2g9l: Difference between revisions

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[[Image:2g9l.~~jpg~~|left|200px]]

[[Image:2g9l.png|left|200px]]

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~~'''~~The High-resolution Solution Conformation of an Antimicrobial Peptide Gaegurin 4 and Its Mode of Membrane Interaction~~'''~~

===The High-resolution Solution Conformation of an Antimicrobial Peptide Gaegurin 4 and Its Mode of Membrane Interaction===

~~==Overview==~~

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~~We have applied NMR spectroscopy to determine the high~~-~~resolution structure of gaegurin 4, a 37~~-~~residue antimicrobial peptide from Rana rugosa, under varying hydrophobic conditions. Even in 100% H2O~~, ~~gaegurin 4 contains a nascent turn near its C-terminal Rana box. Under a more hydrophobic condition it forms two amphipathic helices~~, ~~one long encompassing residues 2-23 and~~ the ~~other consisting of residues 25-34, similar~~ to ~~what has been observed in cecropin A. Functional implication of~~ the ~~helix-breaking kink~~ at ~~Gly24 in gaegurin 4 was investigated by preparing several analogs~~. ~~Based upon~~ the ~~current and previous results, we propose a novel seaanemone~~-~~like ion pore~~-~~forming model for gaegurin 4.~~

The line below this paragraph, {{ABSTRACT_PUBMED_17141187}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17141187 is the PubMed ID number.

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==About this Structure==

2G9L is a [[Single protein]] structure. Full ~~crystallographic~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G9L OCA].

2G9L is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G9L OCA].

==Reference==

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[[Category: Han, K H.]]

[[Category: Amphipathic helix]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 04~~:51:20 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:52:08 2008''

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-[[Image:2g9l.jpg|left|200px]]
+{{Seed}}
+[[Image:2g9l.png|left|200px]]
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 {{STRUCTURE_2g9l|  PDB=2g9l  |  SCENE=  }}
-'''The High-resolution Solution Conformation of an Antimicrobial Peptide Gaegurin 4 and Its Mode of Membrane Interaction'''
+===The High-resolution Solution Conformation of an Antimicrobial Peptide Gaegurin 4 and Its Mode of Membrane Interaction===
-==Overview==
+<!--
-We have applied NMR spectroscopy to determine the high-resolution structure of gaegurin 4, a 37-residue antimicrobial peptide from Rana rugosa, under varying hydrophobic conditions. Even in 100% H2O, gaegurin 4 contains a nascent turn near its C-terminal Rana box. Under a more hydrophobic condition it forms two amphipathic helices, one long encompassing residues 2-23 and the other consisting of residues 25-34, similar to what has been observed in cecropin A. Functional implication of the helix-breaking kink at Gly24 in gaegurin 4 was investigated by preparing several analogs. Based upon the current and previous results, we propose a novel seaanemone-like ion pore-forming model for gaegurin 4.
+The line below this paragraph, {{ABSTRACT_PUBMED_17141187}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17141187 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17141187}}
 ==About this Structure==
-G9L is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G9L OCA].
+G9L is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G9L OCA].
 ==Reference==
@@ Line 24: / Line 28: @@
 [[Category: Han, K H.]]
 [[Category: Amphipathic helix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 04:51:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:52:08 2008''