(Q37621833)

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Interplay between conformational selection and induced fit in multidomain protein-ligand binding probed by paramagnetic relaxation enhancement.

scientific article published on 31 August 2013

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scholarly article

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23 February 2020

Interplay between conformational selection and induced fit in multidomain protein-ligand binding probed by paramagnetic relaxation enhancement (English)

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23 February 2020

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G. Marius Clore

1

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23 February 2020

G. Marius Clore

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G Marius Clore

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21 August 2017

publication date

31 August 2013

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23 February 2020

Biophysical Chemistry

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23 February 2020

186

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23 February 2020

3-12

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Europe PubMed Central

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23 February 2020

The length of the calmodulin linker determines the extent of transient interdomain association and target affinity.

1 reference

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Conformational selection or induced fit? A critical appraisal of the kinetic mechanism

1 reference

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Transient, sparsely populated compact states of apo and calcium-loaded calmodulin probed by paramagnetic relaxation enhancement: interplay of conformational selection and induced fit.

1 reference

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1 reference

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1 reference

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Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes.

1 reference

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Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR

1 reference

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Practical aspects of (1)H transverse paramagnetic relaxation enhancement measurements on macromolecules.

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Detecting transient intermediates in macromolecular binding by paramagnetic NMR.

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Ensemble approach for NMR structure refinement against (1)H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecule

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Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides

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Experimentally exploring the conformational space sampled by domain reorientation in calmodulin

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The energetic cost of domain reorientation in maltose-binding protein as studied by NMR and fluorescence spectroscopy

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A Closed Compact Structure of Native Ca2+-Calmodulin

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Theoretical and computational advances in biomolecular NMR spectroscopy

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Solution structure of Ca(2+)-calmodulin reveals flexible hand-like properties of its domains

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Analysis of slow interdomain motion of macromolecules using NMR relaxation data

1 reference

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The 1.0 A crystal structure of Ca(2+)-bound calmodulin: an analysis of disorder and implications for functionally relevant plasticity

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

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On the nature of allosteric transitions: implications of non-exclusive ligand binding

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Three-dimensional structure of calmodulin

1 reference

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Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy

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The solution structures of calmodulin and its complexes with synthetic peptides based on target enzyme binding domains

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1 reference

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1 reference

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1 reference

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Reweighted atomic densities to represent ensembles of NMR structures

1 reference

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Identifiers

10.1016/J.BPC.2013.08.006

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Europe PubMed Central

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23 February 2020

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Europe PubMed Central

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23 February 2020

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23 February 2020

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