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Open access, freely available online Synopses of Research Articles Simple Peptides Stabilize Mighty Membrane Proteins for Study DOI: 10.1371/journal.pbio.0030259 Cell membranes are largely made of proteins, and membrane proteins account for about a third of all genes. Despite their importance, they are stabilize the dauntingly large protein complex photosystem I (PS-I), an integral part of the photosynthetic machinery. The molecule they made, abbreviated A6K, links six units of the hydrophobic amino acid alanine to one of the devilishly hard to isolate and stabilize, and therefore are hard to study.The problem lies in their structure: membrane proteins have at least one hydrophobic domain, composed of a stretch of water- repelling amino acids, which holds the protein snugly in the lipid membrane. Purifying such a protein in an aqueous medium makes the hydrophobic parts aggregate, destroying the protein’s delicate three-dimensional structure and often disrupting its function.The alternative is to extract the protein with a detergent, a two-headed“Janus”molecule with both hydrophobic and hydrophilic ends.The protein remains surrounded by the hydrophobic ends, while water clusters at the hydrophilic ends, easing the protein out of the membrane and into solution, where it can be studied. To date, though, relatively few hydrophilic amino acid lysine.The authors used it to stabilize PS-I and then attached the detergent–protein complex to a glass slide, allowed it to dry, and examined the stability of PS-I by testing its ?uorescence. Intact PS-I emits red light with a characteristic peak wavelength; as it degrades, this peak subsides and is replaced by another, bluer peak. Even the two best standard detergents did poorly at maintaining the red peak. In contrast, the spectrum after A6K extraction was almost a perfect match for the normal one, indicating the complex was largely intact after drying. Furthermore, the complex appeared to remain stable for up to three week