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Collaborative effort led by UMass Chan Medical School spotlights worms as model for personalized medicine

A team of researchers developed a model system to study individual differences in metabolism using C. elegans worms. They identified a novel metabolic condition linked to variation in the hphd-1 gene, which has implications for personalized medicine and tailoring dietary advice and disease treatment to an individual's genome sequence.

SourceUMass Chan Medical School·JournalNature·DateJul 11, 2022

Live wire: new research on nanoelectronics

A study by Arizona State University shows that certain proteins can act as efficient electrical conductors, outperforming DNA-based nanowires in conductance. The protein nanowires display better performance over long distances, enabling potential applications for medical sensing and diagnostics.

SourceArizona State University·JournalACS Nano·TypeExperimental study·DateFeb 24, 2022

Researchers from Tel Aviv University prove for the first time that silent mutations can predict the development of cancer cells

Silent mutations, which don't change protein sequences, hold diagnostic value in predicting cancer types and patient survival. The study analyzed over 10,000 cancer genomes and found that combining information from silent and non-silent mutations improved classification and prognostication up to 17% and 5%, respectively.

SourceTel-Aviv University·Journalnpj Genomic Medicine·DateAug 31, 2021

Coronavirus structure clue to high infection rate

Researchers at Cornell University have discovered a unique feature in the virus that causes COVID-19, which could explain its high transmissibility. The study identified a structural loop in the spike protein and a specific sequence of amino acids that are different from other human coronaviruses.

SourceCornell University·JournalJournal of Molecular Biology·DateMay 5, 2020

Differentiating amino acids

Researchers from the University of Freiburg and US universities have developed a method to differentiate between individual amino acids in short peptides. They used an aerolysin nanopore to measure the ion current through the pore, enabling the sensitive measurement of peptide size and structure.

SourceUniversity of Freiburg·JournalNature Biotechnology·DateDec 17, 2019

X marks the spot: recombination in structurally distinct chromosomes

Researchers discovered that different mechanisms govern chromosome interaction with the synaptonemal complex, particularly for sex chromosomes like X. The findings highlight the importance of structural features over primary amino acid sequences and suggest a chromosome-specific aspect to human meiotic defects.

SourceStowers Institute for Medical Research·JournalProceedings of the National Academy of Sciences·DateOct 16, 2019

From function to form

Researchers at Harvard Medical School have developed a new method for determining 3D protein structures from lab-designed DNA sequences. By assessing the effects of genetic mutations on protein functions, they were able to identify functional interactions within DNA sequences and construct 3D structures that closely mimicked those deri...

SourceHarvard Medical School·JournalNature Genetics·DateJun 17, 2019

Using machine learning to design peptides

A new algorithm that combines experimental data with machine learning reduces the time needed to find optimal peptide sequences, allowing for faster discovery and synthesis. This method has the potential to revolutionize how peptides are designed and could lead to breakthroughs in materials science, chemistry, and medicine.

SourceNorthwestern University·JournalNature Communications·DateDec 10, 2018

Computational approaches reveal new insights into molecular protein function

Recent studies published in PLOS Computational Biology have introduced novel computational methods to explore the molecular function of proteins. These approaches aim to simplify the challenge of determining functions for an ever-increasing amount of known proteins by identifying shared functional sites and predicting their activity.

SourcePLOS·JournalPLOS Computational Biology·DateApr 5, 2018

Modified biomaterials self-assemble on temperature cues

Biomaterials with precisely ordered structures could be used for various biomedical applications due to their precise control of self-assembly. The hybrid approach allows researchers to expand the chemical diversity of protein-based materials by combining different alphabets, such as amino acids and lipids.

SourceDuke University·JournalNature Chemistry·DateMar 19, 2018

Breakthrough for peptide medication

Researchers at Technical University of Munich have developed a strategy for designing peptides that can be administered orally, overcoming the major challenge of stability and absorption. This breakthrough simplifies the creation of peptide medications, potentially offering new treatments for various diseases.

SourceTechnical University of Munich (TUM)·JournalAngewandte Chemie International Edition·DateFeb 21, 2018

Protein intentionally terminates own synthesis by destabilizing synthesis machinery -- the ribosome

Researchers found that proteins with specific sequences can trigger the degradation of their own synthetic ribosomes, leading to aborted translation. However, living organisms also possess a mechanism to counteract this phenomenon, allowing for precise regulation of protein expression in response to environmental changes.

SourceTokyo Institute of Technology·JournalMolecular Cell·DateNov 20, 2017

Sizzling snails prioritize protein stability

The study reveals that Echinolittorina snails have a unique enzyme structure that enables them to maintain protein stability at high temperatures, allowing them to thrive in hot environments. The researchers found that subtle differences in amino acid sequences between the snail proteins enabled them to remain functional and stable at ...

SourceThe Company of Biologists·JournalJournal of Experimental Biology·DateMay 31, 2017

Amino acid sequences are key to the properties of silks

A new study from RIKEN Center for Sustainable Resource Science reveals that amino acid sequences are key determinants of silk fiber material properties. The research sheds light on the unique properties of silkworm silks, including their mechanical and thermal behavior.

SourceRIKEN·JournalScientific Reports·DateJun 9, 2016

The genetic evolution of Zika virus

A recent study analyzing 40 Zika virus strains identifies significant changes in amino acid and nucleotide sequences, diverging between Asian and African lineages. The data suggests the strains evolved from a common ancestor, with human isolates more closely related to the French Polynesia/2013 strain.

SourceCell Press·JournalCell Host & Microbe·DateApr 15, 2016

Evolution meets biochemistry to better understand how dopamine receptors work

Baylor College of Medicine researchers have developed a new mathematical tool that combines biochemistry and computational analysis to identify specific structural changes in the dopamine 2 receptor, which helps maintain its structure and function throughout an evolutionary time scale. This discovery opens the possibility for better dr...

SourceBaylor College of Medicine·JournalProceedings of the National Academy of Sciences·DateMar 16, 2016

Protein evolution follows a modular principle

Scientists at the Max Planck Institute for Developmental Biology discovered that proteins can be constructed of similar amino acid chains even when their three-dimensional shapes differ significantly. This suggests that modern proteins arose from common precursors, built up from smaller fragments according to a modular principle.

SourceMax-Planck-Gesellschaft·JournalNature Chemical Biology·DateJul 23, 2014

First widespread look at evolution of venomous centipedes

A research team analyzed centipede venom protein and peptide sequences to catalog, categorize, and reconstruct their evolutionary histories. They identified 60 unique venom protein and peptide families from just five species investigated, including 11 new protein families showcasing novel centipede venom ways.

Amino acid fingerprints revealed in new study

Researchers at Arizona State University have developed a technique to identify amino acids, including subtly modified variants, by analyzing electrical activity signals. This breakthrough advances the prospect of clinical protein sequencing and discovery of new biomarkers for diseases such as cancer and Alzheimer's.

SourceArizona State University·JournalNature Nanotechnology·DateApr 6, 2014