(Q45336612)

13 December 2017

title

Probing non-specific interactions of Ca²⁺-calmodulin in E. coli lysate (English)

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13 December 2017

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2

Lewis E Kay

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13 December 2017

Michael P Latham

1

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publication date

17 January 2013

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Journal of Biomolecular NMR

13 December 2017

published in

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13 December 2017

volume

55

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13 December 2017

issue

3

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13 December 2017

page(s)

239-247

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https://scigraph.springernature.com/pub.10.1007/s10858-013-9705-2

13 December 2017

exact match

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cites work

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Macromolecular crowding remodels the energy landscape of a protein by favoring a more compact unfolded state

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

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NMR studies of the methionine methyl groups in calmodulin

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13CHD2 methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamics

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PubMed

https://pubmed.ncbi.nlm.nih.gov/23324860

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Protein Crowding Tunes Protein Stability

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/23324860

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1007/S10858-013-9705-2

1 reference

Dimensions Publication ID

13 December 2017

1043262484

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1 reference