The Structure of the Nucleon: Elastic Electromagnetic Form Factors

Precise proton and neutron form factor measurements at Jefferson Lab, using spin observables, have recently made a significant contribution to the unraveling of the internal structure of the nucleon. Accurate experimental measurements of the nucleon form factors are a test-bed for understanding how the nucleon's static properties and dynamical behavior emerge from QCD, the theory of the strong interactions between quarks. There has been enormous theoretical progress, since the publication of the Jefferson Lab proton form factor ratio data, aiming at reevaluating the picture of the nucleon. We will review the experimental and theoretical developments in this field and discuss the outlook for the future.Comment: arXiv admin note: text overlap with arXiv:1301.0905, arXiv:hep-ph/0609004, arXiv:1411.6908 by other author

Insights from the x-ray crystal structure of coral 8R-lipoxygenase: Calcium activation via a C2-like domain and a structural basis of product chirality

Lipoxygenases (LOXs) catalyze the regio- and stereospecific dioxygenation of polyunsaturated membrane-embedded fatty acids. We report here the 3.2 Å resolution structure of 8R-LOX from the Caribbean sea whip coral Plexaura homomalla, a LOX isozyme with calcium dependence and the uncommon R chiral stereospecificity. Structural and spectroscopic analyses demonstrated calcium binding in a C2-like membrane-binding domain, illuminating the function of similar amino acids in calcium-activated mammalian 5-LOX, the key enzyme in the pathway to the pro-inflammatory leukotrienes. Mutation of Ca2+- ligating amino acids in 8R-LOX resulted not only in a diminished capacity to bind membranes, as monitored by fluorescence resonance energy transfer, but also in an associated loss of Ca2+-regulated enzyme activity. Moreover, a structural basis for R chiral specificity is also revealed; creation of a small oxygen pocket next to Gly428 (Ala in all S-LOX isozymes) promoted C-8 oxygenation with R chirality on the activated fatty acid substrate. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc

Electroexcitation of the P33(1232), P11(1440), D13(1520), S11(1535) at Q^2=0.4 and 0.65(GeV/c)^2

Using two approaches: dispersion relations and isobar model, we have analyzed recent high precision CLAS data on cross sections of \pi^0, \pi^+, and \eta electroproduction on protons, and the longitudinally polarized electron beam asymmetry for p(\vec{e},e'p)\pi^0 and p(\vec{e},e'n)\pi^+. The contributions of the resonances P33(1232), P11(1440), D13(1520), S11(1535) to \pi electroproduction and S11(1535) to \eta electroproduction are found. The results obtained in the two approaches are in good agreement with each other. There is also good agreement between amplitudes of the \gamma^* N \to S11(1535) transition found in \pi and \eta electroproduction. For the first time accurate results are obtained for the longitudinal amplitudes of the P11(1440), D13(1520) and S11(1535) electroexcitation on protons.Comment: 9 pages, 9 figure

Subdiffusion and weak ergodicity breaking in the presence of a reactive boundary

We derive the boundary condition for a subdiffusive particle interacting with a reactive boundary with finite reaction rate. Molecular crowding conditions, that are found to cause subdiffusion of larger molecules in biological cells, are shown to effect long-tailed distributions with identical exponent for both the unbinding times from the boundary to the bulk and the rebinding times from the bulk. This causes a weak ergodicity breaking: typically, an individual particle either stays bound or remains in the bulk for very long times. We discuss why this may be beneficial for in vivo gene regulation by DNA-binding proteins, whose typical concentrations are nanomolarComment: 4 pages, 1 figure, REVTeX4, accepted to Phys Rev Lett, some typos correcte

Crystal structure of a lipoxygenase in complex with substrate: The arachidonic acid-binding site of 8R-lipoxygenase

Lipoxygenases (LOX) play critical roles in mammalian biology in the generation of potent lipid mediators of the inflammatory response; consequently, they are targets for the development of isoform-specific inhibitors. The regio- and stereo-specificity of the oxygenation of polyunsaturated fatty acids by the enzymes is understood in terms of the chemistry, but structural observation of the enzyme-substrate interactions is lacking. Although several LOX crystal structures are available, heretofore the rapid oxygenation of bound substrate has precluded capture of the enzyme-substrate complex, leaving a gap between chemical and structural insights. In this report, we describe the 2.0 Å resolution structure of 8R-LOX in complex with arachidonic acid obtained under anaerobic conditions. Subtle rearrangements, primarily in the side chains of three amino acids, allow binding of arachidonic acid in a catalytically competent conformation. Accompanying experimental work supports a model in which both substrate tethering and cavity depth contribute to positioning the appropriate carbon at the catalytic machinery