Cube Biotech

𝗠𝗲𝗺𝗯𝗿𝗮𝗻𝗲 𝗽𝗿𝗼𝘁𝗲𝗶𝗻 𝘀𝗼𝗹𝘂𝗯𝗶𝗹𝗶𝘇𝗮𝘁𝗶𝗼𝗻 𝗳𝗼𝗿 𝗖𝗿𝘆𝗼-𝗘𝗠: 𝗧𝗿𝗲𝗻𝗱𝘀 𝗔𝗿𝗲 𝗖𝗵𝗮𝗻𝗴𝗶𝗻𝗴!   The recent study by Le Bon et al. on surfactant use in cryo-EM paints a fascinating picture of how membrane protein research is evolving. One standout finding: 𝟭𝟬% 𝗼𝗳 𝘀𝗼𝗹𝘂𝗯𝗶𝗹𝗶𝘇𝗮𝘁𝗶𝗼𝗻 𝗮𝗴𝗲𝗻𝘁𝘀 𝘂𝘀𝗲𝗱 𝗳𝗼𝗿 𝘃𝗶𝘁𝗿𝗶𝗳𝗶𝗰𝗮𝘁𝗶𝗼𝗻 𝗮𝗿𝗲 𝗶𝗻 𝟮𝟬𝟮𝟬 𝗮𝗺𝗽𝗵𝗶𝗽𝗮𝘁𝗵𝗶𝗰 𝗽𝗼𝗹𝘆𝗺𝗲𝗿𝘀. This shift signals a growing demand for maintaining proteins in environments that mimic their native state.   It’s striking to see that by 2020, MSP-based nanodiscs were used more frequently than traditional detergents like digitonin or maltosides in cryo-EM studies. To me, this underscores how scientists are prioritizing near-native conditions. While MSP nanodiscs offer an artificial lipid environment, copolymers present a more authentic native lipid setting.   Historically, the first high-resolution structures came from abundant and detergent-resistant bacterial membrane proteins (MPs). Now, we’re tackling more fragile, low-abundance eukaryotic MPs—opening new avenues for disease research and drug discovery.   While challenges remain—like managing copolymer charge—progress is clear. The potential for high-quality eukaryotic MP structures could redefine therapeutic strategies.   𝗪𝗵𝗶𝗰𝗵 𝘀𝗼𝗹𝘂𝗯𝗹𝗶𝘇𝗮𝘁𝗶𝗼𝗻 𝗮𝗴𝗲𝗻𝘁𝘀 𝗮𝗿𝗲 𝘆𝗼𝘂 𝘂𝘀𝗶𝗻𝗴 𝗶𝗻 𝗰𝗿𝘆𝗼-𝗘𝗠? 𝗛𝗮𝘃𝗲 𝘆𝗼𝘂 𝘁𝗿𝗶𝗲𝗱 𝗰𝗼𝗽𝗼𝗹𝘆𝗺𝗲𝗿𝘀 𝘆𝗲𝘁? If you’re keen to work in a truly native environment, feel free to DM me! Let’s push the boundaries together.

