Correction to What’s in Your Buffer? Solute Altered Millisecond Motions Detected by Solution NMR

Wong, Madeline; Khirich, Gennady; Loria, J. Patrick

doi:10.1021/bi401247g

Cited by 1 publication

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“…Note that caution has to be taken when interpreting relaxation dispersion data for different buffers due to their impact on the chemical shifts of ground and excitedstate conformations. [21][22][23] Figure 2(A, B) show the R ex rates for the proteins ubiquitin and MBP. For ubiquitin, which shows an overall extremely low [20] Boxes extend from the first to the third quartile with a line at the median.…”

Section: Resultsmentioning

confidence: 99%

“…Whereas such measurements can also inform on conformational‐exchange timescales and even populations, in this work we restrict our interpretation of differences in R ex between two salt concentrations as indicating a different extent of conformational exchange. Note that caution has to be taken when interpreting relaxation dispersion data for different buffers due to their impact on the chemical shifts of ground and excited‐state conformations [21–23] …”

Section: Resultsmentioning

confidence: 99%

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Nonlinear Impact of Electrolyte Solutions on Protein Dynamics

Daronkola,

Söldner,

Singh

et al. 2024

ChemBioChem

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Halophilic organisms have adapted to multi‐molar salt concentrations, their cytoplasmic proteins functioning despite stronger attraction between hydrophobic groups. These proteins, of interest in biotechnology because of decreasing fresh‐water resources, have excess acidic amino acids. It has been suggested that conformational fluctuations ‐‐ critical for protein function ‐‐ decrease in the presence of a stronger hydrophobic effect, and that an acidic proteome would counteract this decrease. However, our understanding of the salt‐ and acidic amino acid dependency of enzymatic activity is limited. Here, using solution NMR relaxation and molecular dynamics simulations for in total 14 proteins, we show that salt concentration has a limited and moreover non‐monotonic impact on protein dynamics. The results speak against the conformational‐fluctuations model, instead indicating that maintaining protein dynamics to ensure protein function is not an evolutionary driving force behind the acidic proteome of halophilic proteins.

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