Cell proteins {heat-shock protein} can increase during stress. HSP40 carries newly folded amino-acid chains. HSP60 chaperone covers proteins as they fold, to prevent partly folded proteins from hitting others, and binds to misfolded intermediates to restart folding. HSP70 holds ATP, but when ATP leaves, it binds peptide and so aids protein conformation and assembly. HSP90, such as gp96, organizes proteins from other chaperones into receptors and other multiprotein structures. HSP70 and HSP90 carry antigens to antigen-presenting-cell CD91 receptors.
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5-Chemistry-Biochemistry-Protein-Kinds
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Date Modified: 2022.0224