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      <title>Quartz 4</title>
      <link>https://notes.delalamo.xyz</link>
      <description>Last 10 notes on Quartz 4</description>
      <generator>Quartz -- quartz.jzhao.xyz</generator>
      <item>
    <title>Model type less important than data quantity when predicting catalytic properties of protein sequences</title>
    <link>https://notes.delalamo.xyz/notes/Model-type-less-important-than-data-quantity-when-predicting-catalytic-properties-of-protein-sequences</link>
    <guid>https://notes.delalamo.xyz/notes/Model-type-less-important-than-data-quantity-when-predicting-catalytic-properties-of-protein-sequences</guid>
    <description><![CDATA[ Summary The type of predictive model used is less important than the quantity of data available when predicting catalytic properties of protein sequences (1). ]]></description>
    <pubDate>Sun, 10 May 2026 10:41:28 GMT</pubDate>
  </item><item>
    <title>Cysteines are the most common conserved residue in E. coli</title>
    <link>https://notes.delalamo.xyz/notes/Cysteines-are-the-most-common-conserved-residue-in-E.-coli</link>
    <guid>https://notes.delalamo.xyz/notes/Cysteines-are-the-most-common-conserved-residue-in-E.-coli</guid>
    <description><![CDATA[ Summary Cysteine residues are the most widespread conserved residue in E. coli(1). Figures Ref(1) 1. ]]></description>
    <pubDate>Wed, 06 May 2026 14:04:27 GMT</pubDate>
  </item><item>
    <title>Buried CDR residue mutations have similar effects on expression in other globular proteins</title>
    <link>https://notes.delalamo.xyz/notes/Buried-CDR-residue-mutations-have-similar-effects-on-expression-in-other-globular-proteins</link>
    <guid>https://notes.delalamo.xyz/notes/Buried-CDR-residue-mutations-have-similar-effects-on-expression-in-other-globular-proteins</guid>
    <description><![CDATA[ Summary Buried CDR residue mutations affect expression similarly to partially buried residues in other globular proteins(1). Figures Ref(1) 1. ]]></description>
    <pubDate>Wed, 06 May 2026 10:04:28 GMT</pubDate>
  </item><item>
    <title>CDR sequence changes are enough to destabilize antibodies</title>
    <link>https://notes.delalamo.xyz/notes/CDR-sequence-changes-are-enough-to-destabilize-antibodies</link>
    <guid>https://notes.delalamo.xyz/notes/CDR-sequence-changes-are-enough-to-destabilize-antibodies</guid>
    <description><![CDATA[ Summary Changes in the sequence of CDRs is sufficient to destabilize antibodies and lower thermostability (1). ]]></description>
    <pubDate>Wed, 06 May 2026 10:04:28 GMT</pubDate>
  </item><item>
    <title>CDR1 and CDR2 contribute more to antibody stability than CDR3</title>
    <link>https://notes.delalamo.xyz/notes/CDR1-and-CDR2-contribute-more-to-antibody-stability-than-CDR3</link>
    <guid>https://notes.delalamo.xyz/notes/CDR1-and-CDR2-contribute-more-to-antibody-stability-than-CDR3</guid>
    <description><![CDATA[ Summary An antibody’s CDR1 and CDR2 contribute more to overall fold stability than CDR3(1). ]]></description>
    <pubDate>Wed, 06 May 2026 10:04:28 GMT</pubDate>
  </item><item>
    <title>ESM-IF outperforms ProteinMPNN on Ab inverse folding and affinity prediction</title>
    <link>https://notes.delalamo.xyz/notes/ESM-IF-outperforms-ProteinMPNN-on-Ab-inverse-folding-and-affinity-prediction</link>
    <guid>https://notes.delalamo.xyz/notes/ESM-IF-outperforms-ProteinMPNN-on-Ab-inverse-folding-and-affinity-prediction</guid>
    <description><![CDATA[ Summary ESM-IF outperforms ProteinMPNN on designing high-affinity structures of antibodies in both a zero-shot (1) and few-shot (2) setting. ]]></description>
    <pubDate>Wed, 06 May 2026 10:04:28 GMT</pubDate>
  </item><item>
    <title>Fold stability is more strongly correlated with a protein&#039;s ability to refold after denaturing than its melting temperature</title>
    <link>https://notes.delalamo.xyz/notes/Fold-stability-is-more-strongly-correlated-with-a-protein's-ability-to-refold-after-denaturing-than-its-melting-temperature</link>
    <guid>https://notes.delalamo.xyz/notes/Fold-stability-is-more-strongly-correlated-with-a-protein's-ability-to-refold-after-denaturing-than-its-melting-temperature</guid>
    <description><![CDATA[ Summary A protein’s fold stability is more strongly correlated with its ability to refold after denaturing than its absolute melting temperature(1). ]]></description>
    <pubDate>Wed, 06 May 2026 10:04:28 GMT</pubDate>
  </item><item>
    <title>Inverse folding model logits can  zero-shot predict expression changes arising from in antibody CDRs in cases where ground truth structure is known</title>
    <link>https://notes.delalamo.xyz/notes/Inverse-folding-model-logits-can--zero-shot-predict-expression-changes-arising-from-in-antibody-CDRs-in-cases-where-ground-truth-structure-is-known</link>
    <guid>https://notes.delalamo.xyz/notes/Inverse-folding-model-logits-can--zero-shot-predict-expression-changes-arising-from-in-antibody-CDRs-in-cases-where-ground-truth-structure-is-known</guid>
    <description><![CDATA[ Summary Inverse folding models like ProteinMPNN can zero-shot predict expression changes arising from mutations in CDRs when the ground truth experimental structure is available(1). ]]></description>
    <pubDate>Wed, 06 May 2026 10:04:28 GMT</pubDate>
  </item><item>
    <title>Large-scale measurements, such as Kd and IC50, from different assays correlate weakly in different studies</title>
    <link>https://notes.delalamo.xyz/notes/Large-scale-measurements,-such-as-Kd-and-IC50,-from-different-assays-correlate-weakly-in-different-studies</link>
    <guid>https://notes.delalamo.xyz/notes/Large-scale-measurements,-such-as-Kd-and-IC50,-from-different-assays-correlate-weakly-in-different-studies</guid>
    <description><![CDATA[ Summary Measurements of protein-ligand effects (such as K_d and IC_50) carried out in different assays only weakly correlate with each other. ]]></description>
    <pubDate>Wed, 06 May 2026 10:04:28 GMT</pubDate>
  </item><item>
    <title>iPAE is anticorrelated with number of interface H-bonds</title>
    <link>https://notes.delalamo.xyz/notes/iPAE-is-anticorrelated-with-number-of-interface-H-bonds</link>
    <guid>https://notes.delalamo.xyz/notes/iPAE-is-anticorrelated-with-number-of-interface-H-bonds</guid>
    <description><![CDATA[ Summary Interface PAE is anticorrelated with the number of H-bonds in PPIs(1). ]]></description>
    <pubDate>Wed, 06 May 2026 10:04:28 GMT</pubDate>
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