Ion Mobility Mass Spectrometry Uncovers the Impact of the Patterning of Oppositely Charged Residues on the Conformational Distributions of Intrinsically Disordered Proteins

Keyphrases

• Charged Residue 100%
• Oppositely Charged 100%
• Intrinsically Disordered Proteins 100%
• Conformational Distribution 100%
• Ion Mobility Spectrometry 100%
• State of Charge 50%
• Salt Concentration 33%
• Conformational Heterogeneity 33%
• Solvation 33%
• Solvate 33%
• Linear Segregation 33%
• Charge Patterning 33%
• Molecular Dynamics Simulation 16%
• Conformational Fluctuations 16%
• Amino Acid Composition 16%
• Gas Phase 16%
• Evenly Distributed 16%
• Conformational States 16%
• Intra-chain 16%
• Intrinsically Disordered Region 16%
• Inhibitory Proteins 16%
• Primary Sequence 16%
• Sensitivity to Change 16%
• P27Kip1 16%
• Collision Cross Section 16%
• Type Sequences 16%
• Global Dimension 16%
• Linear Mixture 16%
• Narrow Distribution 16%

Biochemistry, Genetics and Molecular Biology

• Wild Type 100%
• Intrinsically Disordered Protein 100%
• Ion Mobility Mass Spectrometry 100%
• Solution and Solubility 50%
• Solvation 50%
• C-Terminus 25%
• Cell Cycle 25%
• Amino Acid Composition 25%
• CDKN1B 25%

Chemistry

• Ion Mobility Mass Spectrometry 100%
• Solvation 66%
• State-of-Charge 66%
• Collisional 33%
• Amino Acid Composition 33%
• Molecular Dynamics Simulation 33%