𝗨𝗻𝗹𝗼𝗰𝗸𝗶𝗻𝗴 𝗠𝗲𝗺𝗯𝗿𝗮𝗻𝗲 𝗣𝗿𝗼𝘁𝗲𝗶𝗻𝘀 𝘄𝗶𝘁𝗵 𝘁𝗵𝗲 𝗡𝗮𝘁𝗶𝘃𝗲𝗠𝗣™ 𝗧𝗮𝗿𝗴𝗲𝘁𝘀 Working with complex membrane proteins, like GPCRs and ion channels, is a major challenge in drug discovery. These targets are vital for many biological processes yet notoriously difficult to handle, especially when 𝗹𝗶𝗽𝗶𝗱 𝗶𝗻𝘁𝗲𝗿𝗮𝗰𝘁𝗶𝗼𝗻𝘀 and 𝗽𝗵𝘆𝘀𝗶𝗼𝗹𝗼𝗴𝗶𝗰𝗮𝗹 𝘁𝗲𝗺𝗽𝗲𝗿𝗮𝘁𝘂𝗿𝗲𝘀 add layers of complexity. This Summer, the NativeMP™ Targets have changed the game by maintaining membrane proteins in their native environment—enabling high-quality assays, deep insights into 𝗽𝗿𝗼𝘁𝗲𝗶𝗻-𝗹𝗶𝗽𝗶𝗱 𝗶𝗻𝘁𝗲𝗿𝗮𝗰𝘁𝗶𝗼𝗻𝘀, and application versatility at physiological conditions. We were already able to present data from a wide array of protein classes, acquired detergent-free, rapidly solubilized, and stabilized directly from the cell. Even large and complex targets, such as 𝗧𝗟𝗥𝟱, 𝗔𝗕𝗖𝗔𝟭𝟮, or coexpression of 𝗜𝗧𝗚𝗕𝟯/𝗔𝗩 have been possible. And more is yet to come. What are you waiting for? 👉 Let’s enable drug discovery together by embracing new possibilities in target acquisition and innovation, streamlining research processes, and achieving reliable, consistent results.   #drugdiscovery #membraneproteins #nativeMP

𝗙𝗿𝗼𝗺 𝗔𝗳𝗳𝗶𝗻𝗶𝘁𝘆 𝗣𝘂𝗿𝗶𝗳𝗶𝗰𝗮𝘁𝗶𝗼𝗻 𝘁𝗼 𝗣𝘂𝗹𝗹-𝗗𝗼𝘄𝗻 𝗔𝘀𝘀𝗮𝘆𝘀 - 𝗢𝗻𝗲 𝘁𝗲𝗰𝗵𝗻𝗼𝗹𝗼𝗴𝘆 𝗳𝗼𝗿 𝘆𝗼𝘂𝗿 𝗲𝗻𝘁𝗶𝗿𝗲 𝗺𝗲𝗺𝗯𝗿𝗮𝗻𝗲 𝗽𝗿𝗼𝘁𝗲𝗶𝗻 𝘄𝗼𝗿𝗸𝗳𝗹𝗼𝘄 𝖮𝗎𝗋 𝗆𝗈𝗌𝗍 𝗉𝗈𝗐𝖾𝗋𝖿𝗎𝗅 𝗌𝗈𝗅𝗎𝗍𝗂𝗈𝗇 𝗒𝖾𝗍: 𝖳𝗁𝖾 𝗡𝗮𝘁𝗶𝘃𝗲𝗠𝗣™ 𝗕𝗶𝗼𝘁𝗶𝗻 𝗞𝗶𝘁! 𝖡𝖺𝗌𝖾𝖽 𝗈𝗇 𝗈𝗎𝗋 𝗡𝗮𝘁𝗶𝘃𝗲𝗠𝗣™ 𝗧𝗲𝗰𝗵𝗻𝗼𝗹𝗼𝗴𝘆—𝗍𝗁𝖺𝗍 𝗉𝗋𝖾𝗌𝖾𝗋𝗏𝖾𝗌 𝗆𝖾𝗆𝖻𝗋𝖺𝗇𝖾 𝗉𝗋𝗈𝗍𝖾𝗂𝗇𝗌 𝗂𝗇 𝗍𝗁𝖾𝗂𝗋 𝗇𝖺𝗍𝗂𝗏𝖾 𝗅𝗂𝗉𝗂𝖽 𝖾𝗇𝗏𝗂𝗋𝗈𝗇𝗆𝖾𝗇𝗍 𝗐𝗂𝗍𝗁 𝖼𝗈𝗉𝗈𝗅𝗒𝗆𝖾𝗋 𝗇𝖺𝗇𝗈𝖽𝗂𝗌𝖼𝗌—𝗐𝖾 𝗁𝖺𝗏𝖾 𝖾𝗑𝗉𝖺𝗇𝖽𝖾𝖽 𝗂𝗍𝗌 𝖼𝖺𝗉𝖺𝖻𝗂𝗅𝗂𝗍𝗂𝖾𝗌 𝗐𝗂𝗍𝗁 𝖻𝗂𝗈𝗍𝗂𝗇𝗒𝗅𝖺𝗍𝖾𝖽 𝖼𝗈𝗉𝗈𝗅𝗒𝗆𝖾𝗋𝗌. 