Conformation of lysozyme langmuir monolayer studied by infrared reflection absorption spectroscopy

Garima Thakur, Roger Leblanc

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

The surface chemistry and spectroscopy of the reduced lysozyme Langmuir monolayer were investigated at different pH values to compare with the native one. It was found that the limiting molecular area of the reduced lysozyme was not subphase pH dependent as the native lysozyme. To explain this result in terms of the conformation and orientation of the lysozyme Langmuir monolayer at various subphase pH values, we have used infrared reflection absorption spectroscopy. The interpretation of the results make plausible change of the conformation and orientation of the native lysozyme Langmuir monolayer with the subphase pH 3, 6, and 11.

Original languageEnglish
Pages (from-to)2842-2849
Number of pages8
JournalLangmuir
Volume25
Issue number5
DOIs
StatePublished - Mar 3 2009

Fingerprint

monomolecular films
infrared reflection
lysozyme
Muramidase
Absorption spectroscopy
Conformations
Monolayers
absorption spectroscopy
Enzymes
Infrared radiation
Crystal orientation
Surface chemistry
Spectroscopy
chemistry
spectroscopy

ASJC Scopus subject areas

  • Electrochemistry
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Materials Science(all)
  • Spectroscopy

Cite this

Conformation of lysozyme langmuir monolayer studied by infrared reflection absorption spectroscopy. / Thakur, Garima; Leblanc, Roger.

In: Langmuir, Vol. 25, No. 5, 03.03.2009, p. 2842-2849.

Research output: Contribution to journalArticle

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