Phase Transitions in a Symmetry-Conserving Framework

Phase transitions are often associated with the breaking of a symmetry in the low-temperature phase described by non-vanishing values of certain order parameters. However, in finite-size systems the correlated equilibrium configuration preserves the symmetries of the underlying Hamiltonian. We discuss a method to calculate the statistical distribution of the order parameters without breaking the corresponding symmetries. The maxima of these statistical distributions mimic the phase transitions that are found in a mean-field approximation. We demonstrate the method for the case of shape transitions in atomic nuclei

Investigation of active regions at high resolution by balloon flights of the Solar Optical Universal Polarimeter (SOUP)

SOUP is a versatile, visible-light solar observatory, built for space or balloon flight. It is designed to study magnetic and velocity fields in the solar atmosphere with high spatial resolution and temporal uniformity, which cannot be achieved from the surface of the earth. The SOUP investigation is carried out by the Lockheed Palo Alto Research Laboratory, under contract to NASA's Marshall Space Flight Center. Co-investigators include staff members at a dozen observatories and universities in the U.S. and Europe. The primary objectives of the SOUP experiment are: to measure vector magnetic and velocity fields in the solar atmosphere with much better spatial resolution than can be achieved from the ground; to study the physical processes that store magnetic energy in active regions and the conditions that trigger its release; and to understand how magnetic flux emerges, evolves, combines, and disappears on spatial scales of 400 to 100,000 km. SOUP is designed to study intensity, magnetic, and velocity fields in the photosphere and low chromosphere with 0.5 arcsec resolution, free of atmospheric disturbances. The instrument includes: a 30 cm Cassegrain telescope; an active mirror for image stabilization; broadband film and TV cameras; a birefringent filter, tunable over 5100 to 6600 A with 0.05 A bandpass; a 35 mm film camera and a digital CCD camera behind the filter; and a high-speed digital image processor

Mapping the Two-Component Atomic Fermi Gas to the Nuclear Shell-Model

The physics of a two-component cold fermi gas is now frequently addressed in laboratories. Usually this is done for large samples of tens to hundreds of thousands of particles. However, it is now possible to produce few-body systems (1-100 particles) in very tight traps where the shell structure of the external potential becomes important. A system of two-species fermionic cold atoms with an attractive zero-range interaction is analogous to a simple model of nucleus in which neutrons and protons interact only through a residual pairing interaction. In this article, we discuss how the problem of a two-component atomic fermi gas in a tight external trap can be mapped to the nuclear shell model so that readily available many-body techniques in nuclear physics, such as the Shell Model Monte Carlo (SMMC) method, can be directly applied to the study of these systems. We demonstrate an application of the SMMC method by estimating the pairing correlations in a small two-component Fermi system with moderate-to-strong short-range two-body interactions in a three-dimensional harmonic external trapping potential.Comment: 13 pages, 3 figures. Final versio

Evolution of Broader Impacts

This work is supported by the National Science Foundation under grant number OIA-1810732 and MCB-1940655, the Kavli Foundation and the Burroughs Wellcome Fund. Any opinions, findings, and conclusions or recommendations expressed in this material are those of the author(s) and do not necessarily reflect the views of the National Science Foundation, the Kavli Foundation or Burroughs Wellcome Fund

Discovery of High-Affinity Protein Binding Ligands – Backwards

BACKGROUND: There is a pressing need for high-affinity protein binding ligands for all proteins in the human and other proteomes. Numerous groups are working to develop protein binding ligands but most approaches develop ligands using the same strategy in which a large library of structured ligands is screened against a protein target to identify a high-affinity ligand for the target. While this methodology generates high-affinity ligands for the target, it is generally an iterative process that can be difficult to adapt for the generation of ligands for large numbers of proteins. METHODOLOGY/PRINCIPAL FINDINGS: We have developed a class of peptide-based protein ligands, called synbodies, which allow this process to be run backwards--i.e. make a synbody and then screen it against a library of proteins to discover the target. By screening a synbody against an array of 8,000 human proteins, we can identify which protein in the library binds the synbody with high affinity. We used this method to develop a high-affinity synbody that specifically binds AKT1 with a K(d)<5 nM. It was found that the peptides that compose the synbody bind AKT1 with low micromolar affinity, implying that the affinity and specificity is a product of the bivalent interaction of the synbody with AKT1. We developed a synbody for another protein, ABL1 using the same method. CONCLUSIONS/SIGNIFICANCE: This method delivered a high-affinity ligand for a target protein in a single discovery step. This is in contrast to other techniques that require subsequent rounds of mutational improvement to yield nanomolar ligands. As this technique is easily scalable, we believe that it could be possible to develop ligands to all the proteins in any proteome using this approach

SIMS: A Hybrid Method for Rapid Conformational Analysis

Proteins are at the root of many biological functions, often performing complex tasks as the result of large changes in their structure. Describing the exact details of these conformational changes, however, remains a central challenge for computational biology due the enormous computational requirements of the problem. This has engendered the development of a rich variety of useful methods designed to answer specific questions at different levels of spatial, temporal, and energetic resolution. These methods fall largely into two classes: physically accurate, but computationally demanding methods and fast, approximate methods. We introduce here a new hybrid modeling tool, the Structured Intuitive Move Selector (SIMS), designed to bridge the divide between these two classes, while allowing the benefits of both to be seamlessly integrated into a single framework. This is achieved by applying a modern motion planning algorithm, borrowed from the field of robotics, in tandem with a well-established protein modeling library. SIMS can combine precise energy calculations with approximate or specialized conformational sampling routines to produce rapid, yet accurate, analysis of the large-scale conformational variability of protein systems. Several key advancements are shown, including the abstract use of generically defined moves (conformational sampling methods) and an expansive probabilistic conformational exploration. We present three example problems that SIMS is applied to and demonstrate a rapid solution for each. These include the automatic determination of ﾑﾑactiveﾒﾒ residues for the hinge-based system Cyanovirin-N, exploring conformational changes involving long-range coordinated motion between non-sequential residues in Ribose- Binding Protein, and the rapid discovery of a transient conformational state of Maltose-Binding Protein, previously only determined by Molecular Dynamics. For all cases we provide energetic validations using well-established energy fields, demonstrating this framework as a fast and accurate tool for the analysis of a wide range of protein flexibility problems

The deformation dependence of level densities in the configuration-interaction shell model

The auxiliary-field quantum Monte Carlo (AFMC) method has enabled the microscopic calculation of nuclear level densities from the underlying Hamil- tonian. However, AFMC is applied within the rotationally invariant framework of the configuration-interaction (CI) shell model, while deformation arises in the framework of a mean-field approximation that breaks rotational invariance. We review a recent method to study deformation in the CI shell model without invoking a mean-field approximation. Using a Landau-like expansion of the logarithm of the distribution of the quadrupole deformation tensor in the so- called quadrupole invariants, we determine the dependence of this distribution on intrinsic deformation. We can then calculate the dependence of nuclear state densities on intrinsic deformation. The method is demonstrated for a chain of even-mass samarium nuclei