Identifying Protein Conformational Dynamics Using Spin‐label ESR

Abstract

Spin‐label electron spin resonance (ESR) has emerged as a powerful tool to characterize protein dynamics. One recent advance is the development of ESR for resolving dynamical components that occur or coexist during a biological process. It has been applied to study the complex structural and dynamical aspects of membranes and proteins, such as conformational changes in protein during translocation from cytosol to membrane, conformational exchange between equilibria in response to protein‐protein and protein‐ligand interactions in either soluble or membrane environments, protein oligomerization, and temperature‐ or hydration‐dependent protein dynamics. As these topics are challenging but urgent for understanding the function of a protein on the molecular level, the newly developed ESR methods to capture individual dynamical components, even in low‐populated states, have become a great complement to other existing biophysical tools.

Structure and regulation of the BsYetJ calcium channel in lipid nanodiscs

“…SI Appendix, Figs. S2-S4 for data analysis) using the Tikhonovbased regulation methods (18,(22)(23)(24). Fig.…”

“…Seeking structural clues into the mechanism of calcium release activity in lipid bilayers, we undertake to identify the structure of BsYetJ reconstituted in 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) phospholipid bilayer nanodiscs using pulsed electron spin resonance (ESR) double electron electron resonance (DEER) technique (Fig. 1B) (16)(17)(18). We focus on the POPC lipid environment as phosphatidylcholines account for more than 60% of total lipid content in ER membrane, in which BI-1 is embedded.…”

Molecular Complexity from Aromatics: Recent Advances in the Chemistry of paraQuinol and Masked para‐Quinone Monoketal

“…The asymmetric version of this reaction was also developed by using (DHQ) 2 PHAL which provided the corresponding compound 254 in 80 % ee. [82] Synthesis of bicyclic 1,3-dioxolane and its analogs is one of the examples of the utility of para-quinol. Various methods were developed.…”

Structural polymorphism and substrate promiscuity of a ribosome-associated molecular chaperone

“…TF is a unique molecular chaperone in that it is the first molecular chaperone that all newly synthesized nascent polypeptide chains encounter (Hoffmann et al, 2012;Kaiser et al, 2006). TF binds to the ribosomal protein L23 through the RBD in a 1 : 1 stoichiometry at the exit of the ribosomal tunnel from which newly syn-thesized nascent polypeptide chains emerge during translation (Ferbitz et al, 2004;Lakshmipathy et al, 2007;Merz et al, 2008;Rutkowska et al, 2008). Unlike most molecular chaperones, which display ATPase activity to confer chaperone activities, TF does not have ATPase activity.…”