𝖳𝗁𝗂𝗌 𝗅𝖺𝗍𝖾𝗌𝗍 𝖾𝗏𝗈𝗅𝗎𝗍𝗂𝗈𝗇 𝗂𝗇 𝗆𝖾𝗆𝖻𝗋𝖺𝗇𝖾 𝗉𝗋𝗈𝗍𝖾𝗂𝗇 𝗋𝖾𝗌𝖾𝖺𝗋𝖼𝗁 𝖻𝗋𝗂𝗇𝗀𝗌 𝗒𝗈𝗎 𝖺 𝖼𝗈𝗆𝗉𝗅𝖾𝗍𝖾 𝗌𝗈𝗅𝗎𝗍𝗂𝗈𝗇, 𝖺𝗅𝗅𝗈𝗐𝗂𝗇𝗀 𝗒𝗈𝗎 𝗍𝗈 𝗍𝗋𝖾𝖺𝗆𝗅𝗂𝗇𝖾 𝗒𝗈𝗎𝗋 𝗐𝗈𝗋𝗄𝖿𝗅𝗈𝗐 𝗅𝗂𝗄𝖾 𝗇𝖾𝗏𝖾𝗋 𝖻𝖾𝖿𝗈𝗋𝖾. 𝖳𝗋𝖺𝗇𝗌𝗂𝗍𝗂𝗈𝗇 𝗌𝖾𝖺𝗆𝗅𝖾𝗌𝗌𝗅𝗒 𝖺𝖼𝗋𝗈𝗌𝗌 𝗆𝗎𝗅𝗍𝗂𝗉𝗅𝖾 𝖺𝗉𝗉𝗅𝗂𝖼𝖺𝗍𝗂𝗈𝗇𝗌: ◾ 𝗔𝗳𝗳𝗶𝗻𝗶𝘁𝘆 𝗣𝘂𝗿𝗶𝗳𝗶𝗰𝗮𝘁𝗶𝗼𝗻: 𝖨𝗌𝗈𝗅𝖺𝗍𝖾 𝖻𝗂𝗈𝗍𝗂𝗇-𝗍𝖺𝗀𝗀𝖾𝖽 𝖼𝗈𝗉𝗈𝗅𝗒𝗆𝖾𝗋 𝗇𝖺𝗇𝗈𝖽𝗂𝗌𝖼𝗌 𝗍𝗁𝖺𝗍 𝖼𝗈𝗇𝗍𝖺𝗂𝗇 𝗒𝗈𝗎𝗋 𝗆𝖾𝗆𝖻𝗋𝖺𝗇𝖾 𝗉𝗋𝗈𝗍𝖾𝗂𝗇. ◾ 𝗦𝘂𝗿𝗳𝗮𝗰𝗲 𝗜𝗺𝗺𝗼𝗯𝗶𝗹𝗶𝘇𝗮𝘁𝗶𝗼𝗻: 𝖴𝗌𝖾 𝗍𝗁𝖾 𝖻𝗂𝗈𝗍𝗂𝗇 𝗍𝖺𝗀 𝗈𝗇 𝗍𝗁𝖾 𝖼𝗈𝗉𝗈𝗅𝗒𝗆𝖾𝗋 𝖿𝗈𝗋 𝖽𝗂𝗋𝖾𝖼𝗍 𝗂𝗆𝗆𝗈𝖻𝗂𝗅𝗂𝗓𝖺𝗍𝗂𝗈𝗇 𝗂𝗇 𝖲𝖯𝖱, 𝖤𝖫𝖨𝖲𝖠, 𝖺𝗇𝖽 𝗈𝗍𝗁𝖾𝗋 𝖺𝗌𝗌𝖺𝗒𝗌. ◾ 𝗣𝘂𝗹𝗹-𝗗𝗼𝘄𝗻 𝗔𝘀𝘀𝗮𝘆𝘀: 𝖢𝖺𝗉𝗍𝗎𝗋𝖾, 𝖺𝗇𝖺𝗅𝗒𝗓𝖾, 𝖺𝗇𝖽 𝗂𝖽𝖾𝗇𝗍𝗂𝖿𝗒 𝗉𝗋𝗈𝗍𝖾𝗂𝗇 𝗂𝗇𝗍𝖾𝗋𝖺𝖼𝗍𝗂𝗈𝗇𝗌 𝗂𝗇 𝗏𝗂𝗍𝗋𝗈. 𝖮𝗎𝗋 𝖻𝗂𝗈𝗍𝗂𝗇𝗒𝗅𝖺𝗍𝗂𝗈𝗇 𝗂𝗇𝗇𝗈𝗏𝖺𝗍𝗂𝗈𝗇 𝗉𝗅𝖺𝖼𝖾𝗌 𝗍𝗁𝖾 𝗍𝖺𝗀 𝗈𝗇 𝗍𝗁𝖾 𝖼𝗈𝗉𝗈𝗅𝗒𝗆𝖾𝗋 𝗂𝗍𝗌𝖾𝗅𝖿—𝗻𝗼𝘁 𝘁𝗵𝗲 𝗽𝗿𝗼𝘁𝗲𝗶𝗻, 𝗆𝖾𝖺𝗇𝗂𝗇𝗀 𝗇𝗈 𝗂𝗇𝗍𝖾𝗋𝖿𝖾𝗋𝖾𝗇𝖼𝖾 𝗐𝗂𝗍𝗁 𝗍𝗁𝖾 𝗉𝗋𝗈𝗍𝖾𝗂𝗇’𝗌 𝗌𝗍𝗋𝗎𝖼𝗍𝗎𝗋𝖾 𝗈𝗋 𝖿𝗎𝗇𝖼𝗍𝗂𝗈𝗇. 𝖳𝗁𝗂𝗌 𝖺𝗅𝗅𝗈𝗐𝗌 𝗒𝗈𝗎 𝗍𝗈 𝖿𝗈𝖼𝗎𝗌 𝗈𝗇 𝖾𝗑𝗉𝗋𝖾𝗌𝗌𝗂𝗇𝗀 𝗈𝗇𝖾 𝗌𝗂𝗇𝗀𝗅𝖾 𝘂𝗻𝗺𝗼𝗱𝗶𝗳𝗶𝗲𝗱 𝗽𝗿𝗼𝘁𝗲𝗶𝗻 𝖿𝗈𝗋 𝗆𝗎𝗅𝗍𝗂𝗉𝗅𝖾 𝖽𝗈𝗐𝗇𝗌𝗍𝗋𝖾𝖺𝗆 𝗉𝗋𝗈𝖼𝖾𝗌𝗌𝖾𝗌 𝗅𝗂𝗄𝖾 𝖲𝖯𝖱, 𝖥𝖠𝖢𝖲, 𝖺𝗇𝖽 𝗆𝗈𝗋𝖾. 𝗔 𝗖𝗼𝗺𝗽𝗹𝗲𝘁𝗲, 𝗙𝗹𝗲𝘅𝗶𝗯𝗹𝗲 𝗦𝗼𝗹𝘂𝘁𝗶𝗼𝗻: 𝖶𝗂𝗍𝗁 𝗍𝗁𝖾 𝖿𝗈𝗎𝗋 𝖼𝗈𝗉𝗈𝗅𝗒𝗆𝖾𝗋 𝖻𝖺𝖼𝗄𝖻𝗈𝗇𝖾𝗌 𝗖𝘂𝗯𝗶𝗽𝗼𝗹, 𝗨𝗹𝘁𝗿𝗮𝘀𝗼𝗹𝘂𝘁𝗲™ 𝗔𝗺𝗽𝗵𝗶𝗽𝗼𝗹, 𝗗𝗜𝗕𝗠𝗔, 𝖺𝗇𝖽 𝗔𝗔𝗦𝗧𝗬, 𝗍𝗁𝖾 𝖭𝖺𝗍𝗂𝗏𝖾𝖬𝖯™ 𝖡𝗂𝗈𝗍𝗂𝗇 𝖪𝗂𝗍 𝖺𝖽𝖺𝗉𝗍𝗌 𝗍𝗈 𝗒𝗈𝗎𝗋 𝗉𝗋𝗈𝗍𝖾𝗂𝗇'𝗌 𝗎𝗇𝗂𝗊𝗎𝖾 𝗇𝖾𝖾𝖽𝗌, 𝗈𝗉𝗍𝗂𝗆𝗂𝗓𝗂𝗇𝗀 𝖾𝗏𝖾𝗋𝗒 𝗌𝗍𝖾𝗉 𝗈𝖿 𝗍𝗁𝖾 𝗐𝖺𝗒. O𝗎𝗋 𝖡𝗂𝗈𝗍𝗂𝗇 𝖪𝗂𝗍 𝗇𝗈𝗍 𝗈𝗇𝗅𝗒 𝗌𝖺𝗏𝖾𝗌 𝗍𝗂𝗆𝖾 in the lab 𝖻𝗎𝗍 𝖺𝗅𝗌𝗈 𝖾𝗇𝗁𝖺𝗇𝖼𝖾𝗌 𝗽𝗿𝗲𝗰𝗶𝘀𝗶𝗼𝗻, 𝗰𝗼𝗻𝘃𝗲𝗻𝗶𝗲𝗻𝗰𝗲, and 𝗾𝘂𝗮𝗹𝗶𝘁𝘆—𝗍𝗋𝗎𝖾 𝗍𝗈 𝗈𝗎𝗋 𝖭𝖺𝗍𝗂𝗏𝖾𝖬𝖯™ 𝗉𝗋𝗈𝗆𝗂𝗌𝖾. ➡️ 𝖢𝗁𝖾𝖼𝗄 𝗈𝗎𝗍 𝗈𝗎𝗋 𝖲𝖯𝖱 𝖽𝖺𝗍𝖺 𝗈𝗇 𝗍𝗁𝖾 𝗉𝗋𝗈𝖽𝗎𝖼𝗍 𝗌𝗂𝗍𝖾: https://lnkd.in/ewdqgsPG #BiotinTag #SPR #NativeMP #MembraneProtein #CubeBiotech

