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 H-1,N-15 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.

Proline Fingerprint in Intrinsically Disordered Proteins / Murrali, Maria Grazia; Piai, Alessandro; Bermel, Wolfgang; Felli, Isabella C.*; Pierattelli, Roberta. - In: CHEMBIOCHEM. - ISSN 1439-4227. - STAMPA. - 19:(2018), pp. 1625-1629. [10.1002/cbic.201800172]

Proline Fingerprint in Intrinsically Disordered Proteins

MURRALI, MARIA GRAZIA;Piai, Alessandro;Felli, Isabella C.
;
Pierattelli, Roberta
2018

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 H-1,N-15 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.
2018
19
1625
1629
Murrali, Maria Grazia; Piai, Alessandro; Bermel, Wolfgang; Felli, Isabella C.*; Pierattelli, Roberta
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/1135689
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