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Energy supply channels

Scientists at the University of Freiburg have elucidated the mechanism of protein insertion into the mitochondrial outer membrane. The discovery sheds light on the formation and function of mitochondria, which play a crucial role in cellular energy production.

SourceUniversity of Freiburg·JournalScience·DateJan 25, 2018

Proteins' fluorescence a little less mysterious

Rice University researchers confirmed their theory on the mechanism behind a fluorescent biosensor that monitors neurons by sensing changes in voltage. They developed a method to test fluorescent biosensors using computer simulations, resolving a decade-long debate between scientists.

SourceRice University·JournalJournal of the American Chemical Society·DateJan 25, 2018

How a biophysical simulation method might accelerate drug target discovery

Researchers developed a computational simulation method to predict protein sequence changes for efficient membrane insertion, correlating improved insertion efficiency with increased protein yield. The new approach offers a way forward for membrane protein researchers struggling to express their proteins.

SourceAmerican Society for Biochemistry and Molecular Biology·JournalJournal of Biological Chemistry·DateNov 29, 2017

The importance of asymmetry in bacteria

A team of researchers from Newcastle University discovered the MlaA protein, which removes lipids from the outer membrane to increase permeability for toxic compounds. This process could be exploited by drugs to decrease bacterial virulence and enhance antibiotic effectiveness.

SourceNewcastle University·JournalNature Microbiology·DateOct 16, 2017

Closing the gate to mitochondria

Researchers create 'ImportOmics' method to identify proteins imported into mitochondria, uncovering new insights into cell function and potential disease causes. The study reveals over 1,120 mitochondrial proteins, including previously unknown associations.

SourceUniversity of Freiburg·JournalNature Communications·DateMay 9, 2017

On the trail of Parkinson's disease

A team of chemists from Konstanz University has made a significant discovery about the effects of selective mutations on the alpha-synuclein protein. By applying magnetic probes to the protein, they found that these changes disturb the binding of alpha-synuclein to membranes.

SourceUniversity of Konstanz·JournalJournal of the American Chemical Society·DateMar 24, 2017

Cellular 'garbage disposal' has another job

Researchers discovered proteasomes embedded in nerve cell membranes, degrading proteins and expelling peptides that carry essential signals. This finding suggests a new role for proteasomes in cell-to-cell communications and raises questions about neurological disease.

SourceJohns Hopkins Medicine·JournalNature Structural & Molecular Biology·DateMar 13, 2017

Biophysicists propose new approach for membrane protein crystallization

Researchers from MIPT and their international collaborators have developed a novel method to crystallize membrane proteins using synthetic patches called nanodiscs. This approach enables the transfer of membrane proteins into lipidic cubic phase for crystal growth, preserving their functional state and enabling high-resolution X-ray di...

SourceMoscow Institute of Physics and Technology·JournalCrystal Growth & Design·DateMar 6, 2017

New findings detail structure of immature Zika virus

The study reveals differences in protein arrangement between immature Zika and other flaviviruses, shedding light on the virus's role in infection and disease. Understanding the structure of the immature form could help develop effective antiviral treatments and vaccines for diseases like microcephaly.

SourcePurdue University·JournalNature Structural & Molecular Biology·DateJan 9, 2017

From rigid to flexible

Researchers have found a mechanism that explains how cells transport cargo efficiently and selectively within their boundaries. The discovery reveals that flexibility in large tether proteins plays a crucial role in initiating the fusion process.

New technology selects high-affinity proteins

Researchers at Kobe University and AIST in Japan developed a technology to select high-affinity proteins that bind with membrane proteins, a key feature in controlling physiological functions. This discovery has potential applications in the development of new biopharmaceuticals for various drug targets, including cancer treatment.

SourceKobe University·JournalScientific Reports·DateDec 1, 2015

Unraveling iridescence

Researchers at UC Santa Barbara have clarified the mechanism of iridescence in squid skin, revealing that specific sequences of reflectins correlate with color output. The study identifies three major types of reflectins and their roles in static and tunable iridocytes.

SourceUniversity of California - Santa Barbara·JournalJournal of Biological Chemistry·DateJul 1, 2015

The pertussis pathogen -- New findings

Researchers discovered that the protein structure of a key membrane protein differs from a previously postulated model, providing a basis for new treatments. The study reveals how the protein pore opens and closes in response to substrate binding, offering insights into the pathogen's attachment mechanism.

SourceUniversity of Basel·JournalNature Communications·DateJun 23, 2015

Rafts on the cell membrane

Researchers used advanced techniques to study single molecules and protein interactions on the cell membrane. The findings revealed that lipid rafts, previously thought to move within the membrane, do not exist. Instead, proteins may be anchored at specific positions on the surface, influencing cellular processes.

SourceVienna University of Technology·JournalNature Communications·DateApr 21, 2015

Artificial membranes on silicon

Researchers have developed a new technology to create artificial membranes on silicon surfaces, mimicking those found in living organisms. The process uses commercial chemicals and is the first time anyone has made an artificial membrane without mixing liquid solvents together.

SourceAmerican Institute of Physics·JournalThe Journal of Chemical Physics·DateSep 9, 2014

Molecular biology mystery unravelled

Researchers at the University of Bristol and EMBL have identified the 'holo-translocon' as the machinery responsible for inserting proteins into cell membranes. This breakthrough could lead to the design of new anti-bacterial drugs and applications in synthetic biology.

SourceUniversity of Bristol·JournalProceedings of the National Academy of Sciences·DateFeb 18, 2014

Discovery aids in fight against antifungal drug resistance

Researchers have determined the complex structure of a key cell membrane protein involved in sterol metabolism and resistance in a yeast model. The study's findings provide new insights into mechanisms underlying fungal resistance to triazole drugs, which can help develop new broad-spectrum drugs with minimal side effects.

SourceUniversity of Otago·JournalProceedings of the National Academy of Sciences·DateFeb 3, 2014

Tricky protein may help HIV vaccine development

Researchers at Duke University have determined the structure of a key part of the HIV envelope protein, gp41 membrane proximal external region (MPER), which previously eluded detailed structural description. This discovery will help focus HIV vaccine development efforts.

SourceDuke University·JournalProceedings of the National Academy of Sciences·DateJan 13, 2014

Nanopore opens new cellular doorway for drug transport

Engineers have created a biological nanopore that acts as a selective door for DNA molecules to enter cells, potentially revolutionizing gene therapy and targeted drug delivery. The nanopore can be controlled to allow specific genetic information in specific cells, opening new possibilities for precision medicine.

SourceKU Leuven·JournalNature Communications·DateOct 23, 2013

UCSB research group develops a new tool for studying membrane protein structure

A new tool has been developed to resolve the structure of membrane-embedded and membrane-associating proteins by exploiting the unique water dynamics gradient across and above the lipid bilayer. This breakthrough can help determine the location and structure of protein segments at the surface of membranes.

SourceUniversity of California - Santa Barbara·JournalProceedings of the National Academy of Sciences·DateSep 30, 2013