JACS 2016

A joint structural refinement against NMR data and X-ray diffraction patterns offers unique opportunities to detect differences in the conformation of biomolecules between the solution and the crystal states. Read More


An integrated approach which combines in-cell NMR spectroscopy with optical and X-ray fluorescence microscopy was developed to describe the intracellular maturation state of human Cu,Zn-SOD1.  Read More

NCB N terminal

Structural and biophysical evidences define the early steps of iron-sulfur protein maturation in the cytosol, demonstrating that  glutaredoxin-3 passes [2Fe-2S] clusters to anamorsin during a protein-protein interaction mediated by their N-terminal domains.  Read More 

nature chemistry

Dynamic nuclear polarization (DNP) in liquid solutions can enhance 13C NMR signals at magnetic fields of 3 T and room temperature up to three orders of magnitude. Read More  Highlighted in Angewandte Chemie

CERM research on covers

cover ACSnano lr

cover J Phys Chem lr  
High relaxivity Gd(III)-DNA gold nanostars: investigation of shape effects on proton relaxation, ACS nano, 9, 3385–3396, 2015 Exploring regions of conformational space occupied by two-domain proteins, J.Phys.Chem.B, 118, 10576-10587, 2014  


cover IDP

Intrinsically Disordered Proteins Studied by NMR Spectroscopy

Series: Advances in Experimental Medicine and Biology, Vol. 870

Felli I., Pierattelli R., (Ed.), Springer, 2015





 Buy this book on Springer.com

This book discusses the paradigm-shifting phenomenon of intrinsically disordered proteins (IDPs) and hybrid proteins containing ordered domains and functional IDP regions (IDPRs). The properties of IDPs and IDPRs are highly complementary to those deriving from the presence of a unique and well-defined three-dimensional fold. Ignored for a long time in high-resolution studies of proteins, intrinsic protein disorder is now recognized as one of the key features for a large variety of cellular functions, where structural flexibility presents a functional advantage in terms of binding plasticity and promiscuity and this volume explores this exciting new research.

Recent progress in the field has radically changed our perspective to study IDPs through NMR: increasingly complex IDPs can now be characterized, a wide range of observables can be determined reporting on the structural and dynamic properties, computational methods to describe the structure and dynamics are in continuous development and IDPs can be studied in environments as complex as whole cells. This volume communicates the new exciting possibilities offered by NMR and presents open questions to foster further developments.

Intrinsically Disordered Proteins Studied by NMR Spectroscopy provides a snapshot to researchers entering the field as well as providing a current overview for more experienced scientists in related areas.

Keywords: protein structure and function


Table of Contents:

1. Back to the Future: Nuclear Magnetic Resonance and Bioinformatics Studies on Intrinsically Disordered Proteins by Dunker, A. Keith (et al.)

2. Structure and Dynamics of Intrinsically Disordered Proteins by Fu, Biao (et al.)

3. NMR Methods for the Study of Instrinsically Disordered Proteins Structure, Dynamics, and Interactions: General Overview and Practical Guidelines by Brutscher, Bernhard (et al.)

4. Ensemble Calculation for Intrinsically Disordered Proteins Using NMR Parameters by Kragelj, Jaka (et al.)

5. NMR Spectroscopic Studies of the Conformational Ensembles of Intrinsically Disordered Proteins by Kurzbach, Dennis (et al.)

6. Recombinant Intrinsically Disordered Proteins for NMR: Tips and Tricks by Calçada, Eduardo O. (et al.)

7. Biophysical Methods to Investigate Intrinsically Disordered Proteins: Avoiding an “Elephant and Blind Men” Situation by Uversky, Vladimir N.

8. Application of SAXS for the Structural Characterization of IDPs by Kachala, Michael (et al.)

9. Bioinformatics Approaches for Predicting Disordered Protein Motifs by Bhowmick, Pallab (et al.)

10. Towards Understanding Protein Disorder by Cedeño, Cesyen (et al.)

11. The Protein Ensemble Database by Varadi, Mihaly (et al.)

12. Order and Disorder in the Replicative Complex of Paramyxoviruses by Erales, Jenny (et al.)

13. Druggability of Intrinsically Disordered Proteins by Joshi, Priyanka (et al.)

14. Beta Amyloid Hallmarks: From Intrinsically Disordered Proteins to Alzheimer’s Disease by Korsak, Magdalena (et al.)