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Saitama University researchers discover that a natural peptide aptamer switches between two target proteins depending on metal ions

A team of researchers from Saitama University has discovered a natural peptide aptamer called Calmodulin-binding peptide (CBP) that can selectively recognize two structurally distinct proteins, calmodulin and human midkine. CBP binds to calmodulin in the presence of calcium ions and to human midkine in the presence of sodium ions.

SourceSaitama University·JournalBiochemical and Biophysical Research Communications·TypeExperimental study·DateJul 15, 2026

More polar ocean turbulence due to planetary warming

New research suggests that ocean turbulence and horizontal stirring will dramatically increase in the Arctic and Southern Oceans due to human-induced Global Warming. The study uses ultra-high-resolution simulations to investigate how mesoscale horizontal stirring (MHS) responds to warming, revealing a pronounced future intensification ...

SourceInstitute for Basic Science·JournalNature Climate Change·TypeComputational simulation/modeling·DateNov 5, 2025
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Folded peptides are more electrically conductive than unfolded peptides

Researchers found that folded peptides are more electrically conductive than their unfolded counterparts due to the formation of a specific secondary structure called the 3_10 helix. This discovery has implications for the design and development of molecular electronic devices.

SourceBeckman Institute for Advanced Science and Technology·JournalProceedings of the National Academy of Sciences·DateJul 25, 2024

A new antibody capture method reveals G-quadruplex landscape and its regulation

Researchers developed an improved method for G4 landscape determination, revealing that sequence property-specific constraints in the nuclear environment mitigate G4 formation. The technique, AbC G4-ChIP, captures G4s efficiently without bias, showing that depletion of a repeat-binding protein enhances net G4 capture at specific sites.

SourceImpact Journals LLC·JournalOncotarget·TypeObservational study·DateMar 18, 2024

New software brings lower-resolution cryo-EM maps into focus

Researchers at Purdue University have developed a new software called Emap2sec that can identify secondary structures in proteins from lower-resolution cryo-EM maps. This technique has the potential to speed up protein structure analysis and improve accuracy, enabling researchers to develop more effective drugs for various diseases.

SourcePurdue University·JournalNature Methods·DateJul 29, 2019
Apple AirPods Pro (2nd Generation, USB-C)

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Infrared sheds light on single protein complexes

A new infrared spectroscopy technique called nano-FTIR has enabled researchers to map the secondary structure of proteins on the nanometer scale. The technique, which combines scanning near-field optical microscopy and FTIR spectroscopy, allows for nanoscale-resolved protein spectroscopy and identification of single protein complexes w...

SourceElhuyar Fundazioa·JournalNature Communications·DateDec 17, 2013

Backing out of the nanotunnel

Researchers have developed a new method for analyzing the spatial conformations of biomolecules like proteins and DNA, minimizing interactions with pore materials. The approach enables the prediction of translocation dynamics of nucleic acids with varying sequences.

SourceLudwig-Maximilians-Universität München·JournalBiophysical Journal·DateJan 10, 2012

Genetic mechanism helps explain chronic pain disorders

A study at UNC Chapel Hill found that specific genetic variants of the COMT gene can affect pain processing by altering messenger RNA secondary structure. The discovery may lead to more effective treatments for TMJD and other chronic pain conditions.

SourceUniversity of North Carolina at Chapel Hill·JournalScience·DateDec 22, 2006
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