Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Macromolecular crowding effects on two homologs of ribosomal protein s16: protein-dependent structural changes and local interactions.

Biophysical journal - 15 Jul 2014

Mikaelsson Therese, Ådén Jörgen, Wittung-Stafshede Pernilla, Johansson Lennart B-Å

Abstract excerpt

Proteins function in cellular environments that are crowded with biomolecules, and in this reduced available space, their biophysical properties may differ from those observed in dilute solutions in vitro. Here, we investigated the effects of a synthetic macromolecular crowding agent, dextran 20, on the folded states of hyperthermophilic (S16Thermo) and mesophilic (S16Meso) homologs of the ribosomal protein S16....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Dextrans

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Aggregates

Share to Protein Denaturation

Share to Protein Multimerization

Share to Ribosomal Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 25028882
DOI: 10.1016/j.bpj.2014.05.038
PMCID: PMC4104055

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Macromolecular crowding effects on two homologs of ribosomal protein s16: protein-dependent structural changes and local interactions.PMID 25028882Read ↗

Extreme temperature tolerance of a hyperthermophilic protein coupled to residual structure in the unfolded state.Semantic proximity Read ↗

Solution structures and backbone dynamics of the ribosomal protein S6 and its permutant P(54-55).Semantic proximity Read ↗

An improved molecular crowding sensor CRONOS for detection of crowding changes in membrane-less organelles under pathological conditionsSemantic proximity Read ↗

Burst-phase expansion of native protein prior to global unfolding in SDS.Semantic proximity Read ↗

Backbone-driven collapse in unfolded protein chains.Semantic proximity Read ↗

Effects of tryptophan microenvironment, soluble domain, and vesicle size on the thermodynamics of membrane protein folding: lessons from the transmembrane protein OmpA.Semantic proximity Read ↗

Effect of circular permutations on transient partial unfolding in proteins.Semantic proximity Read ↗

Molecular crowders and cosolutes promote folding cooperativity of RNA under physiological ionic conditions.Semantic proximity Read ↗

Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis.Semantic proximity Read ↗

Quaternary structure of human small heat shock protein HSPB6 (Hsp20) in crowded media modeled by trimethylamine N-oxide (TMAO): Effect of protein phosphorylation.Semantic proximity Read ↗

The unfolded state of NTL9 is compact in the absence of denaturant.Semantic proximity Read ↗

Molecular crowding: impacts on the activity of the 10-23 DNAzymeSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.