[NMR paper] Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase.
Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase.
Related ArticlesMillisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase.
J Am Chem Soc. 2020 Dec 07;:
Authors: Jeon J, Yau WM, Tycko R
Abstract
Calmodulin (CaM) mediates a wide range of biological responses to changes in intracellular Ca2+ concentrations through its calcium-dependent binding affinities to numerous target proteins. Binding of two Ca2+ ions to each of the two four-helix-bundle domains of CaM results in major conformational changes that create a potential binding site for the CaM binding domain of a target protein, which also undergoes major conformational changes to form the complex with CaM. Details of the molecular mechanism of complex formation are not well established, despite numerous structural, spectroscopic, thermodynamic, and kinetic studies. Here, we report a study of the process by which the 26-residue peptide M13, which represents the CaM binding domain of skeletal muscle myosin light chain kinase, forms a complex with CaM in the presence of excess Ca2+ on the millisecond time scale. Our experiments use a combination of selective 13C labeling of CaM and M13, rapid mixing of CaM solutions with M13/Ca2+ solutions, rapid freeze-quenching of the mixed solutions, and low-temperature solid state nuclear magnetic resonance (ssNMR) enhanced by dynamic nuclear polarization. From measurements of the dependence of 2D 13C-13C ssNMR spectra on the time between mixing and freezing, we find that the N-terminal portion of M13 converts from a conformationally disordered state to an ?-helix and develops contacts with the C-terminal domain of CaM in about 2 ms. The C-terminal portion of M13 becomes ?-helical and develops contacts with the N-terminal domain of CaM more slowly, in about 8 ms. The level of structural order in the CaM/M13/Ca2+ complexes, indicated by 13C ssNMR line widths, continues to increase beyond 27 ms.
PMID: 33280387 [PubMed - as supplied by publisher]
[NMR paper] Light-induced uncaging for time-resolved observations of biochemical reactions by MAS NMR spectroscopy.
Light-induced uncaging for time-resolved observations of biochemical reactions by MAS NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7388-69-wiley-full-text.png Related Articles Light-induced uncaging for time-resolved observations of biochemical reactions by MAS NMR spectroscopy.
Chemistry. 2020 Apr 02;:
Authors: de Mos J, Jakob A, Becker-Baldus J, Heckel A, Glaubitz C
Abstract
Light-induced activation of biomolecules by uncaging of photolabile protection groups...
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[NMR paper] Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine ?-Lactalbumin.
Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine ?-Lactalbumin.
Related Articles Millisecond Time Resolved Photo-CIDNP NMR Reveals a Non-Native Folding Intermediate on the Ion-Induced Refolding Pathway of Bovine ?-Lactalbumin.
Angew Chem Int Ed Engl. 2001 Nov 19;40(22):4248-4251
Authors: Wirmer J, Kühn T, Schwalbe H
Abstract
Aspects of the structure of the intermediate populated after 200 ms in the Ca2+ -induced refolding of ?-lactalbumin have been...
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Differences in Protein Concentration Dependence forNucleation and Elongation in Light Chain Amyloid Formation
Differences in Protein Concentration Dependence forNucleation and Elongation in Light Chain Amyloid Formation
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b01043/20170124/images/medium/bi-2016-010439_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b01043
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[NMR paper] Structure-Function Analysis of the Non-Muscle Myosin Light Chain Kinase (nmMLCK) Isoform by NMR Spectroscopy and Molecular Modeling: Influence of MYLK Variants.
Structure-Function Analysis of the Non-Muscle Myosin Light Chain Kinase (nmMLCK) Isoform by NMR Spectroscopy and Molecular Modeling: Influence of MYLK Variants.
Related Articles Structure-Function Analysis of the Non-Muscle Myosin Light Chain Kinase (nmMLCK) Isoform by NMR Spectroscopy and Molecular Modeling: Influence of MYLK Variants.
PLoS One. 2015;10(6):e0130515
Authors: Shen K, Ramirez B, Mapes B, Shen GR, Gokhale V, Brown ME, Santarsiero B, Ishii Y, Dudek SM, Wang T, Garcia JG
Abstract
The MYLK gene encodes the...
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06-26-2015 09:55 PM
[NMR paper] Solution NMR assignment of the heavy chain complex of the human cardiac myosin regulatory light chain.
Solution NMR assignment of the heavy chain complex of the human cardiac myosin regulatory light chain.
Related Articles Solution NMR assignment of the heavy chain complex of the human cardiac myosin regulatory light chain.
Biomol NMR Assign. 2014 Jan 12;
Authors: Rostkova E, Gautel M, Pfuhl M
Abstract
The regulatory light chain (RLC) of striated and cardiac muscle myosin plays a complex role in muscle function and regulation. Together with the essential light chain it provides stability to the lever arm, which is essential for force...
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Solid-state NMR applied to photosynthetic light-harvesting complexes.
Solid-state NMR applied to photosynthetic light-harvesting complexes.
Solid-state NMR applied to photosynthetic light-harvesting complexes.
Photosynth Res. 2011 Aug 13;
Authors: Pandit A, de Groot HJ
This short review describes how solid-state NMR has provided a mechanistic and electronic picture of pigment-protein and pigment-pigment interactions in photosynthetic antenna complexes. NMR results on purple bacterial antenna complexes show how the packing of the protein and the pigments inside the light-harvesting oligomers induces mutual...
Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase.
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