The glassy state of crambin and the THz time scale protein-solvent fluctuations possibly related to protein function
Author:
Publisher
Springer Science and Business Media LLC
Subject
Biophysics
Link
http://link.springer.com/content/pdf/10.1186/s13628-014-0008-0.pdf
Reference70 articles.
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3. Schmidt A, Teeter M, Weckert E, Lamzin VS: Crystal structure of small protein crambin at 0.48 Å resolution. Acta Crystallograph Sect F Struct Biol Cryst Commun. 2011, 67 (Pt 4): 424-428. 10.1107/S1744309110052607.
4. Ringe D, Petsko GA: The “glass transition” in protein dynamics: what it is, why it occurs, and how to exploit it. Biophys Chem. 2003, 105: 667-680. 10.1016/S0301-4622(03)00096-6.
5. Chen JC-H, Hanson BL, Fisher SZ, Langan P, Kovalevsky AY: Direct observation of hydrogen atom dynamics and interactions by ultrahigh resolution neutron protein crystallography. Proc Natl Acad Sci. 2012, 109: 15301-15306. 10.1073/pnas.1208341109.
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