From local structure to a global framework: recognition of protein folds

Author:

Joseph Agnel Praveen1234,de Brevern Alexandre G.3456

Affiliation:

1. Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford, Didcot OX11 0QX, UK

2. National Centre for Biological Sciences, GKVK, Bellary Road, Bangalore 560065, India

3. INSERM, U1134, DSIMB, 75739 Paris, France

4. Université Paris Diderot, Sorbonne Paris Cité, UMR_S 1134, 75739 Paris, France

5. Institut National de la Transfusion Sanguine (INTS), 75739 Paris, France

6. Laboratoire d'Excellence, GR-Ex, 75739 Paris, France

Abstract

Protein folding has been a major area of research for many years. Nonetheless, the mechanisms leading to the formation of an active biological fold are still not fully apprehended. The huge amount of available sequence and structural information provides hints to identify the putative fold for a given sequence. Indeed, protein structures prefer a limited number of local backbone conformations, some being characterized by preferences for certain amino acids. These preferences largely depend on the local structural environment. The prediction of local backbone conformations has become an important factor to correctly identifying the global protein fold. Here, we review the developments in the field of local structure prediction and especially their implication in protein fold recognition.

Publisher

The Royal Society

Subject

Biomedical Engineering,Biochemistry,Biomaterials,Bioengineering,Biophysics,Biotechnology

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