Self‐assembling systems comprising intrinsically disordered protein polymers like elastin‐like recombinamers
Sign Up to like & getrecommendations! Published in 2021 at "Journal of Peptide Science"
DOI: 10.1002/psc.3362
Abstract: Despite lacking cooperatively folded structures under native conditions, numerous intrinsically disordered proteins (IDPs) nevertheless have great functional importance. These IDPs are hybrids containing both ordered and intrinsically disordered protein regions (IDPRs), the structure of which… read more here.
Keywords: disordered protein; like recombinamers; protein; intrinsically disordered ... See more keywords
Intrinsically disordered protein NUPR1 binds to the armadillo-repeat domain of Plakophilin 1.
Sign Up to like & getrecommendations! Published in 2020 at "International journal of biological macromolecules"
DOI: 10.1016/j.ijbiomac.2020.12.193
Abstract: Plakophilin 1 (PKP1), a member of the armadillo repeat family of proteins, is a scaffold component of desmosomes, which are key structural components for cell-cell adhesion. However, PKP1 can be also found in the nucleus… read more here.
Keywords: pkp1; plakophilin; armadillo repeat; disordered protein ... See more keywords
Predicting Protein-Protein Interfaces that Bind Intrinsically Disordered Protein Regions.
Sign Up to like & getrecommendations! Published in 2019 at "Journal of molecular biology"
DOI: 10.1016/j.jmb.2019.06.010
Abstract: A long-standing goal in biology is the complete annotation of function and structure on all protein-protein interactions, a large fraction of which is mediated by intrinsically disordered protein regions (IDRs). However, our knowledge base of… read more here.
Keywords: protein; protein protein; biology; protein regions ... See more keywords
How do intrinsically disordered protein regions encode a driving force for liquid-liquid phase separation?
Sign Up to like & getrecommendations! Published in 2020 at "Current opinion in structural biology"
DOI: 10.1016/j.sbi.2020.09.004
Abstract: Liquid-liquid phase separation is the mechanism underlying the formation of biomolecular condensates. Disordered protein regions often drive phase separation, but molecular interactions of disordered protein regions are not well understood, sometimes leading to the conflation… read more here.
Keywords: phase separation; phase; liquid; protein regions ... See more keywords
Disordered Protein Kinase Regions in Regulation of Kinase Domain Cores.
Sign Up to like & getrecommendations! Published in 2019 at "Trends in biochemical sciences"
DOI: 10.1016/j.tibs.2018.12.002
Abstract: Since publication of the crystal structure of protein kinase (PK)A three decades ago, a structural portrait of the conserved kinase core has been drawn. The next challenge is to elucidate structures of full-length kinases and… read more here.
Keywords: regulation kinase; kinase; kinase regions; regions regulation ... See more keywords
Controlling Structure and Dimensions of a Disordered Protein via Mutations
Sign Up to like & getrecommendations! Published in 2019 at "Biochemistry"
DOI: 10.1021/acs.biochem.9b00678
Abstract: The dimensions of intrinsically disordered proteins (IDPs) are sensitive to small energetic-entropic differences between intramolecular and protein–solvent interactions. This is commonly observed on modulating solvent composition and temperature. However, the inherently heterogeneous conformational landscape of… read more here.
Keywords: controlling structure; dimensions disordered; structure; via mutations ... See more keywords
Preparation of Bioderived and Biodegradable Surfactants Based on an Intrinsically Disordered Protein Sequence.
Sign Up to like & getrecommendations! Published in 2022 at "Biomacromolecules"
DOI: 10.1021/acs.biomac.2c00051
Abstract: Surfactants, block copolymers, and other types of micellar systems are used in a wide variety of biomedical and industrial processes. However, most commonly used surfactants are synthetically derived and pose environmental and toxicological concerns throughout… read more here.
Keywords: sequence; domain; biodegradable surfactants; disordered protein ... See more keywords
Disordered Protein Stabilization by Co-Assembly of Short Peptides Enables Formation of Robust Membranes.
Sign Up to like & getrecommendations! Published in 2021 at "ACS applied materials & interfaces"
DOI: 10.1021/acsami.1c22136
Abstract: Molecular self-assembly is a spontaneous natural process resulting in highly ordered nano to microarchitectures. We report temperature-independent formation of robust stable membranes obtained by the spontaneous interaction of intrinsically disordered elastin-like polypeptides (ELPs) with short… read more here.
Keywords: formation robust; assembly short; disordered protein; stabilization assembly ... See more keywords
Self-assembly of globular proteins with intrinsically disordered protein polyelectrolytes and block copolymers.
Sign Up to like & getrecommendations! Published in 2022 at "Soft matter"
DOI: 10.1039/d2sm00415a
Abstract: Intrinsically disordered polypeptides are a versatile class of materials, combining the biocompatibility of peptides with the disordered structure and diverse phase behaviors of synthetic polymers. Synthetic polyelectrolytes are capable of complex phase behavior when mixed… read more here.
Keywords: intrinsically disordered; protein polyelectrolytes; phase; disordered protein ... See more keywords
An intrinsically disordered protein region encoded by the human disease gene CLEC16A regulates mitophagy
Sign Up to like & getrecommendations! Published in 2022 at "Autophagy"
DOI: 10.1080/15548627.2022.2080383
Abstract: ABSTRACT CLEC16A regulates mitochondrial health through mitophagy and is associated with over 20 human diseases. However, the key structural and functional regions of CLEC16A, and their relevance for human disease, remain unknown. Here, we report… read more here.
Keywords: intrinsically disordered; human disease; protein region; clec16a ... See more keywords
CLIP: accurate prediction of disordered linear interacting peptides from protein sequences using co-evolutionary information
Sign Up to like & getrecommendations! Published in 2022 at "Briefings in bioinformatics"
DOI: 10.1093/bib/bbac502
Abstract: One of key features of intrinsically disordered regions (IDRs) is facilitation of protein-protein and protein-nucleic acids interactions. These disordered binding regions include molecular recognition features (MoRFs), short linear motifs (SLiMs) and longer binding domains. Vast… read more here.
Keywords: disordered protein; evolutionary information; binding regions; protein binding ... See more keywords