activity
19982007
most citedInhibition of protein crystallization by evolutionary negative design

96 citations · 140 across the 6 of their papers we have counts for

collaborators
Showing q-bio.BMShow all

6 papers · 1 filter

q-bio.BM2009121 cited

Generic Mechanism of Emergence of Amyloid Protofilaments from Disordered Oligomeric aggregates

Stefan Auer, Filip Meersman, Christopher M. Dobson +1

The presence of oligomeric aggregates, which is often observed during the process of amyloid formation, has recently attracted much attention since it has been associated with neur…

q-bio.BM2009103 cited

Self-Templated Nucleation in Peptide and Protein aggregation

Stefan Auer, Christopher M. Dobson, Michele Vendruscolo +1

Peptides and proteins exhibit a common tendency to assemble into highly ordered fibrillar aggregates, whose formation proceeds in a nucleation-dependent manner that is often preced…

q-bio.BM2004

Looking at structure, stability, and evolution of proteins through the principal eigenvector of contact matrices and hydrophobicity profiles

Ugo Bastolla, Markus Porto, H. Eduardo Roman +1

We review and further develop an analytical model that describes how thermodynamic constraints on the stability of the native state influence protein evolution in a site-specific m…

q-bio.BM2004

Prediction of site-specific amino acid distributions and limits of divergent evolutionary changes in protein sequences

Markus Porto, H. Eduardo Roman, Michele Vendruscolo +1

We derive an analytic expression for site-specific stationary distributions of amino acids from the Structurally Constrained Neutral (SCN) model of protein evolution with conservat…

q-bio.BM20042 cited

The principal eigenvector of contact matrices and hydrophobicity profiles in proteins

Ugo Bastolla, Markus Porto, H. Eduardo Roman +1

With the aim to study the relationship between protein sequences and their native structures, we adopt vectorial representations for both sequence and structure. The structural rep…

q-bio.BM200496 cited

Inhibition of protein crystallization by evolutionary negative design

Jonathan P. K. Doye, Ard A. Louis, Michele Vendruscolo

In this perspective we address the question: why are proteins seemingly so hard to crystallize? We suggest that this is because of evolutionary negative design, i.e. proteins have…