Structural highlights
Function
SPTN1_CHICK Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.
Publication Abstract from PubMed
Understanding macromolecular function, interactions, and stability hinges on detailed assessment of conformational ensembles. For solid proteins, accurate elucidation of the spatial aspects of dynamics at physiological temperatures is limited by the qualitative character or low abundance of solid-state nuclear magnetic resonance internuclear distance information. Here, we demonstrate access to abundant proton-proton internuclear distances for integrated structural biology and chemistry with unprecedented accuracy. Apart from highest-resolution single-state structures, the exact distances enable molecular dynamics (MD) ensemble simulations orchestrated by a dense network of experimental interproton distance boundaries gathered in the context of their physical lattices. This direct embedding of experimental ensemble distances into MD will provide access to representative, atomic-level spatial details of conformational dynamics in supramolecular assemblies, crystalline and lipid-embedded proteins, and beyond.
Integrated Assessment of the Structure and Dynamics of Solid Proteins.,Soldner B, Grohe K, Neidig P, Auch J, Blach S, Klein A, Vasa SK, Schafer LV, Linser R J Phys Chem Lett. 2023 Feb 23;14(7):1725-1731. doi: 10.1021/acs.jpclett.2c03398. , Epub 2023 Feb 9. PMID:36757335[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Söldner B, Grohe K, Neidig P, Auch J, Blach S, Klein A, Vasa SK, Schäfer LV, Linser R. Integrated Assessment of the Structure and Dynamics of Solid Proteins. J Phys Chem Lett. 2023 Feb 23;14(7):1725-1731. PMID:36757335 doi:10.1021/acs.jpclett.2c03398
