Proteins articles from across Nature Portfolio

Proteins are biopolymers of amino acids (polypeptides), joined by peptide bonds, that are generated by ribosomes. The amino acid sequence, encoded by its gene, determines a protein’s structure and function. Newly synthesized proteins can be modified by post-translational modification, altering its protein folding, stability and activity. Proteins often associate into protein–protein interaction networks for function.

Related Subjects

Latest Research and Reviews

Optimization of plasma-based BioID identifies plasminogen as a ligand of ADAMTS13
- Hasam Madarati
- Veronica DeYoung
- Colin A. Kretz
ResearchOpen Access20 Apr 2024 Scientific Reports
Volume: 14, P: 9073
Type 1 secretion necessitates a tight interplay between all domains of the ABC transporter
- Manuel T. Anlauf
- Florestan L. Bilsing
- Lutz Schmitt
ResearchOpen Access18 Apr 2024 Scientific Reports
Volume: 14, P: 8994
Modulation of peroxisomal import by the PEX13 SH3 domain and a proximal FxxxF binding motif

Import of proteins into peroxisomes depends on PEX5, PEX13 and PEX14. Here the authors obtain crystal structures and NMR data to show the recognition of diaromatic peptide motifs on a noncanonical surface of the PEX13 SH3 domain, revealing a dynamic network which modulates peroxisomal matrix import.
- Stefan Gaussmann
- Rebecca Peschel
- Michael Sattler
ResearchOpen Access18 Apr 2024 Nature Communications
Volume: 15, P: 3317
Cross-link assisted spatial proteomics to map sub-organelle proteomes and membrane protein topologies

The spatial mapping of proteins can give important functional insights. Here, Zhu et al. develop a cross-linking mass spectrometry-based spatial proteomics method that does not require protein engineering, affords sub-organelle resolution, and elucidates both protein locations and membrane topologies.
- Ying Zhu
- Kerem Can Akkaya
- Fan Liu
ResearchOpen Access17 Apr 2024 Nature Communications
Volume: 15, P: 3290
Promiscuous G-protein activation by the calcium-sensing receptor

Structures of the human calcium-sensing receptor can be bound into complex with G proteins from three different Gα subtypes while maintaining G-protein-binding specificity.
- Hao Zuo
- Jinseo Park
- Qing R. Fan
Research17 Apr 2024 Nature
P: 1-8
Mechanism and structural dynamics of sulfur transfer during de novo [2Fe-2S] cluster assembly on ISCU2

The biogenesis of iron-sulfur proteins in eukaryotes is initiated by the mitochondrial core ISC complex. Here, the authors provide structural, biochemical and spectroscopic data to characterize sulfur transfer intermediates in the core ISC complex.
- Vinzent Schulz
- Ralf Steinhilper
- Roland Lill
ResearchOpen Access16 Apr 2024 Nature Communications
Volume: 15, P: 3269

All Research & Reviews

News and Comment

Shifting our perspective on orphan G protein-coupled receptors

G protein-coupled receptors (GPCRs) with no known endogenous ligand are termed orphans. Deorphanization of a GPCR involves identifying the ligand, which can be a painstaking exercise. In this Comment, we discuss the challenges in the process, its role in drug discovery and alternative approaches to characterizing orphan GPCRs.
- Nicola J. Smith
- Fiona Murray
Comments & Opinion02 Apr 2024 Nature Structural & Molecular Biology
Volume: 31, P: 582-583
Graphene sandwich for cryo-EM
- Arunima Singh
Research Highlights12 Mar 2024 Nature Methods
Volume: 21, P: 371
The regulatory landscape of chromatin accessibility

A study in Nature Genetics identifies many regulators of genome-wide chromatin accessibility and then reports the mechanistic underpinnings for one of the identified transcription factors.
- Henry Ertl
Research Highlights11 Mar 2024 Nature Reviews Genetics
Volume: 25, P: 305
Mesoscale condensates organize the cytoplasm

Biomolecular condensates are recognized for their ability to compartmentalize the cytoplasm without bounding membranes, but the degree to which they organize the cytoplasm has not been clear. A new study reveals that condensates at a scale of 100 nm are responsible for the organization of at least 18% of the cytoplasmic proteome.
- Leshani Ahangama Liyanage
- Jonathon A. Ditlev
News & Views29 Feb 2024 Nature Cell Biology
Volume: 26, P: 310-312
Turning vaccine design on its head
- Katarzyna Ciazynska
News & Views16 Feb 2024 Nature Structural & Molecular Biology
Volume: 31, P: 215
Micropolarized to the core

Macromolecules can undergo liquid–liquid phase separation to form condensates that have critical roles in biological functions and dysfunctions. A new study demonstrates that differences in micropolarity between components is a prime determinant of the multiphasic architecture of biomolecular condensates.
- My Diem Quan
- Josephine C. Ferreon
- Allan Chris M. Ferreon
News & Views07 Feb 2024 Nature Chemical Biology
Volume: 20, P: 399-400