186 research outputs found
Realization of a Resonant Fermi Gas with a Large Effective Range
We have measured the interaction energy and three-body recombination rate for
a two-component Fermi gas near a narrow Feshbach resonance and found both to be
strongly energy dependent. Even for deBroglie wavelengths greatly exceeding the
van der Waals length scale, the behavior of the interaction energy as a
function of temperature cannot be described by atoms interacting via a contact
potential. Rather, energy-dependent corrections beyond the scattering length
approximation are required, indicating a resonance with an anomalously large
effective range. For fields where the molecular state is above threshold, the
rate of three-body recombination is enhanced by a sharp, two-body resonance
arising from the closed-channel molecular state which can be magnetically tuned
through the continuum. This narrow resonance can be used to study strongly
correlated Fermi gases that simultaneously have a sizeable effective range and
a large scattering length.Comment: to appear in Phys. Rev. Let
Three-body recombination in a three-state Fermi gas with widely tunable interactions
We investigate the stability of a three spin state mixture of ultracold
fermionic Li atoms over a range of magnetic fields encompassing three
Feshbach resonances. For most field values, we attribute decay of the atomic
population to three-body processes involving one atom from each spin state and
find that the three-body loss coefficient varies by over four orders of
magnitude. We observe high stability when at least two of the three scattering
lengths are small, rapid loss near the Feshbach resonances, and two unexpected
resonant loss features. At our highest fields, where all pairwise scattering
lengths are approaching , we measure a three-body loss
coefficient and a trend
toward lower decay rates for higher fields indicating that future studies of
color superfluidity and trion formation in a SU(3) symmetric Fermi gas may be
feasible
Changes in Dynamics upon Oligomerization Regulate Substrate Binding and Allostery in Amino Acid Kinase Family Members
Oligomerization is a functional requirement for many proteins. The interfacial interactions and the overall packing geometry of the individual monomers are viewed as important determinants of the thermodynamic stability and allosteric regulation of oligomers. The present study focuses on the role of the interfacial interactions and overall contact topology in the dynamic features acquired in the oligomeric state. To this aim, the collective dynamics of enzymes belonging to the amino acid kinase family both in dimeric and hexameric forms are examined by means of an elastic network model, and the softest collective motions (i.e., lowest frequency or global modes of motions) favored by the overall architecture are analyzed. Notably, the lowest-frequency modes accessible to the individual subunits in the absence of multimerization are conserved to a large extent in the oligomer, suggesting that the oligomer takes advantage of the intrinsic dynamics of the individual monomers. At the same time, oligomerization stiffens the interfacial regions of the monomers and confers new cooperative modes that exploit the rigid-body translational and rotational degrees of freedom of the intact monomers. The present study sheds light on the mechanism of cooperative inhibition of hexameric N-acetyl-L-glutamate kinase by arginine and on the allosteric regulation of UMP kinases. It also highlights the significance of the particular quaternary design in selectively determining the oligomer dynamics congruent with required ligand-binding and allosteric activities
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