1z2f
From Proteopedia
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'''solution structure of CfAFP-501''' | '''solution structure of CfAFP-501''' | ||
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[[Category: Jin, C.]] | [[Category: Jin, C.]] | ||
[[Category: Li, C.]] | [[Category: Li, C.]] | ||
| - | [[Category: | + | [[Category: Antifreeze protein]] |
| - | [[Category: | + | [[Category: Choristoneura fumiferana]] |
| - | [[Category: | + | [[Category: Solution structure]] |
| - | [[Category: | + | [[Category: Spruce budworm]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:06:26 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:06, 3 May 2008
solution structure of CfAFP-501
Overview
Antifreeze proteins (AFPs) are widely employed by various organisms as part of their overwintering survival strategy. AFPs have the unique ability to suppress the freezing point of aqueous solution and inhibit ice recrystallization through binding to the ice seed crystals and restricting their growth. The solution structure of CfAFP-501 from spruce budworm has been determined by NMR spectroscopy. Our result demonstrates that CfAFP-501 retains its rigid and highly regular structure in solution. Overall, the solution structure is similar to the crystal structure except the N- and C-terminal regions. NMR spin-relaxation experiments further indicate the overall rigidity of the protein and identify a collection of residues with greater flexibilities. Furthermore, Pro91 shows a cis conformation in solution instead of the trans conformation determined in the crystal structure.
About this Structure
1Z2F is a Single protein structure of sequence from Choristoneura fumiferana. Full crystallographic information is available from OCA.
Reference
Solution structure of an antifreeze protein CfAFP-501 from Choristoneura fumiferana., Li C, Guo X, Jia Z, Xia B, Jin C, J Biomol NMR. 2005 Jul;32(3):251-6. PMID:16132825 Page seeded by OCA on Sat May 3 17:06:26 2008
