Karlin D, Belshaw R (2012) Detecting remote sequence homology in disordered proteins: discovery of conserved motifs in the N-termini of Mononegavirales phosphoproteins. PLoS One 7:e31719

Rancurel C, Pedro R, Khosravi M, Canard B, Dunker K, Karlin D (2009) Overlapping genes produce proteins with unusual sequence properties and offer insight into de novo protein creation. Journal of Virology 83:10719-36 

Ferron F, Canard B, Longhi S, Karlin D (2006) A practical overview of protein disorder prediction methods. Proteins 65:1-14

Karlin D, Ferron F, Canard B, Longhi S (2003) Structural disorder and modular organization in Paramyxovirinae N and P. Journal of General Virology 84:3239-52

Longhi S, Receveur-Brechot V, Karlin D, Johansson K, Darbon H, Bhella D, Yeo R, Finet S, Canard B (2003) The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. J. Biol. Chem. 278:18638-48

Karlin D, Longhi S, Receveur V, Canard B (2002) The N-terminal domain of the phosphoprotein of Morbilliviruses belongs to the natively unfolded class of proteins. Virology 296:251-62

Room E111

Department of Zoology

University of Oxford

South Parks Road

Oxford, OX1 3PS, UK

Phone: +44 1865 281223

(Email)

I am interested in the appearance of novelties in nature, which I study using a combination of bioinformatics and wetlab approaches (biochemistry/structural biology). Until recently, it was thought that nature did not really innovate, but rather mainly proceeded by “tinkering”. For instance new proteins would be created from "re-used" pieces of DNA, a process called duplication. However, recent studies, including mine, have shown that a significant number of proteins are in fact created "from scratch". This is especially true in viruses, in which it seems that such proteins created de novo might allow viruses to infect new hosts or to become more pathogenic.

    In spite of this, proteins created de novo have been largely neglected so far, and very little is known about them. The few studied so far look very unusual and thus I think that they might be a treasure trove of new functions and structures. With colleagues Robert Belshaw and Jonathan Grimes, I am collecting numerous viral proteins created de novo in order to study their properties. In particular, their structure is of particular interest. At present, proteins sampled in nature seem to adopt only a limited number of shapes, and we have no idea why. Studying totally new proteins might provide us with clues: is nature limited in its capacity to innovate, or have we missed “innovative” proteins?