Hydrodynamic Radii of Intrinsically Disordered Proteins Determined from Experimental Polyproline II Propensities.
The properties of disordered proteins are thought to depend on intrinsic conformational propensities for polyproline II (PPII) structure. While intrinsic PPII propensities have been measured for the common biological amino acids in short peptides, the ability of these experimentally determined prope...
Main Authors: | Maria E Tomasso, Micheal J Tarver, Deepa Devarajan, Steven T Whitten |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2016-01-01
|
Series: | PLoS Computational Biology |
Online Access: | http://europepmc.org/articles/PMC4699819?pdf=render |
Similar Items
-
Prediction of polyproline II secondary structure propensity in proteins
by: Kevin T. O’Brien, et al.
Published: (2020-01-01) -
Glycine in Water Favors the Polyproline II State
by: Brian Andrews, et al.
Published: (2020-07-01) -
Do polyproline II helix associations modulate biomolecular condensates?
by: Miguel Mompeán, et al.
Published: (2021-09-01) -
The Synthesis of Fluorous Polyproline Peptides
by: Huang, Chun Yi, et al.
Published: (2017) -
Plant Polypeptide Hormone Systemin Prefers Polyproline II Conformation in Solution
by: Saikat Dutta Chowdhury, et al.
Published: (2017-10-01)