Dynamics in protein powders on the nanosecond-picosecond time scale are dominated by localized motions

Jonathan D. Nickels, Victoria García Sakai, Alexei P. Sokolov

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

We present analysis of nanosecond-picosecond dynamics of Green Fluorescence Protein (GFP) using neutron scattering data obtained on three spectrometers. GFP has a β-barrel structure that differs significantly from the structure of other globular proteins and is thought to result in a more rigid local environment. Despite this difference, our analysis reveals that the dynamics of GFP are similar to dynamics of other globular proteins such as lysozyme and myoglobin. We suggest that the same general concept of protein dynamics may be applicable to all these proteins. The dynamics of dry protein are dominated by methyl group rotations, while hydration facilitates localized diffusion-like motions in the protein. The latter has an extremely broad relaxation spectrum. The nanosecond-picosecond dynamics of both dry and hydrated GFP are localized to distances of ∼1-3.5 Å, in contrast to the longer range diffusion of hydration water.

Original languageEnglish
Pages (from-to)11548-11555
Number of pages8
JournalJournal of Physical Chemistry B
Volume117
Issue number39
DOIs
StatePublished - Oct 3 2013

Fingerprint

Dive into the research topics of 'Dynamics in protein powders on the nanosecond-picosecond time scale are dominated by localized motions'. Together they form a unique fingerprint.

Cite this