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Predicting structures for genome proteins
Current Opinion in Structural Biology, 1999Assigning three-dimensional protein folds to genome sequences is essential to understanding protein function. Although experimental three-dimensional structures are currently available for only a very small fraction of these sequences, computational fold assignment is able to assign folds to 20-30% of the sequences in various genomes.
D, Fischer, D, Eisenberg
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Predicting Protein Structures Accurately
Science, 2004In their Research Article “Design of a novel globular protein fold with atomic-level accuracy,” B. Kuhlman et al. describe an extremely successful attempt to design a new protein (Top7) that folds to a predefined structure (21 Nov, p. [1364][1]).
Marcin, von Grotthuss +3 more
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Biochimie, 1990
Current methods developed for predicting protein structure are reviewed. The most widely used algorithms of Chou and Fasman and Garnier et al for predicting secondary structure are compared to the most recent ones including sequence similarity methods, neural network, pattern recognition or joint prediction methods.
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Current methods developed for predicting protein structure are reviewed. The most widely used algorithms of Chou and Fasman and Garnier et al for predicting secondary structure are compared to the most recent ones including sequence similarity methods, neural network, pattern recognition or joint prediction methods.
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Approaches to prediction of protein structure
2011 9th IEEE/ACS International Conference on Computer Systems and Applications (AICCSA), 2011Protein structure prediction (PSP) is one of the most important and challenging problems in bioinformatics today. This is due to the fact that the biological function of the protein is determined by its structure. While there is a gap between the number of known protein sequences and the number of known structures, protein structure prediction aims at ...
Walaa Fathy Ahmed, Walid E. Gomaa
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Toolbox for Protein Structure Prediction
2016Protein tertiary structure prediction algorithms aim to predict, from amino acid sequence, the tertiary structure of a protein. In silico protein structure prediction methods have become extremely important, as in vitro-based structural elucidation is unable to keep pace with the current growth of sequence databases due to high-throughput next ...
Roche, Daniel Barry +1 more
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Protein Tertiary Structure Prediction
Current Protocols in Protein Science, 2000AbstractThis unit addresses how to predict the tertiary structure of a protein from its amino acid sequence using computational methods. Three types of prediction methods‐‐homology modeling, fold recognition, and ab initio prediction‐‐are introduced.
D, Xu, Y, Xu
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Prediction of Protein Structural Classes
Critical Reviews in Biochemistry and Molecular Biology, 1995A protein is usually classified into one of the following five structural classes: alpha, beta, alpha + beta, alpha/beta, and zeta (irregular). The structural class of a protein is correlated with its amino acid composition. However, given the amino acid composition of a protein, how may one predict its structural class?
K C, Chou, C T, Zhang
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Agent-based protein structure prediction [PDF]
Multiagent and Grid Systems, 2007 A protein is identified by a finite sequence of amino acids, each of them chosen from a set of 20 elements. The Protein Structure Prediction Problem is the problem of predicting the 3D native conformation of a protein, when its sequence of amino acids is known.
Luca Bortolussi +2 more
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Structure prediction of the RPE65 protein
Journal of Theoretical Biology, 2006The RPE65 protein is located in the retinal pigment epithelial cells and plays an important role in the visual cycle. Although numerous experimental results demonstrate that it participates in the visual cycle, its detailed structure and function are not clear yet because of difficulties in isolation and crystallization.
Hao, Guo +2 more
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Structure Predictions for Membrane Proteins
1987To predict the folding of membrane proteins one usually starts by identifying stretches of ∿ 20 hydrophobic residues on the amino acid sequence. Folded in an α-helix, these residues would span the hydrocarbon core of the lipid bilayer. Following Kyte and Doolittle (1982), a hydrophobicity index h is attributed to each amino acid residue and the mean ...
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