Time-resolved Solid State NMR of Biomolecular Processes with Millisecond Time Resolution

Overview

Journal J Magn Reson

Publisher Elsevier

Date 2022 Aug 23

PMID 35998398

Authors

Jaekyun Jeon

C Blake Wilson

Wai-Ming Yau

Kent R Thurber

Robert Tycko

Affiliations

Soon will be listed here.

Abstract

We review recent efforts to develop and apply an experimental approach to the structural characterization of transient intermediate states in biomolecular processes that involve large changes in molecular conformation or assembly state. This approach depends on solid state nuclear magnetic resonance (ssNMR) measurements that are performed at very low temperatures, typically 25-30 K, with signal enhancements from dynamic nuclear polarization (DNP). This approach also involves novel technology for initiating the process of interest, either by rapid mixing of two solutions or by a rapid inverse temperature jump, and for rapid freezing to trap intermediate states. Initiation by rapid mixing or an inverse temperature jump can be accomplished in approximately-one millisecond. Freezing can be accomplished in approximately 100 microseconds. Thus, millisecond time resolution can be achieved. Recent applications to the process by which the biologically essential calcium sensor protein calmodulin forms a complex with one of its target proteins and the process by which the bee venom peptide melittin converts from an unstructured monomeric state to a helical, tetrameric state after a rapid change in pH or temperature are described briefly. Future applications of millisecond time-resolved ssNMR are also discussed briefly.

Citing Articles

Optimization of N-C double-resonance NMR experiments under low temperature magic angle spinning dynamic nuclear polarization conditions.

Wilson C, Tycko R J Magn Reson. 2024; 368:107783.

PMID: 39383594 PMC: 11573627. DOI: 10.1016/j.jmr.2024.107783.

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