Proline Fingerprint in Intrinsically Disordered Proteins. (21st June 2018)

• Record Type: Journal Article
• Authors: Murrali, Maria Grazia; Piai, Alessandro; Bermel, Wolfgang; Felli, Isabella C.; Pierattelli, Roberta
• Is Part Of: Chembiochem. Volume 19:Number 15(2018)
• Page Start: 1625
• Page End: 1629
• Publication Date: 2018-06-21
• Subjects: 13C NMR spectroscopy -- intrinsically disordered proteins -- protein dynamics -- NMR spectroscopy -- proline; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201800172
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract: NMR spectroscopy is one of the main techniques used for high‐resolution studies of intrinsically disordered proteins (IDPs), permitting mapping of the structural and dynamic features of all the amino acids constituting the polypeptide at atomic resolution. Only proline residues are less straightforward to characterize because they lack any amide proton, thus rendering them not directly visible in the commonly used 2D 1 H, 15 N correlation experiments. However, proline residues are highly abundant in IDPs and can mediate important functions. In this work we present an easy and effective way to obtain fingerprints of proline residues in IDPs at high resolution. Abstract : Capturing proline residues : Proline residues' signals are not directly visible in commonly used NMR experiments and often escape investigation. We propose here an effective tool for capturing their features by exploiting 13 C direct‐detection NMR spectroscopy.