Structural models and Sort-seq data for: Packing of apolar amino acids is not a strong stabilizing force in transmembrane helix dimerization

The factors that stabilize the folding and oligomerization of membrane proteins are still not well understood. In particular, it remains unclear how the tight and complementary packing between apolar side chains observed in the core of membrane proteins contributes to their stability. Complementary packing is a necessary feature since packing defects are generally destabilizing for membrane proteins. The question is the extent to which packing of apolar side chains – and the resulting van der Waals interactions – is a sufficient driving force for stabilizing the interaction between transmembrane helices in the absence of hydrogen bonding and polar interactions. We addressed this question with an approach based on high-throughput protein design and the homodimerization of single-pass helices as the model system. We designed hundreds of transmembrane helix dimers mediated by apolar packing in the backbone configurations that are most commonly found in membrane proteins. We assessed the as..., , # Structural models and Sort-seq data for: Packing of apolar amino acids is not a strong stabilizing force in transmembrane helix dimerization

This repository contains data relative to Loiseau and Senes, bioRxiv article [https://doi.org/10.1101/2025.04.26.649789](https://doi.org/10.1101/2025.04.26.649789)

* Structural model of designed dimers (PDB files)
* Sort-seq Data

---

## Structural model of dimers (PDB files)

The compressed zip file contains the structural models of the designed transmembrane dimers. The file name corresponds to the constructs listed in Table S1: [G/R/L]_NNN.pdb, where

* G identifies the GAS-right dimers
* L the Left dimers
* R the Right dimers NNN is an integer serial number.

### File

* `structural_models.zip`

### Code/software

PDB files are viewable with PyMol or other software that can read Protein Data Bank coordinate files.

---

## NGS Data

Raw data from Next Generation Sequencing utilizing the TOXGREEN sort-seq methods as in Anderson et al., 2025...,