about
The Nedd4-1 WW Domain Recognizes the PY Motif Peptide through Coupled Folding and Binding EquilibriaSignaling States of a Short Blue-Light Photoreceptor Protein PpSB1-LOV Revealed from Crystal Structures and Solution NMR SpectroscopyData describing the solution structure of the WW3* domain from human Nedd4-1Multiple WW domains of Nedd4-1 undergo conformational exchange that is quenched upon peptide binding.Structure and interaction of Corynebacterium pseudotuberculosis cold shock protein A with Y-box single-stranded DNA fragment.Molecular Dynamics Simulations Reveal Key Roles of the Interleukin-6 Alpha Receptor in the Assembly of the Human Interleukin-6 Receptor Complex.1H, 13C, and 15N backbone and sidechain resonance assignments of a monomeric variant of E. coli deoxyribose-5-phosphate aldolase.Conformational Sampling of the Intrinsically Disordered C-Terminal Tail of DERA Is Important for Enzyme CatalysisProline Restricts Loop I Conformation of the High Affinity WW Domain from Human Nedd4-1 to a Ligand Binding-Competent Type I β-Turn
P50
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P50
description
researcher
@en
wetenschapper
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հետազոտող
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name
Vineet Panwalkar
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Vineet Panwalkar
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Vineet Panwalkar
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Vineet Panwalkar
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Vineet Panwalkar
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type
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Vineet Panwalkar
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Vineet Panwalkar
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Vineet Panwalkar
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Vineet Panwalkar
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Vineet Panwalkar
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Vineet Panwalkar
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Vineet Panwalkar
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Vineet Panwalkar
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Vineet Panwalkar
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Vineet Panwalkar
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P106
P31
P496
0000-0003-1621-1606