Premium
Sequence determinants of folding and stability for the P22 Arc repressor dimer
Author(s) -
Salier Robert T.,
Milla Marcos E.,
Waldburger Carey D.,
Brown Bronwen M.,
Schildbach Joel F.
Publication year - 1996
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.10.1.8566546
Subject(s) - folding (dsp implementation) , dimer , hydrogen bond , chemistry , lattice protein , repressor , side chain , hydrophobic effect , crystallography , protein folding , arc (geometry) , sequence (biology) , core (optical fiber) , biophysics , chemical physics , molecule , biochemistry , materials science , polymer , biology , organic chemistry , geometry , mathematics , transcription factor , electrical engineering , gene , engineering , composite material
The Arc repressor is a small, homodi‐ meric protein. Studies of mutant proteins show that the side chains that form the hydrophobic core are the most important determinants of structure. A variety of hydrogen bonds and salt bridges also contribute to stabilization of the native structure, but these can often be replaced by hydrophobic interactions. The transition state for folding/unfolding is dimeric and contains a large amount of buried hydrophobic surface, but the β‐sheet of native Arc is not formed. Moreover, relatively little side chain information appears to be used in the transition state, suggesting that tight packing of the hydrophobic core and optimization of hydrogen‐bond geometry are events that occur later in folding.—Sauer, R. T., Milla, M. E., Waldburger, C. D., Brown, B. M., Schildbach, J. F. Sequence determinants of folding and stability for the P22 Arc repressor dimer. FASEB J. 10, 42‐48 (1996)