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Default Hydrogen bonding on the ice-binding face of a beta-helical antifreeze protein indicat

Hydrogen bonding on the ice-binding face of a beta-helical antifreeze protein indicated by amide proton NMR chemical shifts.

Related Articles Hydrogen bonding on the ice-binding face of a beta-helical antifreeze protein indicated by amide proton NMR chemical shifts.

Biochemistry. 2004 Oct 19;43(41):13012-7

Authors: Daley ME, Graether SP, Sykes BD

The dependence of amide proton chemical shifts on temperature is used as an indication of the hydrogen bonding properties in a protein. The amide proton temperature coefficients of the beta-helical antifreeze protein from Tenebrio molitor are examined to determine their hydrogen bonding state in solution. The temperature-dependent chemical shift behavior of the amides in T. molitor antifreeze protein varies widely throughout the protein backbone; however, very subtle effects of hydrogen bonding can be distinguished using a plot of chemical shift deviation (CSD) versus the backbone amide chemical shift temperature gradient (Deltadelta/DeltaT). We show that differences between the two ranks of ice-binding threonine residues on the surface of the protein indicate that threonine residues in the left-hand rank participate in intrastrand hydrogen bonds that stabilize the flat surface required for optimal ice binding.

PMID: 15476394 [PubMed - indexed for MEDLINE]



Source: PubMed
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