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- W3176032005 abstract "Rapid freezing of samples brought new applications of biomolecular solid state nuclear magnetic resonance (SSNMR) to the structural characterization of kinetically trapped intermediates in protein folding. A frozen protein solution from an elevated temperature up to 90 °C was transferred to an SSNMR spectrometer, where structural measurements were carried out at < -120 °C for many days. We initially studied a small helical protein HP35 (35-residue villin headpiece subdomain) with high stability (70 °C unfolding temperature) and a rapid folding rate(10 μs time scale). A 13C-labeled HP35 solution in glycerol/water was cooled from 90 to -120 °C in ~10 μs by spraying the hot solution through a 20μm-diameter nozzle into a cold isopentane bath, generating slurry of frozen protein solution with ~10 μm particle sizes. 13C NMR spectra show both folded and unfolded protein components in approximately equal proportions for some sites and indicate that the HP35 folding process is not cooperative for several labeled amino acid residues. Moreover, the tertiary contacts and backbone ordering do not form simultaneously through folding." @default.
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- W3176032005 date "2009-04-01" @default.
- W3176032005 modified "2023-09-27" @default.
- W3176032005 title "Rapid Freezing Quench of Transient Conformations of Folding Proteins for Solid State NMR Studies" @default.
- W3176032005 doi "https://doi.org/10.1096/fasebj.23.1_supplement.850.1" @default.
- W3176032005 hasPublicationYear "2009" @default.
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