{"id":15357,"date":"2026-05-10T10:49:13","date_gmt":"2026-05-10T10:49:13","guid":{"rendered":"https:\/\/globalnewstoday.uk\/index.php\/2026\/05\/10\/weill-cornell-team-discovers-previously-unknown-biological-cold-sensor-fingerlakes1-com\/"},"modified":"2026-05-10T10:49:13","modified_gmt":"2026-05-10T10:49:13","slug":"weill-cornell-team-discovers-previously-unknown-biological-cold-sensor-fingerlakes1-com","status":"publish","type":"post","link":"https:\/\/globalnewstoday.uk\/index.php\/2026\/05\/10\/weill-cornell-team-discovers-previously-unknown-biological-cold-sensor-fingerlakes1-com\/","title":{"rendered":"Weill Cornell team discovers previously unknown biological cold sensor – Fingerlakes1.com"},"content":{"rendered":"

Researchers at Weill Cornell Medicine have identified a previously unknown mechanism that allows cells to sense cold temperatures, a discovery that could eventually help scientists better understand temperature regulation disorders in humans.
The study, published April 10 in Nature Communications, focused on a bacterial protein that becomes more active in colder temperatures through an unusual interaction between the protein itself and the fatty molecules surrounding it.
Scientists say the findings could point toward similar temperature-sensing systems in more complex organisms, including humans.
The research centered on a protein known as SthK, found in a species of heat-loving bacteria called Spirochaeta thermophila. The bacteria typically thrive in extremely hot environments, including geothermal waters approaching 150 degrees Fahrenheit.
SthK is part of a class of proteins known as ion channels, which regulate the movement of charged particles through cell membranes and often play critical roles in sensory functions throughout living organisms.
Researchers at Weill Cornell Medicine discovered the channel becomes more active at temperatures below 68 degrees Fahrenheit because of a previously undocumented molecular process involving both the protein and surrounding membrane lipids.
The team found that the mechanism depends on what\u2019s known as a \u201csalt bridge\u201d \u2014 a bond between oppositely charged amino acids within the protein structure.
At warmer temperatures, the salt bridge remains stronger and keeps the channel closed more often. But as temperatures cool, the bond weakens, allowing the channel to open more frequently and respond to colder conditions.
Researchers also found the surrounding lipids play a critical role in fine-tuning that process.
According to the study, certain lipids containing amine groups help maintain the salt bridge in what researchers described as a \u201cGoldilocks\u201d state \u2014 weak enough to respond to cold temperatures but stable enough to avoid constant activation.
Senior author Crina Nimigean, a professor of biochemistry and biophysics in anesthesiology at Weill Cornell Medicine, said the findings suggest temperature sensitivity may emerge from cooperative interactions between proteins and the membranes surrounding them.
Researchers believe similar sensing systems could exist in other organisms and proteins but may have gone undetected until now.
The work relied on high-resolution electron microscopy and laboratory experiments comparing how the protein functioned under different temperatures and structural conditions.
Scientists said the discovery may ultimately contribute to research into disorders involving abnormal temperature regulation, while also broadening understanding of how organisms adapt to changing environments at the cellular level.
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Researchers at Weill Cornell Medicine have identified a previously unknown mechanism that allows cells to sense cold temperatures, a discovery that could eventually help scientists better understand temperature regulation disorders in humans.The study, published April 10 in Nature Communications, focused on a bacterial protein that becomes more active in colder temperatures through an unusual interaction […]<\/p>\n","protected":false},"author":1,"featured_media":15358,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[9],"tags":[],"class_list":{"0":"post-15357","1":"post","2":"type-post","3":"status-publish","4":"format-standard","5":"has-post-thumbnail","7":"category-science"},"_links":{"self":[{"href":"https:\/\/globalnewstoday.uk\/index.php\/wp-json\/wp\/v2\/posts\/15357","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/globalnewstoday.uk\/index.php\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/globalnewstoday.uk\/index.php\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/globalnewstoday.uk\/index.php\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/globalnewstoday.uk\/index.php\/wp-json\/wp\/v2\/comments?post=15357"}],"version-history":[{"count":0,"href":"https:\/\/globalnewstoday.uk\/index.php\/wp-json\/wp\/v2\/posts\/15357\/revisions"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/globalnewstoday.uk\/index.php\/wp-json\/wp\/v2\/media\/15358"}],"wp:attachment":[{"href":"https:\/\/globalnewstoday.uk\/index.php\/wp-json\/wp\/v2\/media?parent=15357"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/globalnewstoday.uk\/index.php\/wp-json\/wp\/v2\/categories?post=15357"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/globalnewstoday.uk\/index.php\/wp-json\/wp\/v2\/tags?post=15357"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}