possible appro aches but also limitations of AlphaFold for the identification of protein- protein interaction interfaces.\n\nPanel discussion was chaired by **Janet Thornton**.\n\n  LOCATION:\, SUMMARY:Impact of AlphaFold on research and development URL;VALUE=URI:https://www.ebi.ac.uk/training/events/impact-alphafold-resear ch-and-development END:VEVENT END:VCALENDAR