Interfacial Water Ordering Is Insufficient to Explain Ice-Nucleating Protein Activity
نویسندگان
چکیده
منابع مشابه
Ice-nucleating bacteria control the order and dynamics of interfacial water
Ice-nucleating organisms play important roles in the environment. With their ability to induce ice formation at temperatures just below the ice melting point, bacteria such as Pseudomonas syringae attack plants through frost damage using specialized ice-nucleating proteins. Besides the impact on agriculture and microbial ecology, airborne P. syringae can affect atmospheric glaciation processes,...
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Transcription factors (TFs) are DNA-binding proteins that regulate gene expression. Sequence-specific TFs recognize DNA via specific amino acid-base hydrogen bonds and contacts that read local DNA shape1. Studying base and shape readout modes of TFs in vivo has been challenging due to technical issues associated with current approaches for mapping TF-binding sites (TFBSs). We recently introduce...
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Proteins bind DNA through combinations of DNA base and shape recognition1. DNA base recognition refers to a unique arrangement of protein interactions with functional groups on the four DNA bases. Shape recognition refers to protein interactions with specific twists and turns of short stretches of DNA that may deviate from the average three-dimensional shape of B-form DNA. A recent study by Zen...
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Chemical and biological properties of the ice nucleating sites of Pseudomonas syringae, strain C-9, and Erwinia herbicola have been characterized. The ice nucleating activity (INA) for both bacteria was unchanged in buffers ranging from pH 5.0 to 9.2, suggesting that there were no essential groups for which a change in charge in this range was critical. The INA of both bacteria was also unaffec...
متن کاملProtein packing defects "heat up" interfacial water.
Ligands must displace water molecules from their corresponding protein surface binding site during association. Thus, protein binding sites are expected to be surrounded by non-tightly-bound, easily removable water molecules. In turn, the existence of packing defects at protein binding sites has been also established. At such structural motifs, named dehydrons, the protein backbone is exposed t...
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ژورنال
عنوان ژورنال: The Journal of Physical Chemistry Letters
سال: 2020
ISSN: 1948-7185,1948-7185
DOI: 10.1021/acs.jpclett.0c03163