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Emotion recognition systems are typically trained to classify a given psychophysiological state into emotion categories. Current platforms for emotion ground-truth collection show limitations for real-world scenarios of long-duration content (e.g. $> $ > 10 minutes), namely: 1) Real-time annotation tools are distracting and become exhausting; 2) Perform retrospective annotation of the whole content in bulk (providing highly coarse annotations); or 3) Are used by external experts (depending on the number of annotators and their subjective experience). We explore a novel approach, the EmotiphAI Annotator, that allows undisturbed content visualisation and simplifies the annotation process by using segmentation algorithms that select brief clips for emotional annotation retrospectively. We compare three methods for content segmentation based on physiological data (Electrodermal Activity (EDA), emotion-based), scene (time-based), and random (control) selection. The EmotiphAI Annotator attained a B+ System Usability Scale score and low-average mental workload as per the NASA Task Load Index (40%). The reliability of the self-report was analysed by the inter-rater agreement (STD $< $ < 0.75), coherence across time segmentation methods (STD $< $ < 0.17), comparison against the state-of-the-art ground truth (STD $< $ < 0.7), and correlation to EDA ($> $ > 0.3 to 0.8), where the EDA-based method obtained the overall best performance. [ABSTRACT FROM AUTHOR]

During group interactions, we react and modulate our emotions and behaviour to the group through phenomena including emotion contagion and physiological synchrony. Previous work on emotion recognition through video/image has shown that group context information improves the classification performance. However, when using physiological data, literature mostly focuses on intrapersonal models that leave-out group information, while interpersonal models are unexplored. This paper introduces a new interpersonal Weighted Group Synchrony approach, which relies on Electrodermal Activity (EDA) and Heart-Rate Variability (HRV). We perform an analysis of synchrony metrics applied across diverse data representations (EDA and HRV morphology and features, recurrence plot, spectrogram), to identify which metrics and modalities better characterise physiological synchrony for emotion recognition. We explored two datasets (AMIGOS and K-EmoCon), covering different group sizes (4 vs dyad) and group-based activities (video-watching vs conversation). The experimental results show that integrating group information improves arousal and valence classification, across all datasets, with the exception of K-EmoCon on valence. The proposed method was able to attain mean M-F1 of $\approx$ ≈ 72.15% arousal and 81.16% valence for AMIGOS, and M-F1 of $\approx$ ≈ 52.63% arousal, 65.09% valence for K-EmoCon, surpassing previous work results for K-EmoCon on arousal, and providing a new baseline on AMIGOS for long-videos. [ABSTRACT FROM AUTHOR]

The NOD-like receptor pyrin domain containing 3 (NLRP3) is a multidomain protein that plays a key role in innate immune response. Structures of NLRP3 in different conformational states and bound to cognate partners are available. In this chapter we present an approach to model the oligomeric structure of NLRP3 by homology modeling using multiple templates, symmetry, and refinement. The overall process presented here represents advanced exercise in structural modeling that provides unique insights into the biological role and activation of NLRP3 oligomer. Finally, the same approach can be easily adapted to the rest of the members of the NLRP family., (© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.)

Proteins are the workhorses of cells to carry out sophisticated and complex cellular processes. Such processes require a coordinated and regulated interactions between proteins that are both time and location specific. The strength, or binding affinity, of protein-protein interactions ranges between the micro- and the nanomolar association constant, often dictating the molecular mechanisms underlying the interaction and the longevity of the complex, i.e., transient or permanent. In consequence, there is a need to quantify the strength of protein-protein interactions for biological, biomedical, and biotechnological applications. While experimental methods are labor intensive and costly, computational ones are useful tools to predict the affinity of protein-protein interactions. In this chapter, we review the methods developed by us to address this question. We briefly present two methods to comprehend the structure of the protein complex derived by either comparative modeling or docking. Then we introduce BADOCK, a method to predict the binding energy without requiring the structure of the protein complex, thus overcoming one of the major limitations of structure-based methods for the prediction of binding affinity. BADOCK utilizes the structure of unbound proteins and the protein docking sampling space to predict protein-protein binding affinities. We present step-by-step protocols to utilize these methods, describing the inputs and potential pitfalls as well as their respective strengths and limitations., (© 2022. Springer Science+Business Media, LLC, part of Springer Nature.)