Journal
PHYSICAL REVIEW LETTERS
Volume 101, Issue 13, Pages -Publisher
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevLett.101.138102
Keywords
-
Categories
Ask authors/readers for more resources
Interdomain motions in proteins are essential to enable or promote biochemical function. Neutron spinecho spectroscopy is used to directly observe the domain dynamics of the protein alcohol dehydrogenase. The collective motion of domains as revealed by their coherent form factor relates to the cleft opening dynamics between the binding and the catalytic domains enabling binding and release of the functional important cofactor. The cleft opening mode hardens as a result of an overall stiffening of the domain complex due to the binding of the cofactor.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available