Sandra Viknander

This paper shows that thermal adaptation can be transferred between unrelated enzymes using a generative framework, improving thermostability without evolutionary homology.

This study uses AlphaFold2 to analyze how metabolism influenced enzyme structural evolution across 400 million years by examining 11,269 enzyme structures and their metabolic reactions.

This study shows that amino acid sequences determine protein abundance by affecting conformational stability and synthesis cost, using deep learning and yeast experiments.

The paper trains a deep learning model to predict enzyme thermal adaptation using a dataset of enzymes labeled with optimal growth temperatures.

This paper introduces ProteinGAN, a GAN that generates functional protein sequences, showing 24% of generated sequences are soluble and active in vitro.