Determination of Protein Secondary Structure and Solvent Accessibility Using Site-Directed Fluorescence Labeling. Studies of T4 Lysozyme Using the Fluorescent Probe Monobromobimane†

Biochemistry ◽  
1999 ◽  
Vol 38 (49) ◽  
pp. 16383-16393 ◽  
Author(s):  
Steven E. Mansoor ◽  
Hassane S. Mchaourab ◽  
David L. Farrens
Keyword(s):  
Secondary Structure ◽  
Fluorescent Probe ◽  
Solvent Accessibility ◽  
Protein Secondary Structure ◽  
Fluorescence Labeling ◽  
T4 Lysozyme

scholarly journals Determination of the secondary structure of group II bulge loops using the fluorescent probe 2-aminopurine

RNA ◽  
2015 ◽  
Vol 21 (5) ◽  
pp. 975-984 ◽  
Author(s):  
Abigael L. Dishler ◽  
Elizabeth L. McMichael ◽  
Martin J. Serra
Keyword(s):  
Secondary Structure ◽  
Fluorescent Probe ◽  
Group Ii

Protein secondary structure and solvent accessibility of proteins in decellularized heart valve scaffolds

2012 ◽  
Vol 1 (1) ◽  
pp. 79-87 ◽  
Author(s):  
Shangping Wang ◽  
Harriëtte Oldenhof ◽  
Andres Hilfiker ◽  
Michael Harder ◽  
Willem F. Wolkers
Keyword(s):  
Secondary Structure ◽  
Heart Valve ◽  
Solvent Accessibility ◽  
Protein Secondary Structure

Determination of protein folding kinetic types using sequence and predicted secondary structure and solvent accessibility

Amino Acids ◽  
2010 ◽  
Vol 42 (1) ◽  
pp. 271-283 ◽  
Author(s):  
Hua Zhang ◽  
Tuo Zhang ◽  
Jianzhao Gao ◽  
Jishou Ruan ◽  
Shiyi Shen ◽  
...  
Keyword(s):  
Protein Folding ◽  
Secondary Structure ◽  
Solvent Accessibility

Protein Secondary Structure Determination (PSSD): A New and Simple Approach

2019 ◽  
Vol 16 (3) ◽  
pp. 246-253
Author(s):  
Anindya Sundar Panja ◽  
Bidyut Bandopadhyay ◽  
Akash Nag ◽  
Smarajit Maiti
Keyword(s):  
Secondary Structure ◽  
Structure Prediction ◽  
Computational Algorithm ◽  
Secondary Structure Prediction ◽  
Protein Secondary Structure ◽  
Structural Features ◽  
Dynamic Algorithm ◽  
Previous Algorithm ◽  
Function Relationship

Background: Our present investigation was conducted to explore the computational algorithm for the protein secondary structure prediction as per the property of evolutionary transient and large number (each 50) of homologous mesophilic-thermophilic proteins. </P><P> Objectives: These mesophilic-thermophilic proteins were used for numerical measurement of helix-sheetcoil and turn tendency for which each amino-acid residue is screened to build up the propensity-table. Methods: In the current study, two different propensity windows have been introduced that allowed predicting the secondary structure of protein more than 80% accuracy. Results: Using this propensity matrix and dynamic algorithm-based programme, a significant and decisive outcome in the determination of protein (both thermophilic and mesophilic) secondary structure was noticed over the previous algorithm based programme. It was demonstrated after comparison with other standard methods including DSSP adopted by PDB with the help of multiple comparisons ANOVA and Dunnett’s t-test. Conclusion: The PSSD is of great importance in the prediction of structural features of any unknown, unresolved proteins. It is also useful in the studies of proteins structure-function relationship.

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