9/23/2023 0 Comments Andersson a3222d manual![]() ![]() Introduction Hsp70 proteins are major constituents of the cellular chaperone network that assists protein folding. On the basis of these data an algorithm was established that predicts DnaK binding sites in protein sequences with high accuracy. The energetic contribution of all 20 amino acids for DnaK binding was determined. Acidic residues are excluded from the core and disfavored in flanking regions. The binding motif consists of a hydrophobic core of four to five residues enriched particularly in Leu, but also in Ile, Val, Phe and Tyr, and two flanking regions enriched in basic residues. In the folded proteins these sites are mostly buried and in the majority found in β‐sheet elements. DnaK binding sites in protein sequences occurred statistically every 36 residues. We identified binding sites and the recognition motif in substrates by screening 4360 cellulose‐bound peptides scanning the sequences of 37 biologically relevant proteins. ![]() The molecular basis for this ability to differentiate between native and non‐native conformers was investigated for the DnaK homolog of Escherichia coli. Hsp70 chaperones assist protein folding by ATP‐dependent association with linear peptide segments of a large variety of folding intermediates. Click to go to download HONDA UMT20S Tools for free. Download and view instructions HONDA UMT20S Tools online. ![]()
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