1z2f
From Proteopedia
(New page: 200px<br /><applet load="1z2f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z2f" /> '''solution structure of CfAFP-501'''<br /> ==...) |
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| - | [[Image:1z2f.gif|left|200px]]<br /><applet load="1z2f" size=" | + | [[Image:1z2f.gif|left|200px]]<br /><applet load="1z2f" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''solution structure of CfAFP-501'''<br /> | '''solution structure of CfAFP-501'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Antifreeze proteins (AFPs) are widely employed by various organisms as | + | 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== | ==About this Structure== | ||
| - | 1Z2F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Choristoneura_fumiferana Choristoneura fumiferana]. Full crystallographic information is available from [http:// | + | 1Z2F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Choristoneura_fumiferana Choristoneura fumiferana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z2F OCA]. |
==Reference== | ==Reference== | ||
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[[Category: spruce budworm]] | [[Category: spruce budworm]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:31 2008'' |
Revision as of 14:11, 21 February 2008
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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
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