1z2f: Difference between revisions

Line 1:

[[Image:1z2f.gif|left|200px]]<br /><applet load="1z2f" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1z2f.gif|left|200px]]<br /><applet load="1z2f" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1z2f" />

'''solution structure of CfAFP-501'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1Z2F OCA].

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==

Line 20:

[[Category: spruce budworm]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sun Nov 25 04~~:42:~~25 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:31 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1z2f.gif|left|200px]]<br /><applet load="1z2f" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1z2f.gif|left|200px]]<br /><applet load="1z2f" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1z2f" />
 '''solution structure of CfAFP-501'''<br />
 ==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.
+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==
-Z2F 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z2F OCA].
+Z2F 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==
@@ Line 20: / Line 20: @@
 [[Category: spruce budworm]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:42:25 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:31 2008''