Computational investigation of retro‐isomer equilibrium structures: Intrinsically disordered, foldable, and cyclic peptides
Sign Up to like & getrecommendations! Published in 2019 at "FEBS Letters"
DOI: 10.1002/1873-3468.13558
Abstract: We use all‐atom modeling and advanced‐sampling molecular dynamics simulations to investigate quantitatively the effect of peptide bond directionality on the equilibrium structures of four linear (two foldable, two disordered) and two cyclic peptides. We find… read more here.
Keywords: retro; computational investigation; cyclic peptides; equilibrium structures ... See more keywords
dentification of intrinsically disordered regions in hub genes of acute myeloid leukemia: a bioinformatics approach.
Sign Up to like & getrecommendations! Published in 2021 at "Biotechnology and applied biochemistry"
DOI: 10.1002/bab.2287
Abstract: Acute myeloid leukemia (AML) is the most common acute leukemia in adults. Over the past decades, there has been a great challenge in the treatment of AML. A combination of gene expression profiling with computational… read more here.
Keywords: myeloid leukemia; hub genes; acute myeloid; leukemia ... See more keywords
An Enantiomeric Fragment Pair (EFP) Approach for the Study of Cellular Uptake of Intrinsically Disordered Proteins
Sign Up to like & getrecommendations! Published in 2022 at "ChemBioChem"
DOI: 10.1002/cbic.202200146
Abstract: The study of intrinsically disordered and amyloidogenic proteins poses a major challenge to researchers due to the propensity of the system to aggregate and to form amyloid fibrils and deposits. This intrinsic nature limits the… read more here.
Keywords: intrinsically disordered; disordered proteins; enantiomeric fragment; approach study ... See more keywords
Hemin and bile pigments are the secondary structure regulators of intrinsically disordered antimicrobial peptides.
Sign Up to like & getrecommendations! Published in 2018 at "Chirality"
DOI: 10.1002/chir.22784
Abstract: The interaction of protoporphyrin compounds of human origin with the major bee venom component melittin (26 a.a., Z +6) and its hybrid derivative (CM15, 15 a.a., Z +6) were studied by a combination of various… read more here.
Keywords: pigments secondary; secondary structure; hemin bile; intrinsically disordered ... See more keywords
Interactions between the Intrinsically Disordered Proteins β‐Synuclein and α‐Synuclein
Sign Up to like & getrecommendations! Published in 2018 at "PROTEOMICS"
DOI: 10.1002/pmic.201800109
Abstract: Several intrinsically disordered proteins have been implicated in the process of amyloid fibril formation in neurodegenerative disease, and developing approaches to inhibit the aggregation of these intrinsically disordered proteins is critical for establishing effective therapies… read more here.
Keywords: beta synuclein; synuclein; alpha synuclein; disordered proteins ... See more keywords
Intrinsically disordered inhibitor of glutamine synthetase is a functional protein with random‐coil‐like pKa values
Sign Up to like & getrecommendations! Published in 2017 at "Protein Science"
DOI: 10.1002/pro.3157
Abstract: The sequential action of glutamine synthetase (GS) and glutamate synthase (GOGAT) in cyanobacteria allows the incorporation of ammonium into carbon skeletons. In the cyanobacterium Synechocystis sp. PCC 6803, the activity of GS is modulated by… read more here.
Keywords: protein; glutamine synthetase; random coil; pka values ... See more keywords
An enhancer sequence in the intrinsically disordered region of FtsZ promotes polymer‐guided substrate processing by ClpXP protease
Sign Up to like & getrecommendations! Published in 2022 at "Protein Science"
DOI: 10.1002/pro.4306
Abstract: The essential bacterial division protein in Escherichia coli, FtsZ, assembles into the FtsZ‐ring at midcell and recruits other proteins to the division site to promote septation. A region of the FtsZ amino acid sequence that… read more here.
Keywords: intrinsically disordered; region ftsz; region; polymer guided ... See more keywords
The return of the rings: Evolutionary convergence of aromatic residues in the intrinsically disordered regions of RNA‐binding proteins for liquid–liquid phase separation
Sign Up to like & getrecommendations! Published in 2022 at "Protein Science"
DOI: 10.1002/pro.4317
Abstract: Aromatic residues appeared relatively late in the evolution of protein sequences to stabilize the globular proteins' folding core and are less in the intrinsically disordered regions (IDRs). Recent advances in protein liquid–liquid phase separation (LLPS)… read more here.
Keywords: intrinsically disordered; liquid phase; aromatic residues; disordered regions ... See more keywords
Distinguishing features of fold‐switching proteins
Sign Up to like & getrecommendations! Published in 2023 at "Protein Science"
DOI: 10.1002/pro.4596
Abstract: Though many folded proteins assume one stable structure that performs one function, a small‐but‐increasing number remodel their secondary and tertiary structures and change their functions in response to cellular stimuli. These fold‐switching proteins regulate biological… read more here.
Keywords: distinguishing features; fold switching; intrinsically disordered; fold switchers ... See more keywords
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
Structural Analyses of Intrinsically Disordered Proteins by Small-Angle X-Ray Scattering.
Sign Up to like & getrecommendations! Published in 2020 at "Methods in molecular biology"
DOI: 10.1007/978-1-0716-0524-0_12
Abstract: Small-angle X-ray scattering (SAXS) is a low-resolution method for the structural characterization of biological macromolecules in solution. Information about the overall structural features provided by SAXS is highly complementary to X-ray crystallography, nuclear magnetic resonance… read more here.
Keywords: small angle; structural analyses; angle ray; ray scattering ... See more keywords