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Related Concept Videos

Amino acids03:42

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Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible for...
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Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...
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Sulfation and α-amino acid conjugation are two critical biotransformation reactions in drug metabolism. Sulfation, a phase II biotransformation reaction, involves adding a polar sulfate group to a drug, enhancing its water solubility and promoting excretion. This process can either co-occur with or occur independently of glucuronidation. Nonmicrosomal sulfotransferase enzymes catalyze the process. The reaction involves 3'-phosphoadenosine-5'-phosphosulfate or PAPS coenzyme...
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Nucleophilic acyl substitution is an important class of substitution reactions involving a nucleophile and an acyl compound, such as carboxylic acids and their derivatives. In these reactions, the leaving group attached to the acyl group is substituted by a nucleophile. The general mechanism proceeds via two steps.
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Acids are classified by the number of protons per molecule that they can give up in a reaction. Acids such as HCl, HNO3, and HCN that contain one ionizable hydrogen atom in each molecule are called monoprotic acids. Their reactions with water are:
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Updated: Feb 12, 2026

Identifying Amino Acid Overproducers Using Rare-Codon-Rich Markers
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RECUR: identifying recurrent amino acid substitutions from multiple sequence alignments.

Elizabeth H J Robbins1, Yi Liu1, Steven Kelly1

  • 1Department of Biology, University of Oxford, Oxford OX1 3RB, UK.

Molecular Biology and Evolution
|February 11, 2026
PubMed
Summary

RECUR identifies recurrent amino acid substitutions in biological sequences, crucial for understanding evolution and disease. This method accurately detects widespread recurrent evolution in SARS-CoV-2 spike proteins, particularly at the hACE2 interface.

Keywords:
SARS-CoV-2 surface glycoproteinadaptationconvergent evolutionmultiple sequence alignmentparallel evolutionphylogenyrecurrent evolution

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Area of Science:

  • Evolutionary biology
  • Genomics
  • Structural biology

Background:

  • Recurrent evolutionary changes in biological sequences are vital for understanding phenotypes, antibiotic resistance, and disease.
  • Identifying these recurrent substitutions aids in pinpointing causative genetic alterations.

Purpose of the Study:

  • To introduce RECUR, a novel computational method for detecting recurrent amino acid substitutions in large multiple sequence alignments.
  • To assess the accuracy and robustness of RECUR using simulated and real-world biological data.

Main Methods:

  • Development of RECUR, a fast, user-friendly, and scalable algorithm for identifying recurrent amino acid substitutions.
  • Validation of RECUR's accuracy (100%) on simulated data and its robustness against tree inference errors.
  • Application of RECUR to analyze surface glycoprotein (S) protein sequences from SARS-CoV-2.

Main Results:

  • RECUR achieved 100% accuracy in detecting recurrent substitutions in simulated evolutionary histories.
  • Widespread recurrent evolution was identified in SARS-CoV-2 S proteins, enriched in the S1 subunit and hACE2 binding interface.
  • Recurrent substitutions were depleted at the S protein trimeric interface, with variable stability effects at the hACE2 interface.

Conclusions:

  • RECUR is a highly accurate and robust tool for identifying recurrent evolutionary events in biological sequences.
  • Recurrent evolution in the SARS-CoV-2 S protein, especially at the hACE2 interface, suggests a balance between receptor binding and immune evasion.
  • The findings highlight the utility of RECUR in studying viral evolution and adaptation.