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Lucy J. Colwell

Researcher at University of Cambridge

Publications -  63
Citations -  4732

Lucy J. Colwell is an academic researcher from University of Cambridge. The author has contributed to research in topics: Computer science & Biology. The author has an hindex of 26, co-authored 51 publications receiving 3050 citations. Previous affiliations of Lucy J. Colwell include Medical Research Council & Harvard University.

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Protein 3D structure computed from evolutionary sequence variation.

TL;DR: Surprisingly, it is found that the strength of these inferred couplings is an excellent predictor of residue-residue proximity in folded structures, and the top-scoring residue couplings are sufficiently accurate and well-distributed to define the 3D protein fold with remarkable accuracy.
Posted Content

Rethinking Attention with Performers

TL;DR: Performers, Transformer architectures which can estimate regular (softmax) full-rank-attention Transformers with provable accuracy, but using only linear space and time complexity, without relying on any priors such as sparsity or low-rankness are introduced.
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Three-dimensional structures of membrane proteins from genomic sequencing.

TL;DR: It is shown that amino acid covariation in proteins, extracted from the evolutionary sequence record, can be used to fold transmembrane proteins, and how the method can predict oligomerization, functional sites, and conformational changes in transmemBRane proteins is shown.
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The interface of protein structure, protein biophysics, and molecular evolution.

TL;DR: The relationship between modeling and needed high‐throughput experimental data as well as experimental examination of protein evolution using ancestral sequence resurrection and in vitro biochemistry are presented, towards an aim of ultimately generating better models for biological inference and prediction.
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InterPro in 2022

TL;DR: The InterPro database as discussed by the authors provides an integrative classification of protein sequences into families, and identifies functionally important domains and conserved sites, and provides a more user friendly access to the data.