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University of South Florida

Molecular Medicine Faculty Publications

2021

Protein Structure

Articles 1 - 2 of 2

Full-Text Articles in Medicine and Health Sciences

On The Roles Of Intrinsically Disordered Proteins And Regions In Cell Communication And Signaling, Sarah E. Bondos, A. Keith Dunker, Vladimir N. Uversky Jan 2021

On The Roles Of Intrinsically Disordered Proteins And Regions In Cell Communication And Signaling, Sarah E. Bondos, A. Keith Dunker, Vladimir N. Uversky

Molecular Medicine Faculty Publications

For proteins, the sequence → structure → function paradigm applies primarily to enzymes, transmembrane proteins, and signaling domains. This paradigm is not universal, but rather, in addition to structured proteins, intrinsically disordered proteins and regions (IDPs and IDRs) also carry out crucial biological functions. For these proteins, the sequence → IDP/IDR ensemble → function paradigm applies primarily to signaling and regulatory proteins and regions. Often, in order to carry out function, IDPs or IDRs cooperatively interact, either intra- or inter-molecularly, with structured proteins or other IDPs or intermolecularly with nucleic acids. In this IDP/IDR thematic collection published in Cell Communication …


Disphscan: A Multi-Sequence Web Tool For Predicting Protein Disorder As A Function Of Ph, Carlos Pintado-Grima, Valentín Iglesias, Jaime Santos, Vladimir N. Uversky, Salvador Ventura Jan 2021

Disphscan: A Multi-Sequence Web Tool For Predicting Protein Disorder As A Function Of Ph, Carlos Pintado-Grima, Valentín Iglesias, Jaime Santos, Vladimir N. Uversky, Salvador Ventura

Molecular Medicine Faculty Publications

Proteins are exposed to fluctuating environmental conditions in their cellular context and during their biotechnological production. Disordered regions are susceptible to these fluctuations and may experience solvent-dependent conformational switches that affect their local dynamism and activity. In a recent study, we modeled the influence of pH in the conformational state of IDPs by exploiting a charge–hydrophobicity diagram that considered the effect of solution pH on both variables. However, it was not possible to predict context-dependent transitions for multiple sequences, precluding proteome-wide analysis or the screening of collections of mutants. In this article, we present DispHScan, the first computational tool dedicated …