Structural characterization of Hsp12, the heat shock protein from Saccharomyces cerevisiae, in aqueous solution where it is intrinsically disordered and in detergent micelles where it is locally α-helical.

Structural Characterization Of Small Heat Shock Protein (Hsp12)

Nmr Structure Of Hsp12 In The Presence Of Dpc

Nmr Structure Of Hsp12, A Protein Induced By And Required For Dietary Restriction-Induced Lifespan Extension In Yeast

12KD heat shock protein [Saccharomyces cerevisiae]

K7_Hsp12p [Saccharomyces cerevisiae Kyokai no. 7]

Hsp12p [Saccharomyces cerevisiae EC1118]

15 kD glucose and lipid regulated protein [Saccharomyces cerevisiae]

12 kDa heat shock protein [Saccharomyces cerevisiae]

Hsp12p [Saccharomyces cerevisiae YJM993]

Hsp12p [Saccharomyces cerevisiae YJM1078]

lipid-binding protein HSP12 [Saccharomyces cerevisiae S288c]

RecName: Full=12 kDa heat shock protein; AltName: Full=Glucose and lipid-regulated protein

TPA: lipid-binding protein HSP12 [Saccharomyces cerevisiae S288c]

Center for Eukaryotic Structural Genomics

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax