Unusual Cold Denaturation of a Small Protein Domain

Autor(en): Buchner, Ginka S.
Shih, Natalie
Reece, Amy E.
Niebling, Stephan
Kubelka, Jan
Stichwörter: Biochemistry & Molecular Biology; ENERGETICS; SOLVENT ACCESSIBILITIES; SURFACE
Erscheinungsdatum: 2012
Herausgeber: AMER CHEMICAL SOC
Journal: BIOCHEMISTRY
Volumen: 51
Ausgabe: 33
Startseite: 6496
Seitenende: 6498
Zusammenfassung: 
A thermal unfolding study of the 45-residue a-helical domain UBA(2) using circular dichroism is presented. The protein is highly thermostable and exhibits a clear cold unfolding transition with the onset near 290 K without denaturant. Cold denaturation in proteins is rarely observed in general and is quite unique among small helical protein domains. The cold unfolding was further investigated in urea solutions, and a simple thermodynamic model was used to fit all thermal and urea unfolding data. The resulting thermodynamic parameters are compared to those of other small protein domains. Possible origins of the unusual cold unfolding of UBA(2) are discussed.
ISSN: 00062960
DOI: 10.1021/bi300916v

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