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RFP Journal of Biochemistry and Biophysics

Volume  1, Issue 2, July - December 2016, Pages 99-110
 

Review Article

Protein Folding, Denaturation and Stability: A Brief Introduction

Shah Ubaid-ullah1*, M Afzal Zargar1,2, Shabir H Qureshi1, Masrat Maswal3 , Javid Ahmad Parray4 , Ummer Rashid Zargar5

1 Department of Biotechnology, School of Life Sciences, Central University of Kashmir (CUK), Transit Campus Sonwar, Srinagar, India – 190004. 2 Department of Biochemistry, University of Kashmir, Srinagar – 190006. 3 Department of Physics, School

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Abstract

 Protein folding refers to the process and path by which a nascent polypeptide obtains its 3-D or native state. Over the years the field of protein folding has evolved, as are the questions pertaining with this perplexing field. Levinthal, was first to propose that the folding code for a polypeptide to fold, is its primary structure or sequence of amino acids. But, still in present era, a major challenge is to predict the native structure of a protein solely from its sequence. This has become more challenging with ever increasing sequence data being accumulated with each day. Thus, protein folding problem continues to be a complex problem to be solved and has perplexed scientists over the decades. In this article, main focus will be to sum up the broad aspects of protein folding, protein denaturation and discuss in brief the methods to estimate protein stability.

Keywords: Protein Folding; Denaturation; Stability; Equilibrium Methods; Differential Scanning Calorimetry.


Corresponding Author : Shah Ubaid-ullah1*