{"689875":{"#nid":"689875","#data":{"type":"news","title":"The Hidden Language of Life\u2019s Early Proteins","body":[{"value":"\u003Cp dir=\u0022ltr\u0022\u003EHow did the earliest life on Earth build complex biological machinery with so few tools? A new study explores how the simplest building blocks of proteins \u2014 once limited to just half of today\u2019s amino acids \u2014 could still form the sophisticated structures life depends on.\u003C\/p\u003E\u003Cp dir=\u0022ltr\u0022\u003EThe paper,\u0026nbsp;\u003Ca href=\u0022https:\/\/www.sciencedirect.com\/science\/article\/pii\/S258959742600047X\u0022\u003E\u003Cem\u003EThe Borderlands of Foldability: Lessons from Simplified Proteins\u003C\/em\u003E\u003C\/a\u003E, is a meta-analysis of six decades of protein research and reveals that ancient proteins may have been far more complicated and dynamic than previously thought.\u0026nbsp;\u003C\/p\u003E\u003Cp dir=\u0022ltr\u0022\u003ERecently published in the journal\u0026nbsp;\u003Cem\u003ETrends in Chemistry\u003C\/em\u003E, the study includes Georgia Tech researchers\u0026nbsp;\u003Ca href=\u0022https:\/\/chemistry.gatech.edu\/people\/lynn-kamerlin\u0022\u003E\u003Cstrong\u003ELynn Kamerlin\u003C\/strong\u003E\u003C\/a\u003E, professor in the\u0026nbsp;\u003Ca href=\u0022http:\/\/chemistry.gatech.edu\u0022\u003ESchool of Chemistry and Biochemistry\u003C\/a\u003E and Georgia Research Alliance Vasser-Woolley Chair in Molecular Design, and\u0026nbsp;\u003Ca href=\u0022https:\/\/www.gatech.edu\/academics\/degrees\/phd\/quantitative-biosciences-phd\u0022\u003EQuantitative Biosciences\u003C\/a\u003E Ph.D. candidate\u0026nbsp;\u003Ca href=\u0022https:\/\/qbios.gatech.edu\/user\/231\u0022\u003E\u003Cstrong\u003EAlfie-Louise Brownless\u003C\/strong\u003E\u003C\/a\u003E.\u003C\/p\u003E\u003Cp dir=\u0022ltr\u0022\u003ECo-authors also include\u003Cstrong\u003E\u0026nbsp;\u003C\/strong\u003E\u003Ca href=\u0022https:\/\/www.isct.ac.jp\/en\u0022\u003EInstitute of Science Tokyo\u003C\/a\u003E graduate student\u0026nbsp;\u003Cstrong\u003EKoh Seya\u0026nbsp;\u003C\/strong\u003Eand\u0026nbsp;\u003Ca href=\u0022https:\/\/liamlongo.org\/\u0022\u003E\u003Cstrong\u003ELiam M. Longo\u003C\/strong\u003E\u003C\/a\u003E, who serves as a specially appointed associate professor at Science Tokyo and as an affiliate research scientist at the\u0026nbsp;\u003Ca href=\u0022https:\/\/bmsis.org\/\u0022\u003EBlue Marble Space Institute of Science\u003C\/a\u003E.\u003C\/p\u003E\u003Cp dir=\u0022ltr\u0022\u003EThe research has implications ranging from the origins of life and the search for life in the universe to cutting-edge medical innovation. \u201cOne of the biggest unanswered questions in science is how life first began,\u201d says Kamerlin, who is a corresponding author of the study. \u201cUnderstanding how the first protein-like molecules formed and what the earliest proteins may have been like is a key part of that puzzle.\u201d\u003C\/p\u003E\u003Cp dir=\u0022ltr\u0022\u003E\u201cProteins power our bodies \u2014 and all life on Earth,\u201d she adds. \u201cSimply put, the evolution of proteins is the reason that we\u2019re able to have this conversation at all.\u201d\u003C\/p\u003E\u003Ch3 dir=\u0022ltr\u0022\u003E\u003Cstrong\u003EA Protein Folding Paradox\u003C\/strong\u003E\u003C\/h3\u003E\u003Cp dir=\u0022ltr\u0022\u003EIf proteins are the scaffolding of life, amino acids are the components that make up that scaffolding. \u201cToday, an average protein is constructed from a chain of about 300 amino acids, involving 20 different types of amino acids,\u201d Kamerlin shares. Proteins fold when these chains twist into a specific 3-dimensional shape, creating structures critical for biology.\u003C\/p\u003E\u003Cp dir=\u0022ltr\u0022\u003EHowever, while these folds are essential, exactly\u0026nbsp;\u003Cem\u003Ehow\u003C\/em\u003E a protein knows which way to fold remains a mystery. \u201cWe know that proteins didn\u2019t just fold randomly,\u201d Kamerlin shares, \u201cbecause randomly trying all possible configurations would take a protein longer than the age of the universe.