Structural, stability, dynamic and binding properties of the ALS-causing T46I mutant of the hVAPB MSP domain as revealed by NMR and MD simulations
10.1371/journal.pone.0027072
Saved in:
Main Authors: | Lua, S., Qin, H., Lim, L., Shi, J., Gupta, G., Song, J. |
---|---|
Other Authors: | BIOLOGICAL SCIENCES |
Format: | Article |
Published: |
2014
|
Online Access: | http://scholarbank.nus.edu.sg/handle/10635/77063 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | National University of Singapore |
Similar Items
-
Elimination of the native structure and solubility of the hVAPB MSP domain by the Pro56Ser mutation that causes amyotrophic lateral sclerosis
by: Shi, J., et al.
Published: (2011) -
ALS-causing P56S mutation and splicing variation on the hVAPB MSP domain transform its β-sandwich fold into lipid-interacting helical conformations
by: Qin, H., et al.
Published: (2014) -
Intrinsically unstructured domain 3 of hepatitis C virus NS5A forms a "fuzzy complex" with VAPB-MSP domain which carries ALS-causing mutations
by: Gupta, G., et al.
Published: (2014) -
Unique Structure and Dynamics of the EphA5 Ligand Binding Domain Mediate Its Binding Specificity as Revealed by X-ray Crystallography, NMR and MD Simulations
by: Huan, X., et al.
Published: (2014) -
Protein dynamics at Eph receptor-ligand interfaces as revealed by crystallography, NMR and MD simulations
by: Qin, H., et al.
Published: (2014)