Journal article
Circular dichroism analysis of the glucan binding domain of Streptococcus mutans glucan binding protein-A
Biochimica et biophysica acta, Protein structure and molecular enzymology, Vol.1384(1), pp.112-120
1998
DOI: 10.1016/S0167-4838(98)00005-3
PMID: 9602086
Abstract
The glucan binding domain (GBD) of the glucan binding protein-A (GBP-A) from the cariogenic bacterium
Streptococcus mutans was studied using circular dichroism (CD) analysis, Chou–Fasman–Rose secondary structure prediction, and absorption and fluorescence spectroscopy. Our data show that the binding domain undergoes a conformational shift upon binding to the ligand dextran. The CD spectrum shows two positive bands at 280 nm and 230 nm which were assigned to aromatic residues. The 230-nm band was seen at 20°C and 30°C, lost intensity at 40°C, and was eliminated at 45°C coinciding with complete denaturation. The protein was stable at physiological pH, but precipitated at pH 5. A pH of 10 changed the secondary structure but had no effect on the 230-nm band. Analysis of the CD data in the far UV using the SELCON computer program revealed a high content of
β-sheets and a lack of
α-helical structures. Secondary structure prediction based on the amino acid sequence of GBD agreed with the CD analysis. The fluorescence emission maximum at 339 nm suggested that the majority of the tryptophans were located in the interior of the protein. This maximum shifted to higher energy upon binding to the ligand dextran.
Details
- Title: Subtitle
- Circular dichroism analysis of the glucan binding domain of Streptococcus mutans glucan binding protein-A
- Creators
- Wolfgang Haas - Albany Medical College-A68, 47 New Scotland Ave., Albany, NY 12208, USARobert MacColl - Wadsworth Center, New York State Department of Health, P.O. Box 509, Albany, NY 12201, USAJeffrey A Banas - Albany Medical College-A68, 47 New Scotland Ave., Albany, NY 12208, USA
- Resource Type
- Journal article
- Publication Details
- Biochimica et biophysica acta, Protein structure and molecular enzymology, Vol.1384(1), pp.112-120
- DOI
- 10.1016/S0167-4838(98)00005-3
- PMID
- 9602086
- NLM abbreviation
- Biochim Biophys Acta
- ISSN
- 0167-4838
- eISSN
- 1879-2588
- Publisher
- Elsevier B.V
- Language
- English
- Date published
- 1998
- Academic Unit
- Pediatric Dentistry; Dental Research
- Record Identifier
- 9984066080102771
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