Abstract
Membrane proteins are challenging to study and restraints for structure determination are typically sparse or of low resolution because the membrane environment that surrounds them leads to a variety of experimental challenges. When membrane protein structures are determined by different techniques in different environments, a natural question is “which structure is most biologically relevant?” Towards answering this question, we compiled a dataset of membrane proteins with known structures determined by both solution NMR and X-ray crystallography. By investigating differences between the structures, we found that RMSDs between crystal and NMR structures are below 5 Å in the membrane region, NMR ensembles have a higher convergence in the membrane region, crystal structures typically have a straighter transmembrane region, have higher stereo-chemical correctness, and are more tightly packed. After quantifying these differences, we used high-resolution refinement of the NMR structures to mitigate them, which paves the way for identifying and improving the structural quality of membrane proteins.
Original language | English (US) |
---|---|
Pages (from-to) | 57-74 |
Number of pages | 18 |
Journal | Proteins: Structure, Function and Bioinformatics |
Volume | 86 |
Issue number | 1 |
DOIs | |
State | Published - Jan 2018 |
Keywords
- Rosetta software
- membrane proteins
- protein modeling
- protein structure
- structural quality
- structure refinement
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Molecular Biology