{"product_id":"observing-residual-structure-in-disordered-peptides-von-joshua-lessing","title":"Observing residual structure in disordered peptides","description":"\u003cp\u003eAn estimated 35% of the human proteome is intrinsically disordered. Disordered proteins  play a key role in physiologic and pathologic regulation, recognition, and signaling making protein disorder the subject of increasing investigation. Since disordered samples do not generate x-ray quality crystals and since they have conformations that interconvert faster than the time resolution of NMR or ESR, little is known about their structure or function. By combining isotope-edited two-dimensional infrared spectroscopy (2D IR) with spectral modeling based on molecular dynamics simulations, this work will show that one can measure the residual structure and conformational heterogeneity of a putatively disordered sequence.\u003c\/p\u003e\u003cdiv class=\"aw-variant-hidden-subtitle-div\" id=\"aw-variant-subtitle-9783659545764\"\u003e\u003ch3\u003e\u003c\/h3\u003e\u003c\/div\u003e","brand":"Autorenwelt Shop","offers":[{"title":"Softcover - 9783659545764","offer_id":39467431460957,"sku":"9783659545764","price":55.9,"currency_code":"EUR","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0940\/0622\/files\/03f43825-e9bf-44c7-ae21-edc109998147.jpg?v=1773122274","url":"https:\/\/shop.autorenwelt.de\/products\/observing-residual-structure-in-disordered-peptides-von-joshua-lessing","provider":"Autorenwelt Shop","version":"1.0","type":"link"}