sokrypton / GREMLIN
GREMLIN is a method to learn a statistical model of a protein family that captures both conservation and co-evolution patterns in the family. The strength of measured co-evolution is strongly predictive of residue-residue contacts in the 3D structure of the protein.
☆19Updated 8 years ago
Alternatives and similar repositories for GREMLIN:
Users that are interested in GREMLIN are comparing it to the libraries listed below
- Tutorial files☆11Updated 6 months ago
- Novel estimator for the change in stability upon point mutation in monomeric and multimeric proteins.☆41Updated 2 months ago
- Fraction of Common Contacts Clustering Algorithm for Protein Structures☆26Updated 3 years ago
- PyDock Tutorial☆30Updated 6 years ago
- HyperMPNN ‒ A general strategy to design thermostable proteins learned from hyperthermophiles☆48Updated this week
- Data sharing for High-throughput Prediction of Changes in Protein Conformational Distributions with Subsampled AlphaFold2☆38Updated 9 months ago
- ☆36Updated last year
- Rosetta FunFolDes – a general framework for the computational design of functional proteins.☆19Updated 5 years ago
- ☆52Updated 10 months ago
- Python tool for the discovery of similar 3D structural motifs across protein structures.☆26Updated last year
- Making Protein folding accessible to all!☆21Updated last year
- An accurate and efficient protein sequence design approach☆22Updated last year
- This repository contains the AlphaCutter.py for the removal of non-globular regions from predicted protein structures.☆15Updated last year
- De novo design of small molecule binding sites into proteins☆13Updated 3 years ago
- Implementation of Protein Invariant Point Packer (PIPPack)☆32Updated 8 months ago
- ☆33Updated last month
- ☆13Updated 3 years ago
- ☆80Updated 4 months ago
- Automated construction of protein chimeras and their analysis.☆14Updated last year
- Extension of ThermoMPNN for double mutant predictions☆24Updated last month
- Code for humanization of antibody and nanobody☆35Updated 2 months ago
- An open-source library for the analysis of protein interactions.☆29Updated 3 years ago
- a fast and accurate physical energy function extended from EvoEF for protein sequence design☆25Updated last year
- Active Learning-Assisted Directed Evolution for Protein Engineering☆37Updated 3 months ago
- Efficient manipulation of protein structures in Python☆51Updated 3 months ago
- ☆25Updated 3 years ago
- Fast and accurate protein domain segmentation using Invariant Point Attention☆33Updated 2 months ago
- ☆19Updated 2 years ago