Role of aromatic side chains in the folding and thermodynamic stability of integral membrane proteins.

Role of aromatic side chains in the folding and thermodynamic stability of integral membrane proteins. Research Abstract Details 

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Role of aromatic side chains in the folding and thermodynamic stability of integral membrane proteins. Abstract Text:

Heedeok Hong,Sangho Park,Ricardo H Flores ,Dennis Rinehart,Lukas K Tamm,

Aromatic residues are frequently found in helical and beta-barrel integral membrane proteins enriched at the membrane-water interface. Although the importance of these residues in membrane protein folding has been rationalized by thermodynamic partition measurements using peptide model systems, their contribution to the stability of bona fide membrane proteins has never been demonstrated. Here, we have investigated the contribution of interfacial aromatic residues to the thermodynamic stability of the beta-barrel outer membrane protein OmpA from Escherichia coli in lipid bilayers by performing extensive mutagenesis and equilibrium folding experiments. Isolated interfacial tryptophanes contribute -2.0 kcal/mol, isolated interfacial tyrosines contribute -2.6 kcal/mol, and isolated interfacial phenylalanines contribute -1.0 kcal/mol to the stability of this protein. These values agree well with the prediction from the Wimley-White interfacial hydrophobicity scale, except for tyrosine residues, which contribute more than has been expected from the peptide models. Double mutant cycle analysis reveals that interactions between aromatic side chains become significant when their centroids are separated by less than 6 A but are nearly insignificant above 7 A. Aromatic-aromatic side chain interactions are on the order of -1.0 to -1.4 kcal/mol and do not appear to depend on the type of aromatic residue. These results suggest that the clustering of aromatic side chains at membrane interfaces provides an additional heretofore not yet recognized driving force for the folding and stability of integral membrane proteins.

Role of aromatic side chains in the folding and thermodynamic stability of integral membrane proteins. Publishing Authors By Initials

H Hong,S Park,RH ,D Rinehart,LK Tamm,

For similar organic chemicals: urea research abstracts see: organic chemicals: urea research

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Role of aromatic side chains in the folding and thermodynamic stability of integral membrane proteins. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Journal of the American Chemical Society

VOLUME: 129

Page Numbers: 8320-7

Journal Abbreviation: J. Am. Chem. Soc.

ISSN: 0002-7863

DAY: 12

MONTH: 06

YEAR: 2007

Role of aromatic side chains in the folding and thermodynamic stability of integral membrane proteins. Information

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LANGUAGE: eng

NlmUniqueID: 7503056

Role of aromatic side chains in the folding and thermodynamic stability of integral membrane proteins. Keywords Mesh Terms:

KEYWORDS: Urea

MESH TERMS: chemistry

Chemical & Substance for Abstract: Role of aromatic side chains in the folding and thermodynamic stability of integral membrane proteins. Information

Substance Name: Urea

Registry Number: 57-13-6

Grant and Affiliation Information for Role of aromatic side chains in the folding and thermodynamic stability of integral membrane proteins.

AFFILIATION: Department of Molecular Physiology and Biological Physics, University of Virginia Health System, Charlottesville, VA 22908-0736, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM051329

ACRONYM: GM

MEDLINETA: J Am Chem Soc

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