{"product_id":"hydrodynamic-analysis-of-groucho-q-domain-physical-biochemistry-techniques-reveals-an-unexpected-shape-3843374236","title":"Hydrodynamic Analysis of Groucho Q-Domain: Physical Biochemistry techniques reveals an unexpected shape","description":"\u003cp\u003e\u003cstrong\u003eISBN:\u003c\/strong\u003e 3843374236\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eAuthor:\u003c\/strong\u003e Kuo, Dennis\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eCondition:\u003c\/strong\u003e New\u003c\/p\u003e\u003cp\u003eThe Groucho (Gro)\/Transducin-like-enhancer of split (TLE) family of corepressors plays a significant role in the regulation of many cellular processes. Having no intrinsic DNA-binding activity, Gro\/TLE interacts with various DNA-bound repressor proteins to repress transcription. Gro\/TLE possesses a conserved region known as the Q-domain, and this region has been shown to direct the oligomerization of Gro\/TLE, which is required for repression. Although the Q-domain is required for oligomerization, its structural properties have never been fully characterized. Here, the Q-domain was tagged with a small ubiquitin-related modifier protein (SUMO) to alleviate aggregation observed with the untagged Q-domain. Size exclusion chromatography (Gel Filtration) and analytical ultracentrifugations were performed. Results show that SUMO-Q oligomerizes predominantly as a tetramer. However, significant heterogeneity is observed at high salt concentrations. Analysis of the hydrodynamic data suggest a markedly non-spherical structure.\u003c\/p\u003e","brand":"Mia Karts","offers":[{"title":"Default Title","offer_id":68099280896288,"sku":"NEW3843374236","price":73.33,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0980\/7426\/3840\/files\/51M4r4iH7OS.jpg?v=1793647842","url":"https:\/\/miakarts.com\/products\/hydrodynamic-analysis-of-groucho-q-domain-physical-biochemistry-techniques-reveals-an-unexpected-shape-3843374236","provider":"Miakarts Books","version":"1.0","type":"link"}