Molecular Chaperones: Structure-Function Relationship and their Role in Protein Folding

  • Bhaskar K. Chatterjee
  • Sarita Puri
  • Ashima Sharma
  • Ashutosh Pastor
  • Tapan K. ChaudhuriEmail author
Part of the Heat Shock Proteins book series (HESP, volume 13)


During heat shock conditions a plethora of proteins are found to play a role in maintaining cellular homeostasis. They play diverse roles from folding of non-native proteins to the proteasomal degradation of harmful aggregates. A few out of these heat shock proteins (Hsp) help in the folding of non-native substrate proteins and are termed as molecular chaperones. Various structural and functional adaptations make them work efficiently under both normal and stress conditions. These adaptations involve transitions to oligomeric structures, thermal stability, efficient binding affinity for substrates and co-chaperones, elevated synthesis during shock conditions, switching between ‘holding’ and ‘folding’ functions etc. Their ability to function under various kinds of stress conditions like heat shock, cancers, neurodegenerative diseases, and in burdened cells due to recombinant protein production makes them therapeutically and industrially important biomolecules.


Chaperone assisted folding Heat shock Molecular chaperones Protein folding Structure-function of chaperones 



The authors acknowledge the financial assistance from IIT Delhi and infrastructural facility from IIT Delhi, India. AS and AP acknowledge financial assistance from CSIR, Government of India for providing fellowships in their doctoral course programme. SP acknowledge financial assistance from UGC, Government of India for providing fellowships in their doctoral course programme. BKC acknowledges IIT Delhi for providing fellowship in the doctoral course program.


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© Springer International Publishing AG, part of Springer Nature 2018

Authors and Affiliations

  • Bhaskar K. Chatterjee
    • 1
  • Sarita Puri
    • 1
  • Ashima Sharma
    • 1
  • Ashutosh Pastor
    • 1
  • Tapan K. Chaudhuri
    • 1
    Email author
  1. 1.Kusuma School of Biological SciencesIndian Institute of Technology DelhiHauzKhasIndia

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