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The Helix-Loop-Helix Motif

1992
Recently, families of transcription factors have been identified, having in common a region of homology in their DNA binding domain. Examples are DNA binding proteins containing zinc fingers, homeo-boxes, leucine zippers, etc. In this review I will discuss the structure and function of a new class of proteins that contain a region of homology in their ...
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Catalysis of the Cleavage of Uridine 3‘-2,2,2-Trichloroethylphosphate by a Designed Helix−Loop−Helix Motif Peptide

Journal of the American Chemical Society, 2007
A 42-residue peptide that folds into a helix-loop-helix motif and dimerizes to form a four-helix bundle has been designed to catalyze the hydrolysis of phosphodiesters. The active site on the surface of the folded catalyst is composed of two histidine and four arginine residues, with the capacity to provide general acid, general base, and/or ...
Jesus, Razkin   +2 more
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A novel type of PTD, common helix–loop–helix motif, could efficiently mediate protein transduction into mammalian cells

Biochemical and Biophysical Research Communications, 2006
Protein transduction domains (PTDs), such as HIV TAT PTD, have been widely used as delivery tools into living cells. Here we reported for the first time that the helix-loop-helix (HLH) domain of basic helix-loop-helix (bHLH) family was a novel type of PTD.
Jing, Chen   +7 more
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An Examination of Glutamic Acid in the −X Chelating Position of the Helix-Loop-Helix Calcium Binding Motif

Archives of Biochemistry and Biophysics, 1994
Poor calcium affinity was exhibited in helix-loop-helix calcium binding motifs with X-axis acid pairs containing aspartic acid in the -X chelating position. In order to increase interaction of the -X chelating residue with the cation, helix-loop-helix calcium binding motifs were synthesized containing three and four acid residues in chelating positions,
R M, Procyshyn, R E, Reid
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Enhanced Complexity and Catalytic Efficiency in the Hydrolysis of Phosphate Diesters by Rationally Designed Helix‐Loop‐Helix Motifs

ChemBioChem, 2008
AbstractHJ1, a 42‐residue peptide that folds into a helix‐loop‐helix motif and dimerizes to form a four‐helix bundle, successfully catalyzes the cleavage of “early stage” DNA model substrates in an aqueous solution at pH 7.0, with a rate enhancement in the hydrolysis of heptyl 4‐nitrophenyl phosphate of over three orders of magnitude over that of the ...
Jesus, Razkin   +3 more
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The site-selective incorporation of a NAD + cofactor mimic into a folded helix–loop–helix polypeptide motif

Journal of the Chemical Society, Perkin Transactions 2, 1997
LA-42, a polypeptide with 42 amino acid residues, has been designed to fold into a hairpin helix–loop–helix motif that can dimerise in solution to form a four-helix bundle. On the surface of the folded motif a reactive site has been introduced that contains a histidine and a lysine residue in a helical sequence.
Martin Kjellstrand   +5 more
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Designed, Functionalized Helix−Loop−Helix Motifs that Bind Human Carbonic Anhydrase II:  A New Class of Synthetic Receptor Molecules

Journal of the American Chemical Society, 2004
Polypeptides designed to fold into helix-loop-helix motifs and to dimerize to form four-helix bundles were functionalized by the introduction of a sulfonamide derivative known to bind human carbonic anhydrase II (HCAII) and one or both of the dansyl- and methoxycoumarin fluorescent probes.
Karin, Enander   +2 more
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The Site-Selective Glycosylation of a Designed Helix-Loop-Helix Polypeptide Motif

The Journal of Organic Chemistry, 1998
Linda Andersson   +2 more
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