Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules.

By A. Palmer, C. Kroenke, J. Loria. Methods in Enzymology, 2001

862 citations recorded by the source corpus.

Subfields: Materials Chemistry, Nuclear and High Energy Physics, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/9568e39e1802d9ec42791f2a45dfef65b29eaa9b

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Materials Chemistry

1. Avner Schlessinger
2. Burkhard Rost
3. Santrupti Nerli
4. Ruth Nussinov
5. Chung-Jung Tsai
6. Nikolaos G. Sgourakis
7. Dorothee Kern
8. Andrew C. McShan

In Nuclear and High Energy Physics

1. Ruth Nussinov
2. Avner Schlessinger
3. Chung-Jung Tsai
4. Nikolaos G. Sgourakis
5. Santrupti Nerli
6. Burkhard Rost
7. Andrew C. McShan

In Spectroscopy

1. Santrupti Nerli
2. Nikolaos G. Sgourakis
3. Ruth Nussinov
4. Avner Schlessinger
5. Chung-Jung Tsai
6. Dorothee Kern
7. Burkhard Rost
8. Andrew C. McShan

Citations in the corpus

• The ensemble nature of allostery (2014, neutral): “local unfolding has a role in allostery is in the enzyme aminoglycoside N-(69)-acetyltransferase II (AAC)—a homodimeric enzyme from Enterococcus faecium responsible for conferring bacterial resistance to amino-”
• A Unified View of “How Allostery Works” (2014, methodology): “A similar free energy landscape of activation of the signaling protein NtrC [8] has been correlated with microscopic rate constants between the inactive and active states, which were extracted from fitted global exchange rate constant (Kex) [40] using rate constants determined by the NMR (15)N backb”
• Protein flexibility and rigidity predicted from sequence (2005, methodology): “Solution NMR spectroscopy methods are commonly used to characterize the dynamic properties of proteins.(21,51,52) It has been previously shown that order parameter data obtained from NMR spin relaxation experiments are, to an extent, correlated with experimental B-value data.”
• The role of dynamics in allosteric regulation. (2003, background): “Fluctuations between conformational substates on the millisecond to microsecond timescale can now be measured quantitatively and site resolved by NMR as well [17].”
• Chemical shift-based methods in NMR structure determination (2018, background): “In particular, PRE/PCS measurements [157] are useful for cases of fast conformational exchange; rotating frame R1p relaxation [158] and Carr–Purcell– Meiboom–Gill (CPMG) dispersion [159] for intermediate exchange; and chemical-exchange saturation transfer (CEST) [160] for slow exchange.”