Electron paramagnetic resonance studies of spin-labeled fatty acid binding sites in Candida rugosa lipases
Article Abstract:
The binding of spin-labeled fatty acids (SLFA) to two isolipases from Candida rugosa has been studied through electron paramagnetic resonance (EPR)spectroscopy. The lipases help the fungus species adapt to nutrient differences in various physiological conditions. A minor isolipase termed lipase A which has greater ability to establish hydrophobic interactions is used in the research. EPR data reveal the presence of a tunnel in the enzyme which restricts the motion of the SLFA. These restrictions depend on the nature of the lipase and the position of the label.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 1998
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Catalytic mechanism and metal specificity of bacterial peptide deformylase: A density functional theory QM/MM study
Article Abstract:
Catalytic mechanism and metal specificity of bacterial peptide deformylase (PDF) is theoretically investigated using a hybrid density functional theory (B3LYP) QM/MM method and by studying both [Fe.sup.2+]-PDF and [Zn.sup.2+] -PDF.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2007
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- Abstracts: Electron paramagnetic resonance and ab initio structural studies on liquid crystalline systems. Layering transitions at the free surface of a smectic liquid crystal
- Abstracts: Experimental and Monte Carlo simulation studies on the competitive binding of Li+, Na+, and K+ ions to DNA in oriented DNA fibers
- Abstracts: Evaluation of functional group contributions to excess volumetric properties of solvated molecules