1amt: Difference between revisions

← Older edit Newer edit →

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1amt.jpg|left|200px]]
+{{Seed}}
+[[Image:1amt.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1amt|  PDB=1amt  |  SCENE=  }}
-'''A VOLTAGE-GATED ION CHANNEL MODEL INFERRED FROM THE CRYSTAL STRUCTURE OF ALAMETHICIN AT 1.5-ANGSTROMS RESOLUTION'''
+===A VOLTAGE-GATED ION CHANNEL MODEL INFERRED FROM THE CRYSTAL STRUCTURE OF ALAMETHICIN AT 1.5-ANGSTROMS RESOLUTION===
-==Overview==
+<!--
-The crystal structure of alamethicin in nonaqueous solvent has been determined, and refined at 1.5-A resolution. The molecular conformation of the three crystallographically independent molecules is largely alpha-helical with a bend in the helix axis at an internal proline residue. The helix structure is highly amphipathic as most of the solvent-accessible polar atoms lie on a narrow strip of surface parallel to the helix axis. Molecular models for the voltage-gated ion channel, with n-fold symmetry and based on the molecular conformations observed in the crystal, are characterized by strong surface complementarity, a hydrophilic interior and a hydrophobic exterior. The channel structures are stabilized by a hydrated annulus of hydrogen-bonded glutamine residues which produce the greatest restriction in the channel diameter.
+The line below this paragraph, {{ABSTRACT_PUBMED_6292726}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 6292726 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_6292726}}
 ==About this Structure==
@@ Line 23: / Line 27: @@
 [[Category: Richards, F M.]]
 [[Category: Peptide antibiotic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:27:48 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:11:14 2008''