Determination of Oligomeric State of Proteins in Solution from Pulsed-Field-Gradient Self-Diffusion Coefficient Measurements. A Comparison of Experimental, Theoretical, and Hard-Sphere Approximated Values

Structure and Inter-domain Interactions of Domain II from the Blood-stage Malarial Protein, Apical Membrane Antigen 1

“…35 Moreover, no obvious changes in line widths and chemical shifts were evident in 1D and 2D NMR spectra over this range of protein concentration. The average value of 1.1!10 K10 m 2 s K1 for domain II is close to published translational diffusion coefficients for lysozyme (14.1 kDa) and dimeric monocyte chemotactic protein-1 (17.4 kDa), 36 indicating that its hydrodynamic properties are similar to those of other globular proteins of similar mass, and therefore that its structure is reasonably compact.…”

A Bimodal Distribution of Two Distinct Categories of Intrinsically Disordered Structures with Separate Functions in FG Nucleoporins

“…Self-diffusion coefficient measurements were obtained using a BPP-SED (bipolar gradient pulse pair selective echo dephasing) sequence (42). Translational diffusion tensor values were calculated based on the bead model approximation method (43) used successfully to calculate translational and rotational diffusion tensors of proteins (44,45). All atoms were considered as beads of equal size ( ϭ 5.1 Å).…”

Measuring protein self-diffusion in protein–protein mixtures using a pulsed gradient spin-echo technique with WATERGATE and isotope filtering

“…Measuring the dependence of the diffusion coefficient on concentration, pH or diffusion time can yield detailed information about the association process, e.g., estimation of association constants, life time of associates, etc. [17][18][19][20][21][22][23]. Because diffusion measurements can be performed relatively quickly, they can be easily done in conjunction with initial HSQC titration studies.…”