Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2030101 | Structure | 2006 | 10 Pages |
Abstract
Solid-state NMR is a versatile and powerful tool for determining the dynamic structure of membrane proteins at atomic resolution. I review the recent progress in determining the orientation, the internal and global protein dynamics, the oligomeric structure, and the ligand-bound structure of membrane proteins with both α-helical and β sheet conformations. Examples are given that illustrate the insights into protein function that can be gained from the NMR structural information.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Mei Hong,