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Article

The Ambivalent Role of Proline Residues in an Intrinsically Disordered Protein: From Disorder Promoters to Compaction Facilitators.

Journal of molecular biology - 17 Apr 2020

Mateos Borja, Conrad-Billroth Clara, Schiavina Marco, Beier Andreas, Kontaxis Georg, Konrat Robert, Felli Isabella C, Pierattelli Roberta

Abstract excerpt

Intrinsically disordered proteins (IDPs) carry out many biological functions. They lack a stable three-dimensional structure, but rather adopt many different conformations in dynamic equilibrium. The interplay between local dynamics and global rearrangements is key for their function. In IDPs, proline residues are significantly enriched. Given their unique physicochemical and structural properties, a more...

Topics

Animals
Avian Proteins
Carbon-13 Magnetic Resonance Spectroscopy
Coturnix
Humans
Mutation
Nuclear Magnetic Resonance, Biomolecular
Osteopontin
Proline
Protein Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Multimerization

Protein Stability

Source

Identifiers

PMID: 31794728
DOI: 10.1016/j.jmb.2019.11.015

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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