B. B. Kragelund

This study shows DNA binding alters the conformational dynamics and accessibility of the IDR in Sox2, affecting activation domains and transcription.

The paper revisits the use of dioxane as a reference compound in PFG NMR to determine protein hydrodynamic radius, finding the current reference value underestimated and proposing a new value.

The paper identifies a PIP-box motif in Spd1 that competes with another PCNA binding site to regulate checkpoint activation in yeast.

This study shows that the prolactin receptor forms a co-structure with JAK2 and PI(4,5)P2, enabling signal transduction by stabilizing the receptor's disordered domain.

This study determines the structure of TPH2's regulatory domain with L-Phe and shows it is a better ligand than L-Trp, revealing dynamic behavior in the tetramer.

This study compares the functional and structural differences between glutamate and aspartate in intrinsically disordered proteins using experimental and computational methods.

The paper evaluates models for calculating the hydrodynamic radius of intrinsically disordered proteins using conformational ensembles validated by small-angle X-ray scattering and finds the Kirkwood-Riseman equation to be the most accurate.

This paper introduces a method to design peptides that fold into single α-helices using glutamine side chain to main chain hydrogen bonds, enabling targeted interactions with globular proteins.

This study shows that monomeric α-synuclein activates the plasma membrane calcium pump (PMCA) in neurons, enhancing calcium expulsion through interactions with acidic phospholipids and membrane anchoring.

The paper compares force fields and methods for refining α-synuclein ensembles using SAXS data, showing that accurate ensembles require compatible simulations and experimental integration.

The paper identifies multiple NHE1:CaM complex states with varying stoichiometry and structure, showing how Ca2+ and phosphorylation regulate NHE1 activation.

This study determines the structure of the full-length human growth hormone receptor using integrated SAXS, X-ray diffraction, NMR, and molecular dynamics simulations, revealing a flexible ensemble of domains.