TY - GEN
T1 - Identification of the folding inhibitors of hen-egg lysozyme
T2 - gathering the right tools
AU - Caldarini, M.
AU - Sutto, L.
AU - Camilloni, C.
AU - Vasile, F.
AU - Broglia, Ricardo Americo
AU - Tiana, G.
PY - 2010/5/1
Y1 - 2010/5/1
N2 - The unfolded state of proteins displays a surprisingly rich amount of local native structure, which appears to be critical for driving the protein to its native state. Peptides with the same sequence of the corresponding structured segments can be used to interfere with the correct folding of the protein. Using model simulations, we investigate the folding of hen-egg lysozyme, identifying its key segments. Activity assays, NMR and circular dichroism experiments are used to screen the peptides which are able to inhibit the folding of lysozyme. Few peptides, corresponding to the segments of the protein which are structured in the unfolded state, are identified to have significant inhibitory effects.
AB - The unfolded state of proteins displays a surprisingly rich amount of local native structure, which appears to be critical for driving the protein to its native state. Peptides with the same sequence of the corresponding structured segments can be used to interfere with the correct folding of the protein. Using model simulations, we investigate the folding of hen-egg lysozyme, identifying its key segments. Activity assays, NMR and circular dichroism experiments are used to screen the peptides which are able to inhibit the folding of lysozyme. Few peptides, corresponding to the segments of the protein which are structured in the unfolded state, are identified to have significant inhibitory effects.
U2 - 10.1007/s00249-009-0441-1
DO - 10.1007/s00249-009-0441-1
M3 - Conference article
SN - 0175-7571
VL - 39
SP - 911
EP - 919
JO - European Biophysics Journal
JF - European Biophysics Journal
IS - 6, Sp.Iss. Sl.
ER -