@article{6158aeac8fd3433191afab4c2d05dea6,
title = "Protein-protein interactions as a tool for site-specific labeling of proteins",
abstract = "Probing structures and dynamics within biomolecules using ensemble and single-molecule fluorescence resonance energy transfer requires the conjugation of fluorophores to proteins in a site-specific and thermodynamically nonperturbative fashion. Using single-molecule fluorescence-aided molecular sorting and the chymotrypsin inhibitor 2-subtilisin BPN′ complex as an example, we demonstrate that protein-protein interactions can be exploited to afford site-specific labeling of a recombinant double-cysteine variant of CI2 without the need for extensive and time-consuming chromatography. The use of protein-protein interactions for site-specific labeling of proteins is compatible with and complementary to existing chemistries for selective labeling of N-terminal cysteines, and could be extended to label multiple positions within a given polypeptide chain.",
keywords = "Alternating laser excitation, Fluorescence resonance energy transfer (FRET), Fluorescence-aided molecular sorting, Protein folding, Protein labeling, Protein-protein interaction, Single molecule spectroscopy",
author = "Marcus J{\"a}ger and Xavier Michalet and Shimon Weiss",
year = "2005",
month = aug,
doi = "10.1110/ps.051384705",
language = "אנגלית",
volume = "14",
pages = "2059--2068",
journal = "Protein Science",
issn = "0961-8368",
publisher = "Wiley-Blackwell",
number = "8",
}