🎉 We're excited to be attending the Human Proteome Organization (HUPO) World Congress in Germany! Stop by Booth 3 and say hello 👋. Or arrange a meeting with our Strategic Partnership Managers, Thomas Perkins, Jr. and Sebastian Lühn – they're looking forward to answering your questions and are happy to assist you! 🤝 See you at HUPO! 🔬💼 #HUPO2024

Our co-founder and CSO Jan Kubicek had the opportunity to share some insights at Discovery on Target 2024 about one of the biggest challenges in membrane protein research: stabilization. In our talk, we discussed how next-generation NativeMP copolymers are paving the way for more efficient stabilization of membrane proteins into native nanodiscs, preserving their natural environment and functionality. If you’re working in biotherapeutics or are interested in membrane protein research, this approach could be a game changer! Check out the full talk here: https://lnkd.in/eKZ8ngFM

The COVID-19 pandemic, resulting in over 5 million deaths, has highlighted the urgent 𝗻𝗲𝗲𝗱 𝗳𝗼𝗿 𝘁𝗵𝗲𝗿𝗮𝗽𝗲𝘂𝘁𝗶𝗰 𝗮𝗽𝗽𝗿𝗼𝗮𝗰𝗵𝗲𝘀, 𝘄𝗶𝘁𝗵 𝘁𝗵𝗲 𝘃𝗶𝗿𝘂𝘀'𝘀 𝘀𝗽𝗶𝗸𝗲 𝗽𝗿𝗼𝘁𝗲𝗶𝗻 𝗲𝗺𝗲𝗿𝗴𝗶𝗻𝗴 𝗮𝘀 𝗮 𝗽𝗿𝗼𝗺𝗶𝘀𝗶𝗻𝗴 𝗰𝗮𝗻𝗱𝗶𝗱𝗮𝘁𝗲, 𝗳𝗼𝗿 𝘁𝗵𝗲 𝗱𝗲𝘃𝗲𝗹𝗼𝗽𝗺𝗲𝗻𝘁 𝗼𝗳 𝘁𝗵𝗲𝗿𝗮𝗽𝗲𝘂𝘁𝗶𝗰 𝘁𝗮𝗿𝗴𝗲𝘁𝘀.   🇵🇦🇵🇪🇷 🇴🇫 🇹🇭🇪 🇲🇴🇳🇹🇭 - 𝘐𝘯𝘴𝘦𝘤𝘵 𝘤𝘦𝘭𝘭 𝘦𝘹𝘱𝘳𝘦𝘴𝘴𝘪𝘰𝘯 𝘢𝘯𝘥 𝘱𝘶𝘳𝘪𝘧𝘪𝘤𝘢𝘵𝘪𝘰𝘯 𝘰𝘧 𝘳𝘦𝘤𝘰𝘮𝘣𝘪𝘯𝘢𝘯𝘵 𝘚𝘈𝘙𝘚-𝘊𝘖𝘝-2 𝘴𝘱𝘪𝘬𝘦 𝘱𝘳𝘰𝘵𝘦𝘪𝘯𝘴 𝘵𝘩𝘢𝘵 𝘥𝘦𝘮𝘰𝘯𝘴𝘵𝘳𝘢𝘵𝘦 𝘈𝘊𝘌2 𝘣𝘪𝘯𝘥𝘪𝘯𝘨 (2022)   𝗝𝗼𝗶𝗻 𝘂𝘀 𝗮𝘀 𝘄𝗲 𝗱𝗲𝗹𝘃𝗲 𝗶𝗻𝘁𝗼 𝗮 𝗺𝗲𝘁𝗵𝗼𝗱 𝘁𝗵𝗮𝘁 𝗼𝗳𝗳𝗲𝗿𝘀 𝗮 𝘀𝗰𝗮𝗹𝗮𝗯𝗹𝗲, 𝗰𝗼𝘀𝘁-𝗲𝗳𝗳𝗲𝗰𝘁𝗶𝘃𝗲 𝗽𝗹𝗮𝘁𝗳𝗼𝗿𝗺 𝗳𝗼𝗿 𝗽𝗿𝗼𝗱𝘂𝗰𝗶𝗻𝗴 𝗳𝘂𝗻𝗰𝘁𝗶𝗼𝗻𝗮𝗹 𝘀𝗽𝗶𝗸𝗲 𝗽𝗿𝗼𝘁𝗲𝗶𝗻𝘀 𝗳𝗼𝗿 𝗿𝗲𝘀𝗲𝗮𝗿𝗰𝗵 𝗮𝗻𝗱 𝘁𝗵𝗲𝗿𝗮𝗽𝗲𝘂𝘁𝗶𝗰 𝗱𝗲𝘃𝗲𝗹𝗼𝗽𝗺𝗲𝗻𝘁. Struble 𝘦𝘵 𝘢𝘭. from the Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Media Center, developed and optimized a robust SARS-CoV-2 spike protein expression and purification protocol using insect cells.    The study focused on four recombinant SARS-CoV-2 spike protein constructs, including the spike receptor-binding domain (S-RBD-eGFP) and various spike ectodomains, with and without stabilizing mutations. The team tested the protein yield in two insect cell lines, Sf9 and Tni, demonstrating higher yields in Tni cells. The purified spike proteins were functional, glycosylated, and capable of binding to the ACE2 receptor, with validation through flow cytometry.     https://lnkd.in/eisiK2jt   Lucas Struble, Audrey Smith, William E. Lutz Nebraska, Gabrielle Grubbs, Sagar Satish, Ken Bayles, Dr. Prakash Radhakrishnan, Surender Khurana, Dalia El-Gamal, Gloria Borgstahl -University of Nebraska Medical Center- We are dedicating a spot in our "Paper of the Month" series to this exciting research. Check it out on our website: https://lnkd.in/eUQds2qu    For the purification procedure of the different SARS-CoV-2 spike protein constructs, 𝘁𝗵𝗲 𝘀𝘁𝘂𝗱𝘆 𝘁𝗲𝘀𝘁𝗲𝗱 𝘁𝗵𝗿𝗲𝗲 𝗜𝗠𝗔𝗖 𝗿𝗲𝘀𝗶𝗻𝘀, 𝗳𝗶𝗻𝗱𝗶𝗻𝗴 𝘁𝗵𝗮𝘁 𝗜𝗡𝗗𝗜𝗚𝗢-𝗡𝗶 𝗿𝗲𝘀𝗶𝗻 𝘄𝗮𝘀 𝘁𝗵𝗲 𝗺𝗼𝘀𝘁 𝗲𝗳𝗳𝗶𝗰𝗶𝗲𝗻𝘁 𝗱𝘂𝗲 𝘁𝗼 𝗶𝘁𝘀 𝗿𝗲𝘀𝗶𝘀𝘁𝗮𝗻𝗰𝗲 𝘁𝗼 𝗻𝗶𝗰𝗸𝗲𝗹 𝗶𝗼𝗻 𝗹𝗲𝗮𝗰𝗵𝗶𝗻𝗴 𝗮𝗻𝗱 𝗿𝗲𝗱𝘂𝗰𝗲𝗱 𝗶𝗺𝗽𝘂𝗿𝗶𝘁𝘆 𝗰𝗼-𝗽𝘂𝗿𝗶𝗳𝗶𝗰𝗮𝘁𝗶𝗼𝗻, 𝗰𝗼𝗺𝗽𝗮𝗿𝗲𝗱 𝘁𝗼 𝘄𝗲𝗹𝗹-𝗸𝗻𝗼𝘄𝗻 𝗰𝗼𝗺𝗽𝗲𝘁𝗶𝘁𝗼𝗿𝘀.  

The 2024 Nobel Prize in Chemistry has celebrated groundbreaking work in protein science, recognizing David Baker for creating new kinds of proteins and Demis Hassabis and John Jumper for revolutionizing protein structure