Oliver Bieri | PubMed Health

PubMed2006

Oscillating steady states.

The signal formation and properties of steady-state free precession (SSFP) in combination with alternating RF pulse phases or alternating spin precession is analyzed. Simulations and experiments demonstrate that the amplitudes of SSFP echo paths are significantly influenced by application of alternating phases either via the exciting RF pulse or via some external mechanism producing alternating spin precession. The influence of alternating phases on echo amplitudes is different for different echo paths. The primary SSFP echo paths F(0) (-) and F(0) (+) exhibit a signal reduction whereas higher-order echoes F(-1) (-) and F(1) (+) show a signal increase upon application of oscillating phases. This behavior can be described using a simple perturbation theory applied to the frequency response profile of balanced SSFP combined with a final signal integration over one balanced SSFP band. The high sensitivity of SSFP echo amplitudes to alternating RF pulse phases or precession is exemplarily used to detect and visualize propagating transverse acoustic shear waves. Detection of flow or alternating currents are further possibilities to apply this unique feature of SSFP.

Magnetic Resonance Imaging↗

PubMed2003

Dynamics of unfolded polypeptide chains as model for the earliest steps in protein folding.

The rate of formation of intramolecular interactions in unfolded proteins determines how fast conformational space can be explored during folding. Characterization of the dynamics of unfolded proteins is therefore essential for the understanding of the earliest steps in protein folding. We used triplet-triplet energy transfer to measure formation of intrachain contacts in different unfolded polypeptide chains. The time constants (1/k) for contact formation over short distances are almost independent of chain length, with a maximum value of about 5 ns for flexible glycine-rich chains and of 12 ns for stiffer chains. The rates of contact formation over longer distances decrease with increasing chain length, indicating different rate-limiting steps for motions over short and long chain segments. The effect of the amino acid sequence on local chain dynamics was probed by using a series of host-guest peptides. Formation of local contacts is only sixfold slower around the stiffest amino acid (proline) compared to the most flexible amino acid (glycine). Good solvents for polypeptide chains like EtOH, GdmCl and urea were found to slow intrachain diffusion and to decrease chain stiffness. These data allow us to determine the time constants for formation of the earliest intrachain contacts during protein folding.

Amino Acid Sequence↗