4clg: Difference between revisions

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 {{Theoretical_model}}
-{{Seed}}
-[[Image:4clg.png|left|200px]]
-<!--
+==AN ENERGETIC EVALUATION OF A "SMITH" COLLAGEN MICROFIBRIL MODEL==
-The line below this paragraph, containing "STRUCTURE_4clg", creates the "Structure Box" on the page.
+<StructureSection load='4clg' size='340' side='right'caption='[[4clg]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CLG FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4clg FirstGlance], [https://www.ebi.ac.uk/pdbsum/4clg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4clg ProSAT]</span></td></tr>
--->
+</table>
-{{STRUCTURE_4clg|  PDB=4clg  |  SCENE=  }}
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+An energy minimized three-dimensional structure of a collagen microfibril template was constructed based on the five-stranded model of Smith (1968), using molecular modeling methods and Kollman force fields (Weiner and Kollman, 1981). For this model, individual molecules were constructed with three identical polypeptide chains [Gly-Pro-Pro)n, (Gly-Prop-Hyp)n, or (Gly-Ala-Ala)n, where n = 4, 12, and 16) coiled into a right-handed triple-helical structure. The axial distance between adjacent amino acid residues is about 0.29 nm per polypeptide chain, and the pitch of each chain is approximately 3.3 residues. The microfibril model consists of five parallel triple helices packed so that a left-handed superhelical twist exists. The structural characteristics of the computed microfibril are consistent with those obtained for collagen by X-ray diffraction and electron microscopy. The energy minimized Smith microfibril model for (Gly-Pro-Pro)12 has an axial length of about 10.2 nm (for a 36 amino acid residue chain), which gives an estimated D-spacing (234 amino acids per chain) of approximately 66.2 nm. Studies of the microfibril models (Gly-Pro-Pro)12, (Gly-Pro-Hyp)12, and (Gly-Ala-Ala)12 show that nonbonded van der Waals interactions are important for microfibril formation, while electrostatic interactions contribute to the stability of the microfibril structure and determine the specificity by which collagen molecules pack within the microfibril.
-===AN ENERGETIC EVALUATION OF A "SMITH" COLLAGEN MICROFIBRIL MODEL===
+An energetic evaluation of a "Smith" collagen microfibril model.,Chen JM, Kung CE, Feairheller SH, Brown EM J Protein Chem. 1991 Oct;10(5):535-52. PMID:1799411<ref>PMID:1799411</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4clg" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_1799411}}, adds the Publication Abstract to the page
+*[[Collagen|Collagen]]
-(as it appears on PubMed at http://www.pubmed.gov), where 1799411 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_1799411}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Theoretical Model]]
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CLG OCA].
+[[Category: Large Structures]]
-==Reference==
-<ref group="xtra">PMID:1799411</ref><references group="xtra"/>
 [[Category: Chen, J M]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 08:25:01 2010''