A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization.
Haslbeck
Martin
M
Institut für Organische Chemie und Biochemie, Fakultät für Chemie, Technische Universität München, D-85747 Garching, Germany.
Ignatiou
Athanasios
A
Saibil
Helen
H
Helmich
Sonja
S
Frenzl
Elke
E
Stromer
Thusnelda
T
Buchner
Johannes
J
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D006358:Hot Temperature; D018832:Molecular Chaperones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D016415:Sequence Alignment; D013552:Swine
C499528:HSP26 protein, S cerevisiae; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D029701:Saccharomyces cerevisiae Proteins