Keating Lab (@keating_lab) 's Twitter Profile
Keating Lab

@keating_lab

We use computational and experimental methods to study protein structure, function, and interactions at @MITBiology @MITBE

ID: 1377741548071256066

calendar_today01-04-2021 21:56:48

15 Tweet

634 Followers

99 Following

UCLA Chem & Biochem (@uclachem) 's Twitter Profile Photo

Read about the amazing accomplishments of alum MIT biologist and president of The Protein Society, Prof. Amy Keating (PhD ’98 Houk/García-Garibay groups) bit.ly/3w0kA7O Ken Houk Garcia-Garibay Research Group (MGG Lab) MIT Biology proteinsociety

Read about the amazing accomplishments of alum MIT biologist and president of The Protein Society, Prof. Amy Keating (PhD ’98 Houk/García-Garibay groups) bit.ly/3w0kA7O <a href="/houk1000/">Ken Houk</a> <a href="/GaribayLab/">Garcia-Garibay Research Group (MGG Lab)</a> <a href="/MITBiology/">MIT Biology</a> <a href="/ProteinSociety/">proteinsociety</a>
Kevin K. Yang 楊凱筌 (@kevinkaichuang) 's Twitter Profile Photo

Review of data-driven protein design, including structure, sequences, and high-throughput functional datasets. Vincent Frappier Keating Lab sciencedirect.com/science/articl…

Review of data-driven protein design, including structure, sequences, and high-throughput functional datasets. 

Vincent Frappier <a href="/KeatingLab/">Keating Lab</a> 

sciencedirect.com/science/articl…
Keating Lab (@keating_lab) 's Twitter Profile Photo

Excited to share our newest work! We describe a surprising mechanism behind how a short linear motif binding domain achieves interaction specificity. elifesciences.org/articles/70601

Raleigh McElvery (@raleighmcelvery) 's Twitter Profile Photo

Scientists in Keating Lab designed a screening method to probe how short stretches of amino acids called SLiMs selectively bind to certain proteins, and distinguish between binding partners with similar structures. I covered this recent work for MIT News: bit.ly/3B4piEb

Scientists in <a href="/keating_lab/">Keating Lab</a> designed a screening method to probe how short stretches of amino acids called SLiMs selectively bind to certain proteins, and distinguish between binding partners with similar structures. I covered this recent work for MIT News: bit.ly/3B4piEb
Sebastian (@sassseabass) 's Twitter Profile Photo

Fast, reliable, computational methods for designing protein-binding peptides would be immensely useful. As a first step, we show that tertiary structural motifs from the PDB can be used to reconstruct known peptide structures and generate new ones. doi.org/10.1002/pro.43… (1/9)

PEC Conference (@pec_conference) 's Twitter Profile Photo

Our first keynote speaker: Dr. Amy Keating (Keating Lab). Interested in protein interaction specificity, Dr. Keating highlights the power of data-driven computational exploration of protein interactions. Dr. Keating was our student choice of #PEC2022 and we are ecstatc to host!

Our first keynote speaker: Dr. Amy Keating (<a href="/keating_lab/">Keating Lab</a>). Interested in protein interaction specificity, Dr. Keating highlights the power of data-driven computational exploration of protein interactions. Dr. Keating was our student choice of #PEC2022 and we are ecstatc to host!
Alex J Li (@alex_j_li) 's Twitter Profile Photo

First twitter thread🧵and also my first BioRxiv preprint! I’m excited to finally release my undergrad work into the world: combining GNNs, Potts models, and Tertiary Motifs (TERMs) for protein design! See the preprint here: biorxiv.org/content/10.110… 1/

PRX Life (@prx_life) 's Twitter Profile Photo

A self-supervised approach aligning protein sequence and structure spaces enables efficient binder screening with only backbone structural information — a powerful asset for early-stage protein binder design. 🔗 go.aps.org/3UY7OVe

A self-supervised approach aligning protein sequence and structure spaces enables efficient binder screening with only backbone structural information — a powerful asset for early-stage protein binder design.

🔗 go.aps.org/3UY7OVe