TGP, an extremely stable, non-aggregating fluorescent protein created by structure-guided surface engineering - PMC
In this paper we describe the engineering and X-ray crystal structure of Thermal Green Protein (TGP), an extremely stable, highly soluble, non-aggregating green fluorescent protein. TGP is a soluble variant of the fluorescent protein eCGP123, which ...
. Author manuscript; available in PMC: 2016 Jul 1. Published in final edited form as: Proteins. 2015 May 8;83(7):1225–1237. doi: 10.1002/prot.24699 Abstract In this paper we describe the engineering and X-ray crystal structure of Thermal Green Protein (TGP), an extremely stable, highly soluble, non-aggregating green fluorescent protein. TGP is a soluble variant of the fluorescent protein eCGP123, which despite being highly stable, has proven to be aggregation-prone. The X-ray crystal structure of eCGP123, also determined within the context of this paper, was used to carry out rational…
saved by
related reading
- The structure and physical properties of a packaged bacteriophage particlenature.com
- Technologies to measure and modulate protein subcellular localizationnature.com
- Coronavirus envelope protein - Wikipediaen.wikipedia.org
- TP-060 (CAS 2601393-20-6)caymanchem.com
- Glycosyltransferase Structure and Functionlink.springer.com
- PDB101: Molecule of the Month: PROTACs and Molecular Glue Degraderspdb101.rcsb.org
- Spontaneous and indefinite blinking in upconverting nanoparticles for ångström-precision multicolour super-resolution imaging | Nature Nanotechnologynature.com
- Highly accurate protein structure prediction with AlphaFoldnature.com
- Protein Magnetofluorescenceandrewgyork.github.io
- Development of a targeted BioPROTAC degrader selective for misfolded SOD1nature.com
- The solution NMR structure of a blue-green algae hepatotoxin, microcystin-RR--a comparison with the structure of microcystin-LR - PubMedpubmed.ncbi.nlm.nih.gov
- Multiscale Ensemble Modeling of Intrinsically Disordered Proteins: p53 N-Terminal Domain - PMCncbi.nlm.nih.gov