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Proline Fingerprint in Intrinsically Disordered Proteins
Author(s) -
Murrali Maria Grazia,
Piai Alessandro,
Bermel Wolfgang,
Felli Isabella C.,
Pierattelli Roberta
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800172
Subject(s) - proline , intrinsically disordered proteins , chemistry , nuclear magnetic resonance spectroscopy , amino acid , polyproline helix , two dimensional nuclear magnetic resonance spectroscopy , computational biology , biochemistry , crystallography , biology , stereochemistry , peptide
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.