Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle

Abstract

Site-selective isotope labeling enables structural and functional investigation of a working 1-MDa chaperonin by NMR spectroscopy.

Structural basis of DegP-protease temperature-dependent activation

“…In order to quantify the interconversion between the open to the locked state we used NMR exchange spectroscopy (Fig. 3f,g) 40,41 . The obtained rate for the interconversion between the different states was kex = 0.33 s -1 from the open to the locked state.…”

Structural Analysis of Jumbo Coliphage phAPEC6

“…For TEM, the phages were stained using 2% ammonium molybdate, pH 7.5, and imaged in a T12 FEI EM using an Orius SC1000 CCD camera according to the method described by Mas et al [44].…”

Aromatic Ring Dynamics, Thermal Activation, and Transient Conformations of a 468 kDa Enzyme by Specific 1H–13C Labeling and Fast Magic-Angle Spinning NMR

“…The use of selective CH 3 -labeling, [3][4][5] deuteration and methyl-TROSY NMR 6 has lifted these protein-size limitations partly, allowing the study of dynamics and interactions of methylbearing residues even in proteins as large as 1 MDa. 3,7,8 Moieties other than methyls have been thought to be generally undetectable in large proteins by solution-NMR, until recent breakthrough isotope labeling methods allowed observing any kinds of aromatic and aliphatic moieties for a 82 kDa protein malate synthase G (MSG) in solution. 9 Aromatic residues have been the subject of much interest since the early days of protein NMR.…”