Biohub Integrations

ESMC marks the latest innovation in the ESM series of protein language models, advancing the understanding of representation learning in protein biology. By training on an enormous dataset of billions of evolutionary sequences, it effectively captures representations that provide insights into the mechanistic aspects of protein structure and function. Utilizing a transformer architecture, the model prioritizes sequences as its main input and is trained on a dataset that includes up to 6 billion proteins. ESMC is designed for a range of applications within protein science, including structure prediction, functional annotation, protein design, and the investigation of evolutionary relationships among proteins. Furthermore, it has the ability to generate new proteins from partial sequences, structures, or specific functional requirements, which allows researchers to explore novel possibilities in protein design and biological research. The model is readily accessible through the Biohub Platform, enabling users to interact with it via an API and the ESM Python package, which offers quickstart resources for installation, API key generation, and connection to the platform, thus ensuring a user-friendly experience. This ease of access not only promotes wider participation in protein research but also fosters collaborative efforts across the scientific community, ultimately driving further advancements in the field. With its capabilities, ESMC opens new doors for innovation and discovery in protein science.

Building upon its predecessor, ESMFold, ESMFold2 sets a new standard in the realm of single-sequence structure prediction while also enabling the design of novel functional proteins by delving into the latent space of the ESMC model. This sophisticated model can accurately predict high-resolution, all-atom 3D structures of biomolecular complexes directly from amino acid sequences and incorporates multiple sequence alignments to enhance accuracy for challenging targets. Designed to predict structures using both sequence and structural modalities, it utilizes ESM representations that power a sequence of looped folding layers, while a diffusion model converts pairwise representations into atomic-resolution results. ESMFold2 stands out in its ability to forecast protein structures from amino acid sequences, providing comprehensive structural information, including exact all-atom coordinates for backbone and side chains, as well as confidence metrics and optional distogram predictions for thorough structural analysis. In addition, its groundbreaking methodology deepens the understanding of protein folding dynamics and their functional implications, positioning it as an indispensable tool for researchers engaging in this area of study. Ultimately, ESMFold2 not only advances structural biology but also opens new avenues for the development of protein-based applications.