Activities per year
Abstract
By specifically labeling leucine/valine methyl groups and lysine side chains "inside" and "outside" dynamics of proteins on the nanosecond timescale are compared using neutron scattering. Surprisingly, both groups display similar dynamics as a function of temperature, and the buried hydrophobic core is sensitive to hydration and undergoes a dynamical transition.
| Original language | English |
|---|---|
| Journal | Angewandte Chemie International Edition |
| Volume | 52 |
| Issue | 2 |
| Pages (from-to) | 665-668 |
| Number of pages | 4 |
| ISSN | 1433-7851 |
| DOIs | |
| Publication status | Published - 2013 |
Keywords
- NMR neutron scattering protein dynamics
Fingerprint
Dive into the research topics of 'Protein Surface and Core Dynamics Show Concerted Hydration-Dependent Activation'. Together they form a unique fingerprint.Activities
- 1 Participation in or organisation of workshop, seminar or course
-
Danish NMR Discussion Group Meeting
Mulder, F. A. A. (Participant)
21 Jan 2013 → 22 Jan 2013Activity: Participating in or organising an event types › Participation in or organisation of workshop, seminar or course