Azido homoalanine is a useful infrared probe for monitoring local electrostatistics and side-chain solvation in proteins

Jun Ho Choi, Daniel Raleigh, Minhaeng Cho

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

The use of IR probes to monitor protein structure, deduce local electric field, and investigate the mechanism of enzyme catalysis and protein folding has attracted increasing attention. Here the azidohomoalanine (Aha) is considered to be a useful IR probe. The intricate details of the distinct effects of backbone peptide bonds and H-bonded water molecules on the azido stretch mode of the IR probe Aha were revealed by carrying out QM/MM MD simulations of two variants of the protein NTL9, NTL9-Met1Aha, and NTL9-Ile4Aha and comparing the resulting simulated IR spectra with experiments.

Original languageEnglish
Pages (from-to)2158-2162
Number of pages5
JournalJournal of Physical Chemistry Letters
Volume2
Issue number17
DOIs
Publication statusPublished - 2011 Sep 1

Fingerprint

Solvation
Infrared radiation
Proteins
Monitoring
Protein Folding
Catalysis
Protein folding
Peptides
Water
Enzymes
Electric fields
Hydrogen
Molecules
azidohomoalanine
Experiments

Keywords

  • Biophysical Chemistry

ASJC Scopus subject areas

  • Materials Science(all)

Cite this

Azido homoalanine is a useful infrared probe for monitoring local electrostatistics and side-chain solvation in proteins. / Choi, Jun Ho; Raleigh, Daniel; Cho, Minhaeng.

In: Journal of Physical Chemistry Letters, Vol. 2, No. 17, 01.09.2011, p. 2158-2162.

Research output: Contribution to journalArticle

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