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Heat shock protein 70 (HSP70) is a molecular chaperone that is expressed in response to stress. HSP70 binds to its protein substrates and stabilize them against denaturation or aggregation until the conditions improve. In addition to its functions during a stress response, HSP70 has multiple responsibilities during normal growth; it assists in the folding of newly synthesized proteins, the subcellular transport of proteins and vesicles, the formation and dissociation of complexes 5 and the degradation of unwanted proteins. The present study describes the cloning, sequence analysis and 3D structure prediction of Bubalus bubalis HSP70. The cloned sequence consists of an open reading frame of 641 amino acid residues. Sequence alignment and predicted 3Dstructure revealed that the HSP70 consists of the signature sequences of the HSP super family. The present study reports the molecular modeling / 3D-structure prediction of HSP70.
[Hitesh N Pawar, Ravi Kant Agrawal, Ramneek and G.S.Brah (2014); In silico analysis of Stress Inducible 70 kDa Heat Shock Protein of Bubalus bubalis Int. J. of Adv. Res. 2 (2). 0] (ISSN 2320-5407). www.journalijar.com
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