Defining Conformational Ensembles of Intrinsically Disordered and Partially Folded Proteins Directly from Chemical Shifts

• Published in: Journal of the American Chemical Society Vol. 132; no. 4; pp. 1270 - 1272
• Main Authors: Jensen, Malene Ringkjøbing, Salmon, Loïc, Nodet, Gabrielle, Blackledge, Martin
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 03.02.2010
• Subjects: Models, Molecular; Nuclear Magnetic Resonance, Biomolecular - methods; Protein Conformation; Protein Folding; Proteins - chemistry
• ISSN: 0002-7863; 1520-5126
• DOI: 10.1021/ja909973n

The development of meaningful descriptions of the conformational behavior of intrinsically disordered proteins represents a key challenge for contemporary structural biology. An approach is developed, based on the combination of ensemble descriptions of unfolded proteins and state-of-the-art chemical shift prediction algorithms, to describe backbone dihedral angle conformational behavior on the basis of 13C and 15N NMR chemical shifts alone. This allows the identification and characterization of entire secondary structural elements and their associated populations, as well as providing indications of the subtle detail of local conformational sampling in unfolded proteins.