Protein knotting through concatenation significantly reduces folding stability
نویسندگان
چکیده
منابع مشابه
Protein knotting through concatenation significantly reduces folding stability
Concatenation by covalent linkage of two protomers of an intertwined all-helical HP0242 homodimer from Helicobacter pylori results in the first example of an engineered knotted protein. While concatenation does not affect the native structure according to X-ray crystallography, the folding kinetics is substantially slower compared to the parent homodimer. Using NMR hydrogen-deuterium exchange a...
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estimation of protein stability is important for many reasons: first providing an understanding of the basic thermodynamics of the process of folding, protein engineering, and protein stability plays important role in biotechnology especially in food and protein drug design. today, proteins are used in many branches, including industrial processes, pharmaceutical industry, and medical fields. a...
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ژورنال
عنوان ژورنال: Scientific Reports
سال: 2016
ISSN: 2045-2322
DOI: 10.1038/srep39357