Conformation of lysozyme Langmuir monolayer studied by infrared reflection absorption spectroscopy.
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.
Department of Chemistry, 1301 Memorial Drive, University of Miami, Coral Gables, Florida 33146, USA.
Garima
G
Thakur
Roger M
RM
Leblanc
D000042:Absorption; D000388:Air; D002138:Calibration; D006863:Hydrogen-Ion Concentration; D008968:Molecular Conformation; D009113:Muramidase / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013053:Spectrophotometry / Q000379:methods; D013055:Spectrophotometry, Infrared / Q000379:methods; D013499:Surface Properties; D014867:Water / Q000737:chemistry
D010455:Peptides; D014867:Water; D009113:Muramidase