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Homoisoleucine: A Translationally Active Leucine Surrogate of Expanded Hydrophobic Surface Area
Author(s) -
Van Deventer James A.,
Fisk John D.,
Tirrell David A.
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000731
Subject(s) - denaturation (fissile materials) , peptide , chemistry , leucine , biophysics , biochemistry , translation (biology) , amino acid , biology , nuclear chemistry , messenger rna , gene
Hil of a strong peptide! Homoisoleucine (Hil) serves as an effective surrogate for leucine with respect to protein translation in bacterial cells. Replacement of Leu by Hil stabilizes coiled‐coil peptides, as shown by the elevation of the thermal denaturation temperature. The increase in denaturation temperature is larger than that observed previously for replacement of Leu by trifluoroleucine.