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Thermal stability of protein secondary structure in Langmuir-Blodgett films.
Nicolini, C; Erokhin, V; Antolini, F; Catasti, P; Facci, P.
Affiliation
  • Nicolini C; Institute of Biophysics, University of Genova, Italy.
Biochim Biophys Acta ; 1158(3): 273-8, 1993 Nov 28.
Article in En | MEDLINE | ID: mdl-8251527
ABSTRACT
The temperature dependence of the secondary structure of photosynthetic reaction centres from Rhodobacter sphaeroides in solution and in Langmuir-Blodgett film was studied by circular dichroism. It was shown that the secondary structure of the protein was not affected in Langmuir-Blodgett films by heating up to 200 degrees C, while in solution it was completely lost at 55 degrees C. Molecular order rather than decreased hydration degree was held responsible.
Subject(s)
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Database: MEDLINE Main subject: Protein Structure, Secondary / Hot Temperature Language: En Year: 1993 Type: Article
Search on Google
Database: MEDLINE Main subject: Protein Structure, Secondary / Hot Temperature Language: En Year: 1993 Type: Article