1kfn: Difference between revisions

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[[Image:1kfn.gif|left|200px]]
{{Seed}}
[[Image:1kfn.png|left|200px]]


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{{STRUCTURE_1kfn|  PDB=1kfn  |  SCENE=  }}  
{{STRUCTURE_1kfn|  PDB=1kfn  |  SCENE=  }}  


'''Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants'''
===Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants===




==Overview==
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Native proteins exhibit precise geometric packing of atoms in their hydrophobic interiors. Nonetheless, controversy remains about the role of core side-chain packing in specifying and stabilizing the folded structures of proteins. Here we investigate the role of core packing in determining the conformation and stability of the Lpp-56 trimerization domain. The X-ray crystal structures of Lpp-56 mutants with alanine substitutions at two and four interior core positions reveal trimeric coiled coils in which the twist of individual helices and the helix-helix spacing vary significantly to achieve the most favored superhelical packing arrangement. Introduction of each alanine "layer" into the hydrophobic core destabilizes the superhelix by 1.4 kcal mol(-1). Although the methyl groups of the alanine residues pack at their optimum van der Waals contacts in the coiled-coil trimer, they provide a smaller component of hydrophobic interactions than bulky hydrophobic side-chains to the thermodynamic stability. Thus, specific side-chain packing in the hydrophobic core of coiled coils are important determinants of protein main-chain conformation and stability.
The line below this paragraph, {{ABSTRACT_PUBMED_12054830}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12054830 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12054830}}


==About this Structure==
==About this Structure==
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[[Category: Lipoprotein]]
[[Category: Lipoprotein]]
[[Category: Protein folding]]
[[Category: Protein folding]]
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