Internal Packing of Helical Membrane Proteins

Helix packing is important in the folding, stability, and association of membrane proteins. Packing analysis of the helical portions of 7 integral membrane proteins and 37 soluble proteins show that the helices in membrane proteins have higher packing values (0.431) than in soluble proteins (0.405)....

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2000-05, Vol.97 (11), p.5796-5801
Main Authors: Eilers, Markus, Shekar, Srinivasan C., Shieh, Ted, Smith, Steven O., Fleming, Patrick J.
Format: Article
Language:English
Subjects:
Amides
Amino acids
Amino Acids - chemistry
Amino Acids - classification
Animals
Arithmetic mean
Atoms
Biochemistry
Biological Sciences
Cytochromes
Membrane proteins
Membrane Proteins - chemistry
Membranes
Oxidases
P branes
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Surface areas
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Summary:Helix packing is important in the folding, stability, and association of membrane proteins. Packing analysis of the helical portions of 7 integral membrane proteins and 37 soluble proteins show that the helices in membrane proteins have higher packing values (0.431) than in soluble proteins (0.405). The highest packing values in integral membrane proteins originate from small hydrophobic (G and A) and small hydroxyl-containing (S and T) amino acids, whereas in soluble proteins large hydrophobic and aromatic residues have the highest packing values. The highest packing values for membrane proteins are found in the transmembrane helix-helix interfaces. Glycine and alanine have the highest occurrence among the buried amino acids in membrane proteins, whereas leucine and alanine are the most common buried residue in soluble proteins. These observations are consistent with a shorter axial separation between helices in membrane proteins. The tight helix packing revealed in this analysis contributes to membrane protein stability and likely compensates for the lack of the hydrophobic effect as a driving force for helix-helix association in membranes.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.97.11.5796