Thermodynamic, structural and functional properties of membrane protein inclusion bodies are analogous to purified counterparts: case study from bacteria and humans
about
Energetics of side-chain partitioning of β-signal residues in unassisted folding of a transmembrane β-barrel protein.Mitochondrial VDAC2 and cell homeostasis: highlighting hidden structural features and unique functionalities.Approaches for Preparation and Biophysical Characterization of Transmembrane β-Barrels
P2860
Thermodynamic, structural and functional properties of membrane protein inclusion bodies are analogous to purified counterparts: case study from bacteria and humans
description
im Jahr 2015 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована у 2015
@uk
name
Thermodynamic, structural and ...... study from bacteria and humans
@en
Thermodynamic, structural and ...... study from bacteria and humans
@nl
type
label
Thermodynamic, structural and ...... study from bacteria and humans
@en
Thermodynamic, structural and ...... study from bacteria and humans
@nl
prefLabel
Thermodynamic, structural and ...... study from bacteria and humans
@en
Thermodynamic, structural and ...... study from bacteria and humans
@nl
P2860
P50
P356
P1433
P1476
Thermodynamic, structural and ...... study from bacteria and humans
@en
P2093
Ankit Gupta
Deepti Chaturvedi
P2860
P304
P356
10.1039/C4RA11207E
P577
2015-01-01T00:00:00Z