Biocomputing Group

Jan 12, 2025 | academic.oup.com | Biocomputing Group |Pier Luigi

The knowledge of protein stability upon residue variation is an important step for functional protein design and for understanding how protein variants can promote disease onset. Computational methods are important to complement experimental approaches and allow a fast screening of large datasets of variations. In this work we present DDGemb, a novel method combining protein language model embeddings and transformer architectures to predict protein ΔΔG upon both single- and multi-point variations.

Aug 4, 2023 | academic.oup.com | Biocomputing Group |Pier Luigi |Giovanni Madeo |Lupas AN

Coiled-coil domains (CCD) in proteins are structural motifs where α‐helices pack together in an arrangement called knobs into holes (Crick 1952, 1953a, b). Since the first crystallographic observation in the structure of influenza virus hemagglutinin (Wilson et al. 1981), CCDs have been resolved in several proteins through all the kingdoms of life (Truebestein and Leonard 2016).