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PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase
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L-Tryptophan on Cu(111): engineering a molecular labyrinth driven by indole groups.

E N Yitamben1, A Clayborne, Seth B Darling

  • 1Center for Nanoscale Materials (CNM), Argonne National Laboratory, Argonne, IL 60439, USA.

Nanotechnology
|May 22, 2015
PubMed
Summary
This summary is machine-generated.

Researchers studied L-Tryptophan

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Area of Science:

  • Surface science
  • Biomolecular chemistry
  • Materials science

Background:

  • L-Tryptophan is an essential amino acid vital for protein synthesis.
  • It holds potential for chiral molecular electronics and biocompatible applications.

Purpose of the Study:

  • Investigate L-Tryptophan adsorption and molecular orientation on Cu(111).
  • Determine the influence of temperature and surface coverage on adsorption structures.

Main Methods:

  • Scanning tunneling microscopy (STM)
  • Scanning tunneling spectroscopy (STS)
  • Experiments conducted at 55 K and room temperature.

Main Results:

  • Adsorption structures of L-Tryptophan on Cu(111) depend on temperature and coverage.
  • Low coverage: small clusters form.
  • High coverage: ordered chains at room temperature, molecular labyrinth at 55 K.
  • Superstructure dominated by hydrogen and π-bonding interactions.

Conclusions:

  • Chemisorption of L-Tryptophan on Cu(111) is temperature and coverage dependent.
  • Intermolecular hydrogen bonding and π-bonding interactions dictate molecular arrangement.
  • Findings are relevant for designing molecular electronic and biocompatible devices.