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Direct visualization of coexisting channels of interaction in CeSb.

ABSTRACT: Our understanding of correlated electron systems is vexed by the complexity of their interactions. Heavy fermion compounds are archetypal examples of this physics, leading to exotic properties that weave magnetism, superconductivity and strange metal behavior together. The Kondo semimetal CeSb is an unusual example where different channels of interaction not only coexist, but have coincident physical signatures, leading to decades of debate about the microscopic picture describing the interactions between the f moments and the itinerant electron sea. Using angle-resolved photoemission spectroscopy, we resonantly enhance the response of the Ce f electrons across the magnetic transitions of CeSb and find there are two distinct modes of interaction that are simultaneously active, but on different kinds of carriers. This study reveals how correlated systems can reconcile the coexistence of different modes on interaction-by separating their action in momentum space, they allow their coexistence in real space.

SUBMITTER: Jang S

PROVIDER: S-EPMC6397026 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature

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Direct visualization of coexisting channels of interaction in CeSb.

Jang Sooyoung S Kealhofer Robert R John Caolan C Doyle Spencer S Hong Ji-Sook JS Shim Ji Hoon JH Si Q Q Erten O O Denlinger Jonathan D JD Analytis James G JG

Science advances 20190301 3

Our understanding of correlated electron systems is vexed by the complexity of their interactions. Heavy fermion compounds are archetypal examples of this physics, leading to exotic properties that weave magnetism, superconductivity and strange metal behavior together. The Kondo semimetal CeSb is an unusual example where different channels of interaction not only coexist, but have coincident physical signatures, leading to decades of debate about the microscopic picture describing the interactio ...[more]

PMID: 30838325

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Project description:Bimolecular Fluorescence Complementation (BiFC) assay is a method used to directly visualize protein-protein interaction in vivo using live-cell imaging or fixed cells. This protocol described here is based on our recent paper describing the functional association of human chromatin adaptor and transcription cofactor Brd4 with p53 tumor suppressor protein (Wu et al., 2013). BiFC was first described by Hu et al. (2002) using two non-fluorescent protein fragments of enhanced yellow fluorescent protein (EYFP), which is an Aequorea victoria GFP variant protein, fused respectively to a Rel family protein and a bZIP family transcription factor to investigate interactions between these two family members in living cells. The YFP was later improved by introducing mutations to reduce its sensitivity to pH and chloride ions, thus generating a super-enhanced YFP, named Venus fluorescent protein, without showing diminished fluorescence at 37 °C as typically observed with EYFP (Nagai et al., 2006). The fluorescence signal is regenerated by complementation of two non-fluorescent fragments (e.g., the Venus N-terminal 1-158 amino acid residues, called Venus-N, and its C-terminal 159-239 amino acid residues, named Venus-C; see Figure 1A and Gully et al., 2012; Ding et al., 2006; Kerppola, 2006) that are brought together by interaction between their respective fusion partners (e.g., Venus-N to p53, and Venus-C to the PDID domain of human Brd4; see Figure 1B and 1C). The intensity and cellular location of the regenerated fluorescence signals can be detected by fluorescence microscope. The advantages of the proximity-based BiFC assay are: first, it allows a direct visualization of spatial and temporal interaction between two partner proteins in vivo; second, the fluorescence signal provides a sensitive readout for detecting protein-protein interaction even at a low expression level comparable to that of the endogenous proteins; third, the intensity of the fluorescence signal is proportional to the strength of protein-protein interaction (Morell et al., 2008); and fourth, the BiFC signals are derived from intrinsic protein-protein interaction, rather than from extrinsic fluorophores that may not reflect true protein-protein interaction due to their nonspecific association with cellular macromolecules or subcellular compartments. However, some limitations of BiFC include slow maturation (T1/2 ~ 1 h) of an eventually stable BiFC complex (Hu et al., 2002), making it unsuitable for real-time observation of transient interaction that disappears prior to BiFC detection, and enhanced BiFC background at high expression levels due to fusion-independent association between two non-fluorescent fragments association. BiFC signals generated by in vivo protein-protein interaction can be validated by amino acid mutation introduced at the protein-protein contact surfaces. This imaging technique has been widely used in different cell types and organisms (Kerppola, 2006).

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Direct visualization of coexisting channels of interaction in CeSb.

Publications

Direct visualization of coexisting channels of interaction in CeSb.

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