prediction with AlphaFold2. Their discoveries are truly a game-changer in structural biology. But as I’ve discussed at recent conferences, the challenge now lies in translating these computational models into real-world structures. Many times, what we see in silico doesn’t fully reflect real-life protein behavior—and one key missing piece might be the native lipid environment. Lipids are critical. Proteins do not exist in isolation; they often interact with lipids, which play a fundamental role in preserving the protein’s structure and function. We must not overlook this factor when validating AI-predicted models in the lab. These discoveries are certainly opening up new horizons, but the wet lab work remains vital to ensure these models meet biological reality. It's up to us to prove these predictions and fully unlock the potential of AI-driven protein science. At Cube Biotech, we're committed to providing the tools and insights necessary to bridge this gap. Through our NativeMP™ platform, we enable researchers to work with membrane proteins in their native lipid environment, getting as close as possible to the real structure. Let's talk more about these advancements and potential collaborations at upcoming events. I'll be attending Festival of Biologics in Basel. Looking forward to connecting! #ProteinScience #NobelPrize2024 #MembraneProteins #StructuralBiology

NOW LIVE: Join us to learn more about cell-free, cryo-EM, GPCRs, and structural biology with Dr. Frank Bernhard from Goethe University Frankfurt, Germany 🎬

🚨 Last Day to Visit Us at Discovery on Target (Booth 503)! If you're looking for membrane protein drug targets, today is your final chance to stop by! We’d love to meet you in Boston with Jan Kubicek, Barbara Maertens, DIDIER DARGENT, and Daniel Turman.   💡 Don't miss Barbara M.'s poster presentation this morning at DOT A21 on Next Generation Copolymers for membrane protein characterization in near-native conditions.   Come chat with us and explore how we can support your research needs!

📢 Join Our Masterclass with Dr. Frank Bernhard Learn how cell-free expression systems offer rapid pathways to Cryo-EM structures of GPCR complexes. Key Takeaways: - Cell-free expression is a modular system and protocols can be adjusted to different targets. - E. coli lysates represent an affordable and efficient production pipeline giving fast access to non-truncated GPCR structures in active conformation. - Co-translational insertion of membrane proteins into preformed nanoparticles avoids any detergent contacts and reduces sample preparation procedures to less than 24 hours. - Cell-free expression is an interesting alternative platform for the production of membrane proteins that are difficult to synthesize in conventional cell-based expression systems #CryoEM #GPCR #BiophysicalChemistry #MembraneProteins #CellFreeSynthesis #StructuralBiology