Enrico Ravera

Prof. Dr. Enrico Ravera

Magnetic Resonance Center (CERM), University of Florence and Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine (CIRMMP), Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
orcid

Research Focus & Metrics

Academic Career Length

17Years (2010-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

View All Publications
1 July 2015 in Angewandte Chemie International Edition
Verified
Journal Article
Open access
PDF file
Jan Henrik Ardenkjaer-LarsenJan Henrik Ardenkjaer-Larsen
Jan Henrik Ardenkjaer-Larsen
GBGregory S. Boebinger
Gregory S. Boebinger
ACArnaud Comment
Arnaud Comment
SDSimon Duckett
Simon Duckett
Arthur EdisonArthur Edison
Arthur Edison
LFLucio Frydman
Lucio Frydman
In the Spring of 2013, NMR spectroscopists convened at the Weizmann Institute in Israel to brainstorm on approaches to improve the sensitivity of NMR experiments, particularly when applied in biomolecular settings. This multi‐author interdisciplinary Review presents a state‐of‐the‐art description of the primary approaches that were considered. Topics discussed included the future of ultrahigh‐field NMR systems, emerging NMR detection technologies, new approaches to nuclear hyperpolarization, and progress in sample preparation. All of these are orthogonal efforts, whose gains could multiply and thereby enhance the sensitivity of solid‐ and liquid‐state experiments. While substantial advances have been made in all these areas, numerous challenges remain in the quest of endowing NMR spectroscopy with the sensitivity that has characterized forms of spectroscopies based on electrical or optical measurements. These challenges, and the ways by which scientists and engineers are striving to solve them, are also addressed.

24 October 2018 in Chemistry of Materials
Verified
Journal Article
Closed access
AKAbhoy Karmakar
Abhoy Karmakar
MDMya S. Dodd
Mya S. Dodd
SASatyam Agnihotri
Satyam Agnihotri
Enrico RaveraEnrico Ravera
Enrico Ravera
VMVladimir K. Michaelis
Vladimir K. Michaelis

13 June 2011 in Proceedings of the National Academy of Sciences
Verified
Journal Article
Closed access
IBIvano Bertini
Ivano Bertini
Claudio LuchinatClaudio Luchinat
Claudio Luchinat
GPGiacomo Parigi
Giacomo Parigi
Enrico RaveraEnrico Ravera
Enrico Ravera
BRBernd Reif
Bernd Reif
Paola TuranoPaola Turano
Paola Turano
Relatively large proteins in solution, spun in NMR rotors for solid samples at typical ultracentrifugation speeds, sediment at the rotor wall. The sedimented proteins provide high-quality solid-state-like NMR spectra suitable for structural investigation. The proteins fully revert to the native solution state when spinning is stopped, allowing one to study them in both conditions. Transiently sedimented proteins can be considered a novel phase as far as NMR is concerned. NMR of transiently sedimented molecules under fast magic angle spinning has the advantage of overcoming protein size limitations of solution NMR without the need of sample crystallization/precipitation required by solid-state NMR.

7 September 2010 in Journal of the American Chemical Society
Verified
Journal Article
Closed access
IBIvano Bertini
Ivano Bertini
AGAndrea Giachetti
Andrea Giachetti
Claudio LuchinatClaudio Luchinat
Claudio Luchinat
GPGiacomo Parigi
Giacomo Parigi
MPMaxim Petoukhov
Maxim Petoukhov
DSDmitri I. Svergun
Dmitri I. Svergun

1 March 2016 in Journal of Magnetic Resonance
Verified
Journal Article
Closed access
Enrico RaveraEnrico Ravera
Enrico Ravera
CLClaudio Luchinat
Claudio Luchinat
GPGiacomo Parigi
Giacomo Parigi

6 November 2015 in Physical Chemistry Chemical Physics
Verified
Journal Article
Closed access
PDF file
Enrico RaveraEnrico Ravera
Enrico Ravera
LSLuca Sgheri
Luca Sgheri
GPGiacomo Parigi
Giacomo Parigi
Claudio LuchinatClaudio Luchinat
Claudio Luchinat
We analyze the different approaches to obtain quantitative and accurate structural information from averaged data. We cluster them in two groups: those satisfying the maximum entropy principle and those recovering ensembles composed of a restricted number of conformations. Information of different types are recovered in the two cases.