Making Sense of Intrinsically Disordered Proteins

• Published in: Biophysical journal Vol. 110; no. 5; pp. 1013 - 1016
• Main Author: Dyson, H. Jane
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 08-03-2016; Biophysical Society; The Biophysical Society
• Subjects: Amino Acid Sequence; Amino acids; Animals; Biophysics; Biophysics Week; Chemical reactions; Humans; Intrinsically Disordered Proteins - chemistry; Intrinsically Disordered Proteins - metabolism; Models, Biological; Models, Molecular; Molecular biology; Protein Folding; Proteins
• ISSN: 0006-3495; 1542-0086
• DOI: 10.1016/j.bpj.2016.01.030

Proteins form the molecular scaffolding of life and are essential to catalyzing the chemical reactions that sustain living systems. These characteristics have led us to think that proteins function only when folded into the right structure. The central dogma of molecular biology states that genetic information encoded in the DNA sequence is transcribed into messenger RNA and then translated into a sequence of amino acids, which folds into a protein. The mechanisms that govern how a linear sequence of amino acids folds into the correct three-dimensional structure are still not well understood.