PubMed Health⌕ Search

PubMed · 16223789

Improving disulfide connectivity prediction with sequential distance between oxidized cysteines.

Abstract

SUMMARY: Predicting disulfide connectivity precisely helps towards the solution of protein structure prediction. In this study, a descriptor derived from the sequential distance between oxidized cysteines (denoted as DOC) is proposed. An approach using support vector machine (SVM) method based on weighted graph matching was further developed to predict the disulfide connectivity pattern in proteins. When DOC was applied, prediction accuracy of 63% for our SVM models could be achieved, which is significantly higher than those obtained from previous approaches. The results show that using the non-local descriptor DOC coupled with local sequence profiles significantly improves the prediction accuracy. These improvements demonstrate that DOC, with a proper scaling scheme, is an effective feature for the prediction of disulfide connectivity. The method developed in this work is available at the web server PreCys (prediction of cys-cys linkages of proteins).

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Chi-Hung Tsai, Bo-Juen Chen, Chen-Hsiung Chan, Hsuan-Liang Liu, Cheng-Yan Kao. 2005-10-13. Improving disulfide connectivity prediction with sequential distance between oxidized cysteines.. https://doi.org/10.1093/bioinformatics%2Fbti715

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Deep UV laser-induced fluorescence detection of unlabeled drugs and proteins in microchip electrophoresis.

Deep UV fluorescence detection at 266-nm excitation wavelength has been realized for sensitive detection in microchip electrophoresis. For this purpose, an epifluorescence setup was developed enabling the coupling of a deep UV laser into a commercial fluorescence microscope. Deep UV laser excitation utilizing a frequency quadrupled pulsed laser operating at 266 nm shows an impressive performance for native fluorescence detection of various compounds in fused-silica microfluidic devices. Aromatic low molecular weight compounds such as serotonin, propranolol, a diol, and tryptophan could be detected at low-micromolar concentrations. Deep UV fluorescence detection was also successfully employed for the detection of unlabeled basic proteins. For this purpose, fused-silica chips dynamically coated with hydroxypropylmethyl cellulose were employed to suppress analyte adsorption. Utilizing fused-silica chips permanently coated with poly(vinyl alcohol), it was also possible to separate and detect egg white chicken proteins. These data show that deep UV fluorescence detection significantly widens the application range of fluorescence detection in chip-based analysis techniques.

Chymotrypsinogen↗

On-line sample enrichment for the determination of proteins by capillary zone electrophoresis with poly(vinyl alcohol)-coated bubble cell capillaries.

Field-amplified sample stacking (FASS) is used to separate basic proteins in a poly-(vinyl alcohol)-coated bubble cell capillary. To our knowledge, this is the first paper describing the on-column stacking of proteins (as cations) using FASS in bubble cell capillary. The bubble cell capillary is fabricated using a one-step method. Cetyltrimethylammonium chloride is added into the running buffer to reverse the EOF and, thus, to pump the water plug out during the sample stacking step. The effect of the water plug lengths and sample injection durations were investigated and optimized. The results obtained were compared with those for the normal capillary without bubble cell in terms of resolution and sensitivity enhancement. Under the optimal condition, this method can improve the sensitivity of the peak areas ranging from 5000- to 26 000-fold. The RSDs (n = 5) of the migration time and peak area are satisfactory (less than 0.6 and 12%, respectively). Application of the capillary electrophoresis method with bubble cell, FASS, and UV detection thereby leads to the determination of these proteins at concentrations ranging from 3 to 10 ng/mL, based on a signal-to-noise ratio of 3:1.

Chymotrypsinogen↗

Noninvasive determination of protein conformation in the solid state using near infrared (NIR) spectroscopy.

Fourier transform infrared (FTIR) spectroscopy is a powerful tool for monitoring structural changes in lyophilized protein formulations. However, direct measurement of IR spectra requires significant handling time and effort. The possibility of using near infrared (NIR) spectroscopy as a rapid and noninvasive alternative to FTIR is explored in this study. NIR and conventional FTIR spectra were collected for two model proteins, alpha-chymotrypsinogen A and cytochrome c, under conditions of varying stability and structural perturbation. NIR was then compared to FTIR and whereby calibration model was generated by partial least square (PLS) regression to correlate NIR data with FTIR spectra. There is a strong correlation of certain NIR bands with the amide I region of FTIR spectra. It appears that NIR can distinguish damage caused by elevated temperatures and freeze-drying stresses. The ability of sucrose to stabilize the structure of these two proteins can be detected by both methods. It appears that NIR spectroscopy has the potential to provide detailed information on the secondary structure of proteins in the solid state. However, many more examples will be needed to demonstrate fully the ability of NIR to replace FTIR as the standard tool for characterizing lyophilized protein formulations.

Chymotrypsinogen↗