Atomic resolution view into the structure-function relationships of the human myelin peripheral membrane protein P2

Keyphrases

• Structure Function 100%
• Atomic Resolution 100%
• Myelin 100%
• Peripheral Membrane Protein 100%
• Fatty Acids 66%
• Conformational Change 66%
• Peripheral Nerve 66%
• Major Components 33%
• Ultra-high Resolution 33%
• Repeated Distances 33%
• Preferred Orientation 33%
• Functional Perspective 33%
• Carboxyl Group 33%
• Phospholipid Membrane 33%
• Arginine Residue 33%
• Positively Charged Surface 33%
• Cultured Cells 33%
• Protonation State 33%
• Lipid Transport 33%
• Hydrogen Bond Network 33%
• Internal Hydrogen 33%
• Transmembrane Domain 33%
• Vertebrates 33%
• Barrel Structure 33%
• Domain Formation 33%
• Ligand Transfer 33%
• Induced Membrane 33%
• Membrane Interaction 33%
• Anion Binding Site 33%
• Structural Perspective 33%
• Fatty Acid Binding Protein 33%
• Double Bilayer 33%

Biochemistry, Genetics and Molecular Biology

• Structure Activity Relation 100%
• Peripheral Membrane Protein 100%
• Myelin 100%
• Conformational Change 66%
• Wild Type 33%
• Lipid Transport 33%
• Fatty Acid-Binding Protein 33%
• Protonation 33%
• Binding Site 33%
• Phospholipid Membrane 33%
• Arginine 33%