The use of residual dipolar couplings (RDCs) in the analysis of biomolecular structure and
dynamics has expanded rapidly since its potential as a source of structural information on …

DnaK is the canonical Hsp70 molecular chaperone protein from Escherichia coli. Like other
Hsp70s, DnaK comprises two main domains: a 44-kDa N-terminal nucleotide-binding …

Proteins with intrinsically disordered domains are implicated in a vast range of biological
processes, especially in cell signaling and regulation. Having solved the quaternary …

The tandem zinc finger (TZF) domain of the protein TIS11d binds to the class II AU-rich
element (ARE) in the 3′ untranslated region (3′ UTR) of target mRNAs and promotes their …

The measurement of residual dipolar couplings in weakly aligned proteins can potentially
provide unique information on their structure and dynamics in the solution state. The …

Partial molecular alignment leads to an incomplete averaging of anisotropic magnetic
interactions such as the magnetic dipole–dipole interaction, the chemical shift anisotropy, or …

Dissolving biological macromolecules in dilute bicelle solutions, which form oriented liquid
crystals in the presence of a magnetic field, permits measurement of anisotropic spin …

RasGRP1 and SOS are Ras-specific nucleotide exchange factors that have distinct roles in
lymphocyte development. RasGRP1 is important in some cancers and autoimmune …

Hsp70s (heat shock protein 70 kDa) are central to protein folding, refolding, and trafficking in
organisms ranging from archaea to Homo sapiens under both normal and stressed cellular …

The PNT (or Pointed) domain, present within a subset of the Ets family of transcription
factors, is structurally related to the larger group of SAM domains through a common tertiary …