\u201d\u003C\/p\u003E\u003Cp dir=\u0022ltr\u0022\u003EIt\u2019s a cornerstone problem in biological science called \u201cLevinthal\u2019s Paradox,\u201d and highlights a fundamental mystery: Proteins fold incredibly quickly into very specific combinations \u2014 but like a sheet of paper spontaneously folding into an origami swan, researchers don\u2019t know how proteins \u201cchoose\u201d the folds they make.\u003C\/p\u003E\u003Cp dir=\u0022ltr\u0022\u003E\u201cWe can predict what a protein will look like, but can\u2019t tell you how it got there,\u201d Kamerlin adds. \u201cThat\u2019s what we\u2019re interested in exploring: how small early proteins developed into the complex proteins that support every living thing on today\u2019s Earth.\u201d\u003C\/p\u003E\u003Ch3 dir=\u0022ltr\u0022\u003E\u003Cstrong\u003ESimple Letters, Sophisticated Structures\u003C\/strong\u003E\u003C\/h3\u003E\u003Cp dir=\u0022ltr\u0022\u003EEarly proteins likely had access to just half of today\u2019s amino acids. \u201cAbout 10-12 amino acids were likely available on early Earth,\u201d Kamerlin says. Like writing a story with just the letters \u201cA\u201d through \u201cL,\u201d researchers assumed that the \u2018vocabulary\u2019 proteins could build from such a limited amino acid alphabet would also be constrained.\u003C\/p\u003E\u003Cp dir=\u0022ltr\u0022\u003E\u201cThere is a language to protein folding,\u201d Kamerlin explains. \u201cThat language is hidden in their structures. Our research is in trying to understand the rules \u2014 the grammar and vocabulary that dictate a protein fold.\u201d\u0026nbsp;\u003C\/p\u003E\u003Cp dir=\u0022ltr\u0022\u003EThe grammar they discovered was surprising: with a combination of creative techniques and environmental support, complex structures can arise from limited amino acid alphabets.\u0026nbsp;\u003C\/p\u003E\u003Cp dir=\u0022ltr\u0022\u003E\u201cWe found that it is possible to develop complex folds with very simple tools \u2014 and certain environments, like salty ones, can help support that,\u201d Kamerlin shares. \u201cEarly proteins could also cross-link and associate, interacting like LEGO blocks to create more complex structures.\u201d\u003C\/p\u003E\u003Ch3 dir=\u0022ltr\u0022\u003E\u003Cstrong\u003EPioneering Proteins\u003C\/strong\u003E\u003C\/h3\u003E\u003Cp dir=\u0022ltr\u0022\u003ENow, the team is conducting research in environments that could mimic conditions on early Earth \u2014 aiming to discover more about how these regions could have given rise to today\u2019s complex proteins. \u201cThis aspect of our research also ties into the amazing\u0026nbsp;\u003Ca href=\u0022https:\/\/cos.gatech.edu\/news\/2026-frontiers-science-advancing-space-exploration-0\u0022\u003Espace research\u003C\/a\u003E happening at Georgia Tech,\u201d Kamerlin says. \u201cWhile we\u2019re interested in understanding early life on Earth, our work could help inform where best to look for evidence of life beyond our planet.\u201d\u003C\/p\u003E\u003Cp dir=\u0022ltr\u0022\u003EKamerlin specializes in creating computer models that simulate possible scenarios \u2013 creating an opportunity to quickly and efficiently test many theories. The most compelling of these can then be tested by her collaborator and co-author at Science Tokyo, Liam Longo, in lab experiments.\u0026nbsp;\u003C\/p\u003E\u003Cp dir=\u0022ltr\u0022\u003EProtein folding is also at the forefront of medical innovation, ranging from diagnostic tools to cancer treatments and neurodegenerative diseases. \u201cIn the broader scope, we\u2019re interested in discovering what we can design, what we can stress test, and what we can reconstruct with AI and other computational tools,\u201d Kamerlin says. \u201cBecause if you can understand how proteins fold, you gain the ability to design them.\u201d\u003C\/p\u003E\u003Cp\u003E\u0026nbsp;\u003C\/p\u003E\u003Cp dir=\u0022ltr\u0022\u003E\u003Cem\u003EFunding: NASA, the Human Frontier Science Program, and the Knut and Alice Wallenberg Foundation\u003C\/em\u003E\u003C\/p\u003E\u003Cp dir=\u0022ltr\u0022\u003E\u003Cem\u003EDOI: \u003C\/em\u003E\u003Ca href=\u0022https:\/\/doi.org\/10.1016\/j.trechm.2026.03.001\u0022 rel=\u0022noreferrer noopener\u0022 target=\u0022_blank\u0022 title=\u0022Persistent link using digital object identifier\u0022\u003E\u003Cem\u003Ehttps:\/\/doi.org\/10.1016\/j.trechm.2026.03.001\u003C\/em\u003E\u003C\/a\u003E\u003C\/p\u003E","summary":"","format":"limited_html"}],"field_subtitle":"","field_summary":[{"value":"\u003Cp\u003EHow did the earliest life on Earth build complex biological machinery with so few tools? A new study explores how the simplest building blocks of proteins formed the sophisticated structures life depends on.