Structural Characterization of small heat shock protein (Hsp12)

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.

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]

10mM MOPS, 100mM NaCl, 100mM SDS, 5mM DTT, 3mM NaN3

Center for Eukaryotic Structural Genomics

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax