Structural Basis for Client Recognition and Activity of Hsp40 Chaperones
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Structural Basis for Client Recognition and Activity of Hsp40 Chaperones
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2024-05-15
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Figure S1 - N-Terminal Helix-Cap in α-Helix 2 Modulates β-State Misfolding in Rabbit and Hamster Prion Proteins
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A Chaperonin Subunit with Unique Structures Is Essential for Folding of a Specific Substrate
Type I chaperonins are large, double-ring complexes present in bacteria (GroEL), mitochondria (Hsp60), and chloroplasts (Cpn60), which are involved in mediating the folding of newly synthesized, trans
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