作者: Dipayan Bose , Abhijit Chakrabarti
DOI: 10.1007/S00232-020-00142-1
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摘要: Spectrin is a multifunctional, multi-domain protein most well known in the membrane skeleton of mature human erythrocytes. Here we review literature on crosstalk chaperone activity spectrin with its other functionalities. We hypothesize that derived from surface exposed hydrophobic patches present individual "spectrin-repeat" domains and show competition between phospholipid binding functionality spectrin. Moreover, post-translational modifications such as glycation which shield these patches, reduce function. On hand, oligomerization linked to increase hydrophobicity seen it. note seems prefer haemoglobin client, it preferentially over denatured proteins. also interact unstable variants higher affinity than case normal haemoglobin. propose could be important cellular biochemistry haemoglobin, particularly context diseases.