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Chapter title |
Characterizing Protein Dynamics with NMR R 1ρ Relaxation Experiments
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Chapter number | 10 |
Book title |
Protein NMR
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Published in |
Methods in molecular biology, January 2018
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DOI | 10.1007/978-1-4939-7386-6_10 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7385-9, 978-1-4939-7386-6
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Authors |
Francesca Massi, Jeffrey W. Peng |
Abstract |
The measurement of R1ρ , the longitudinal relaxation rate constant in the rotating frame, is one of the few available methods to characterize the μs-ms functional dynamics of biomolecules. Here, we focus on (15)N R1ρ experiments for protein NH groups. We present protocols for both on- and off-resonance (15)N R1ρ measurements needed for relaxation dispersion studies, and describe the data analysis for extracting kinetic and thermodynamic parameters characterizing the motional processes. |
Mendeley readers
The data shown below were compiled from readership statistics for 14 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 14 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 4 | 29% |
Student > Ph. D. Student | 3 | 21% |
Student > Bachelor | 2 | 14% |
Other | 1 | 7% |
Student > Master | 1 | 7% |
Other | 1 | 7% |
Unknown | 2 | 14% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 6 | 43% |
Chemistry | 3 | 21% |
Neuroscience | 1 | 7% |
Unknown | 4 | 29% |