(Q30423139)

English

Is buffer a good proxy for a crowded cell-like environment? A comparative NMR study of calmodulin side-chain dynamics in buffer and E. coli lysate

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

5 October 2017

Is buffer a good proxy for a crowded cell-like environment? A comparative NMR study of calmodulin side-chain dynamics in buffer and E. coli lysate (English)

1 reference

Europe PubMed Central

PMC publication ID

5 October 2017

Escherichia coli

0 references

Michael P Latham

object named as

Michael P Latham

1

0 references

2

object named as

Lewis E Kay

1 reference

Europe PubMed Central

PMC publication ID

5 October 2017

language of work or name

0 references

publication date

30 October 2012

1 reference

Europe PubMed Central

PMC publication ID

5 October 2017

1 reference

Europe PubMed Central

PMC publication ID

5 October 2017

7

1 reference

Europe PubMed Central

PMC publication ID

5 October 2017

10

1 reference

Europe PubMed Central

PMC publication ID

5 October 2017

e48226

1 reference

Europe PubMed Central

PMC publication ID

5 October 2017

copyright license

Creative Commons Attribution 4.0 International

30 October 2012

1 reference

April 2022 Public Data File from Crossref

copyright status

0 references

Exploring weak, transient protein--protein interactions in crowded in vivo environments by in-cell nuclear magnetic resonance spectroscopy

1 reference

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The effect of macromolecular crowding, ionic strength and calcium binding on calmodulin dynamics

1 reference

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Coupling of protein and environment fluctuations

1 reference

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Macromolecular crowding fails to fold a globular protein in cells

1 reference

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Protein interactions in the Escherichia coli cytosol: an impediment to in-cell NMR spectroscopy.

1 reference

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In-cell protein NMR and protein leakage

1 reference

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Enzyme dynamics point to stepwise conformational selection in catalysis.

1 reference

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Choreographing an enzyme's dance

1 reference

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Volume exclusion and soft interaction effects on protein stability under crowded conditions

1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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Protein structure determination in living cells by in-cell NMR spectroscopy

1 reference

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1 reference

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Cell water dynamics on multiple time scales

1 reference

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Measurement of bond vector orientations in invisible excited states of proteins

1 reference

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Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy.

1 reference

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1 reference

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1 reference

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1 reference

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Reaction kinetics in intracellular environments with macromolecular crowding: simulations and rate laws

1 reference

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Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling

1 reference

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A perspective on enzyme catalysis.

1 reference

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1 reference

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1 reference

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Multiple conformational changes in enzyme catalysis

1 reference

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Dynamics of the transition between open and closed conformations in a calmodulin C-terminal domain mutant.

1 reference

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Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex

1 reference

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2 references

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Solution structure of calcium-free calmodulin

1 reference

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Calcium-induced conformational transition revealed by the solution structure of apo calmodulin

1 reference

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Solvent viscosity and protein dynamics

1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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In-Cell NMR Spectroscopy†

1 reference

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1 reference

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1 reference

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1 reference

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Identifiers

10.1371/JOURNAL.PONE.0048226

1 reference

Europe PubMed Central

PMC publication ID

5 October 2017

2012PLoSO...748226L

0 references

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

5 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

5 October 2017

ResearchGate publication ID

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