Quantifying protein (dis)order

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Science  24 Feb 2017:
Vol. 355, Issue 6327, pp. 794-795
DOI: 10.1126/science.aam8036

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Twenty-five years ago, Chothia predicted that the structural domains of all proteins can be classified into about 1000 folds (1). Later studies refined this number; however, scientists also found that some proteins or parts of proteins never assume a specific fold. These regions are called intrinsically unstructured or disordered (2). Oncogenes such as p53 or breast cancer 1 (BRCA1) contain long disordered stretches, and aggregation of the disordered α-synuclein is thought to underlie Parkinson's and Alzheimer's diseases (3, 4). On page 812 of this issue, Leuenberger et al. (5) map the thermodynamic stabilities of more than 8000 proteins across four organisms, providing insights not only into the evolution of protein structure and expression in cells but also into possible molecular causes and consequences of human disease.