\u003C\/p\u003E","format":"limited_html"}],"field_summary_sentence":[{"value":"Life\u2019s first alphabet was likely small \u2014 but surprisingly powerful."}],"uid":"35599","created_gmt":"2026-04-20 16:06:30","changed_gmt":"2026-04-22 15:01:58","author":"sperrin6","boilerplate_text":"","field_publication":"","field_article_url":"","location":"Atlanta, GA","dateline":{"date":"2026-04-20T00:00:00-04:00","iso_date":"2026-04-20T00:00:00-04:00","tz":"America\/New_York"},"extras":[],"hg_media":{"677019":{"id":"677019","type":"image","title":"Lynn Kamerlin","body":null,"created":"1746193435","gmt_created":"2025-05-02 13:43:55","changed":"1746193435","gmt_changed":"2025-05-02 13:43:55","alt":"Lynn Kamerlin headshot","file":{"fid":"260878","name":"lynn-kamerlin_portrait.jpg","image_path":"\/sites\/default\/files\/2025\/05\/02\/lynn-kamerlin_portrait.jpg","image_full_path":"http:\/\/hg.gatech.edu\/\/sites\/default\/files\/2025\/05\/02\/lynn-kamerlin_portrait.jpg","mime":"image\/jpeg","size":104455,"path_740":"http:\/\/hg.gatech.edu\/sites\/default\/files\/styles\/740xx_scale\/public\/2025\/05\/02\/lynn-kamerlin_portrait.jpg?itok=UCfaKKYb"}},"680000":{"id":"680000","type":"image","title":"Amino acid diversity in peptides and proteins over time. Now, in the era of biotechnology, the amino acid alphabet is poised to expand again. (Figure Credit: \u201cThe borderlands of foldability: lessons from simplified proteins,\u201d Trends in Chemistry, 2026)","body":"\u003Cp\u003EAmino acid diversity in peptides and proteins over time. Over time, the genetic code expanded into the 20-amino acid alphabet found in contemporary biology. Now, in the era of biotechnology, the amino acid alphabet is poised to expand once more. (Figure Credit: \u201cThe borderlands of foldability: lessons from simplified proteins,\u201d Koh Seya, Alfie\u2011Louise R. Brownless, Shina C. L. Kamerlin, and Liam M. Longo, \u003Cem\u003ETrends in Chemistry, \u003C\/em\u003E2026)\u003C\/p\u003E","created":"1776701693","gmt_created":"2026-04-20 16:14:53","changed":"1776701693","gmt_changed":"2026-04-20 16:14:53","alt":"A diagram showing the history of peptides and proteins over time. It is shaped like an hourglass.","file":{"fid":"264232","name":"Fig1Kamerlin.jpg","image_path":"\/sites\/default\/files\/2026\/04\/20\/Fig1Kamerlin.jpg","image_full_path":"http:\/\/hg.gatech.edu\/\/sites\/default\/files\/2026\/04\/20\/Fig1Kamerlin.jpg","mime":"image\/jpeg","size":591690,"path_740":"http:\/\/hg.gatech.edu\/sites\/default\/files\/styles\/740xx_scale\/public\/2026\/04\/20\/Fig1Kamerlin.jpg?itok=l_Fxw_Fs"}}},"media_ids":["677019","680000"],"groups":[{"id":"1278","name":"College of Sciences"},{"id":"1188","name":"Research Horizons"},{"id":"85951","name":"School of Chemistry and Biochemistry"}],"categories":[{"id":"194606","name":"Artificial Intelligence"},{"id":"141","name":"Chemistry and Chemical Engineering"},{"id":"146","name":"Life Sciences and Biology"},{"id":"135","name":"Research"}],"keywords":[{"id":"192250","name":"cos-microbial"},{"id":"187915","name":"go-researchnews"},{"id":"192863","name":"go-ai"}],"core_research_areas":[{"id":"193655","name":"Artificial Intelligence at Georgia Tech"},{"id":"39441","name":"Bioengineering and Bioscience"},{"id":"193653","name":"Georgia Tech Research Institute"}],"news_room_topics":[],"event_categories":[],"invited_audience":[],"affiliations":[],"classification":[],"areas_of_expertise":[],"news_and_recent_appearances":[],"phone":[],"contact":[{"value":"\u003Cp\u003EWritten by:\u003C\/p\u003E\u003Cp\u003E\u003Ca href=\u0022mailto:sperrin6@gatech.edu\u0022\u003E\u003Cstrong\u003ESelena Langner\u003C\/strong\u003E\u003C\/a\u003E\u003Cbr\u003ECollege of Sciences\u003Cbr\u003EGeorgia Institute of Technology\u003C\/p\u003E","format":"limited_html"}],"email":[],"slides":[],"orientation":[],"userdata":""}}}