Amanote Research
Register
Sign In
Hydration and Packing Along the Folding Pathway of SH3 Domains by Pressure-Dependent NMR
doi 10.1021/bi060177r.s001
Full Text
Open PDF
Abstract
Available in
full text
Date
Unknown
Authors
Unknown
Publisher
American Chemical Society (ACS)
Related search
Structural Characterization of a Ubiquitin Folding Intermediate by Pressure-Jump NMR
Biophysical Journal
Biophysics
Structural Basis for Ubiquitin Recognition by SH3 Domains
Journal of Molecular Biology
Structural Biology
Molecular Biology
Biophysics
Probing Pressure Effects on Core Packing of a Repeat Protein Using 13C NMR
Biophysical Journal
Biophysics
Initiation Sites of Protein Folding by NMR Analysis.
Proceedings of the National Academy of Sciences of the United States of America
Multidisciplinary
GTPase-activating Protein SH2-SH3 Domains Induce Gene Expression in a Ras-Dependent Fashion.
Molecular and Cellular Biology
Cell Biology
Molecular Biology
Distinct Ubiquitin Binding Modes Exhibited by Sh3 Domains: Molecular Determinants and Functional Implications
Cavities and Cooperativity in the Folding of the Leucine Rich Repeat Protein PP32: A Pressure-Jump Fluorescence and High Pressure NMR Study
Biophysical Journal
Biophysics
SH3 Domain Unfolding Pathway Studied by Protein Contact Network Model
International Journal of Digital Content Technology and its Applications
Ubiquitin Binds to and Regulates a Subset of SH3 Domains
Molecular Cell
Cell Biology
Molecular Biology