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Related Concept Videos

Halogens03:01

Halogens

Group 17 elements, known as halogens, are nonmetals. At room temperature, fluorine and chlorine are gases, bromine is a liquid, and iodine a solid. Astatine is a highly unstable radioactive element, so currently, most of its properties are unknown due to its short half-life. Tennessine is a synthetic element also predicted to be in this group.
Electron Affinity03:07

Electron Affinity

The electron affinity (EA) is the energy change for adding an electron to a gaseous atom to form an anion (negative ion).
Electrophilic Aromatic Substitution: Fluorination and Iodination of Benzene01:13

Electrophilic Aromatic Substitution: Fluorination and Iodination of Benzene

Bromination and chlorination of aromatic rings by electrophilic aromatic substitution reactions are easily achieved, but fluorination and iodination are difficult to achieve. Fluorine is so reactive that its reaction with benzene is difficult to control, resulting in poor yields of monofluoroaromatic products. To address this, Selectfluor reagent is used as a fluorine source in which a fluorine atom is bonded to a positively charged nitrogen.
Other Nuclides: 31P, 19F, 15N NMR01:16

Other Nuclides: 31P, 19F, 15N NMR

Many organic, inorganic, and biological molecules contain spin-half nuclei such as nitrogen-15, fluorine-19, and phosphorus-31. As a result, NMR studies of these nuclei have found extensive applications in chemical and biological research.
While fluorine-19 and phosphorous-31 have high natural abundances (100%) and positive gyromagnetic ratios, nitrogen-15 has a low natural abundance and a negative gyromagnetic ratio. However, nitrogen-15 is still preferred over nitrogen-14 (which has a high...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

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Related Experiment Video

Updated: May 25, 2026

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

Fluorine: a new element in protein design.

Benjamin C Buer1, E Neil G Marsh

  • 1Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA.

Protein Science : a Publication of the Protein Society
|January 26, 2012
PubMed
Summary

Engineered fluorinated amino acids enhance protein stability against denaturation. This strategy creates novel proteins with improved chemical and biological properties, expanding possibilities in protein design.

Area of Science:

  • Biochemistry
  • Protein Engineering
  • Synthetic Biology

Background:

  • Fluorocarbons are synthetic molecules with unique properties like chemical inertness and thermal stability.
  • Fluorine is rare in natural biological systems.
  • The goal is to engineer these fluorocarbon properties into proteins.

Purpose of the Study:

  • To review studies on designing proteins with fluorinated amino acid analogs.
  • To assess the potential of fluorination for creating proteins with novel properties.
  • To explore the impact of fluorination on protein stability and function.

Main Methods:

  • Designing proteins incorporating highly fluorinated analogs of hydrophobic amino acids.
  • Reviewing existing research on fluorinated protein engineering.

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Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence
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Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence

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Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions
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Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions

Published on: October 21, 2016

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Last Updated: May 25, 2026

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence
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Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence

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Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions
10:44

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions

Published on: October 21, 2016

  • Investigating both soluble and membrane-bound proteins.

    • Main Results:

    • Fluorination is an effective strategy for enhancing protein stability against chemical and thermal denaturation.
    • Engineered proteins retain their structure and biological activity.
    • Most studies focus on small proteins due to synthesis challenges with larger ones.

    Conclusions:

    • Fluorination offers a general approach to improve protein stability and create novel functionalities.
    • Challenges remain in synthesizing large fluorinated proteins.
    • Biosynthetic methods for noncanonical amino acids will advance the use of fluorinated amino acids in protein design.