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The proregion of growth and differentiation factor (<jats:styled-content style=\"fixed-case\">GDF<\/jats:styled-content>)5 comprises 354 residues.<jats:styled-content style=\"fixed-case\">GDF<\/jats:styled-content>5 therefore belongs to the group of those growth factors with the largest proregions. Here, we report a biophysical analysis of the proform (pro<jats:styled-content style=\"fixed-case\">GDF<\/jats:styled-content>5) and the separate proregion. In the absence of the mature part, the proregion folds reversibly to form a monomeric polypeptide that is stabilized by an intramolecular disulfide bond. In the context of the mature part, i.e. in pro<jats:styled-content style=\"fixed-case\">GDF<\/jats:styled-content>5, the proregion shows increased thermodynamic stability and contains a higher proportion of secondary structural elements than in its isolated form. A subdomain within the proregion represents a well\u2010folded structure as monitored via biophysical analysis and<jats:styled-content style=\"fixed-case\">NMR<\/jats:styled-content>spectroscopy. Furthermore, two point mutations that are associated with skeletal malformations lead to reduced thermodynamic stability, which is interpreted on the basis of a homology model with the structure of the related latency\u2010associated peptide, representing the proregion of transforming growth factor\u2010\u03b21.<\/jats:p>","DOI":"10.1111\/febs.13025","type":"journal-article","created":{"date-parts":[[2014,9,1]],"date-time":"2014-09-01T05:29:01Z","timestamp":1409549341000},"page":"4866-4877","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Biophysical and structural characterization of a folded core domain within the proregion of growth and differentiation factor\u20105"],"prefix":"10.1111","volume":"281","author":[{"given":"Tino","family":"Thieme","sequence":"first","affiliation":[{"name":"Technical Biochemistry Martin\u2010Luther\u2010University Halle\u2010Wittenberg 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