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  • 1
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature biotechnology 22 (2004), S. 1078-1079 
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] To the editor: In their report of the complete genome sequence of the metabolically versatile photosynthetic bacterium Rhodopseudomonas palustris in the January issue, Larimer et al. conclude that “no horizontally transferred islands of DNA are apparent based on anomalous G + C ...
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    The protein journal 15 (1996), S. 59-61 
    ISSN: 1573-4943
    Keywords: DNA ; genetic coding ; protein sequence match
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A DNA double helix consists of two complementary strands antiparallel with each other. One of them is the sense chain, while the other is an antisense chain which does not directly involve the protein-encoding process. The reason that an antisense chain cannot encode for a protein is generally attributed to the lack of certain preconditions such as a promotor and some necessary sequence segments. Suppose it were provided with all these preconditions, could an antisense chain encode for an “antisense protein”? To answer this question, an analysis has been performed based on the existing database. Nine proteins have been found that have a 100% sequence match with the hypothetical antisense proteins derived from the knownEscherichia coli antisense chains.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    The protein journal 14 (1995), S. 251-258 
    ISSN: 1573-4943
    Keywords: Prediction of protein folding types ; amino acid composition ; correlative effect
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A number of methods to predicting the folding type of a protein based on its amino acid composition have been developed during the past few years. In order to perform an objective and fair comparison of different prediction methods, a Monte Carlo simulation method was proposed to calculate the asymptotic limit of the prediction accuracy [Zhang and Chou (1992),Biophys. J. 63, 1523–1529, referred to as simulation method I]. However, simulation method I was based on an oversimplified assumption, i.e., there are no correlations between the compositions of different amino acids. By taking into account such correlations, a new method, referred to as simulation method II, has been proposed to recalculate the objective accuracy of prediction for the least Euclidean distance method [Nakashimaet al. (1986),J. Biochem. 99, 152–162] and the least Minkowski distance method [Chou (1989),Prediction in Protein Structure and the Principles of Protein Conformation, Plenum Press, New York, pp. 549–586], respectively. The results show that the prediction accuracy of the former is still better than that of the latter, as found by simulation method I; however, after incorporating the correlative effect, the objective prediction accuracies become lower for both methods. The reason for this phenomenon is discussed in detail. The simulation method and the idea developed in this paper can be applied to examine any other statistical prediction method, including the computersimulated neural network method.
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    The protein journal 14 (1995), S. 309-326 
    ISSN: 1573-4943
    Keywords: Amino acid composition ; 20D space ; covariance matrix ; Mahalanobis distance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The accuracy of predicting protein folding types can be significantly enhanced by a recently developed algorithm in which the coupling effect among different amino acid components is taken into account [Chou and Zhang (1994)J. Biol. Chem. 269, 22014-22020]. However, in practical calculations using this powerful algorithm, one may sometimes face illconditioned matrices. To overcome such a difficulty, an effective eigenvalue-eigenvector approach is proposed. Furthermore, the new approach has been used to predict a recently constructed set of 76 proteins not included in the training set, and the accuracy of prediction is also much higher than those of other methods.
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    The protein journal 14 (1995), S. 583-593 
    ISSN: 1573-4943
    Keywords: α proteins ; β proteins ; α + β proteins ; α/β proteins ; amino acid composition ; cross-validation ; leaving-one-out test
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract In the development of methodology for statistical prediction of protein folding types, how to test the predicted results is a crucial problem. In addition to the resubstitution test in which the folding type of each protein from a training set is predicted based on the rules derived from the same set, cross-validation tests are needed. Among them, the single-testset method seems to be least reliable due to the arbitrariness in selecting the test set. Although the leaving-one-out (or jackknife) test is more objective and hence more reliable, it may cause a severe information loss by leaving a protein in turn out of the training set when its size is not large enough. In order to overcome the above drawback, a seed-propagated sampling approach is proposed that can be used to generate any number of simulated proteins with a desired type based on a given training set database. There is no need to make any predetermined assumption about the statistical distribution function of the amino acid frequencies. Combined with the existing cross-validation methods, the new technique may provide a more objective estimation for various protein-folding-type prediction methods.
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    The protein journal 19 (2000), S. 269-275 
    ISSN: 1573-4943
    Keywords: Membrane protein ; type of membrane protein ; amino acid composition ; autocorrelation function ; hydrophobic index
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A new algorithm to predict the types of membrane proteins is proposed. Besides the amino acid composition of the query protein, the information within the amino acid sequence is taken into account. A formulation of the autocorrelation functions based on the hydrophobicity index of the 20 amino acids is adopted. The overall predictive accuracy is remarkably increased for the database of 2054 membrane proteins studied here. An improvement of about 13% in the resubstitution test and 8% in the jackknife test is achieved compared with those of algorithms based merely on the amino acid composition. Consequently, overall predictive accuracy is as high as 94% and 82% for the resubstitution and jackknife tests, respectively, for the prediction of the five types. Since the proposed algorithm is based on more parameters than those in the amino acid composition approach, the predictive accuracy would be further increased for a larger and more class-balanced database. The present algorithm should be useful in the determination of the types and functions of new membrane proteins. The computer program is available on request.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    The protein journal 12 (1993), S. 169-178 
    ISSN: 1573-4943
    Keywords: Alla ; all β ; a+β ; a/β ; Amino acid composition ; 20D space ; correlation angle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A new method is proposed for predicting the folding type of a protein according to its amino acid composition based on the following physical picture: (1) a protein is characterized as a vector of 20-dimensional space, in which its 20 components are defined by the compositions of its 20 amino acids; and (2) the similarity of two proteins is proportional to the mutual projection of their characterized vectors, and hence inversely proportional to the size of their correlation angle. Thus, the prediction is performed by calculating the correlation angles of the vector for the predicted protein with a set of standard vectors representing the norms of four protein folding types (i.e., alla, all β,a+β, anda/β). In comparison with the existing methods, the new method has the merits of yielding a higher rate of correct prediction, displaying a more intuitive physical picture, and being convenient in application. For instance, in predicting the 64 proteins in the development set based on which the standard vectors are derived, the average accuracy rate is 83.6%, which is higher than that obtained for the same set of proteins by any of the existing methods. The average accuracy predicted for an independent set of 35 proteins of known X-ray structure is 91.4%, which is significantly higher than any of the reported accuracies so far, implying that the new method is of great value in practical application. All of these have demonstrated that the new method as proposed in this paper is characterized by an improved feature in both self-consistency and extrapolating-effectiveness.
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    The protein journal 12 (1993), S. 329-335 
    ISSN: 1573-4943
    Keywords: Codon position ; DNA bases ; characteristic inequality ; mapping point
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The frequencies of bases A (adenine), C (cytosine), G (guanine), and T (thymine) occurring in codon positioni, denoted bya i ,c i ,g i , andt i , respectively (i=1, 2, 3), have been calculated and diagrammatized for the 1490 human proteins in the codon usage table for primate genes compiled recently. Based on the characteristic graphs thus obtained, an overall picture of codon base distribution has been provided, and the relevant biological implication discussed. For the first codon position, it is shown in most cases that G is the most dominant base, and that the relationshipg 1〉a 1〉c 1〉t 1 generally holds true. For the second codon position, A is generally the most dominant base and G is the one with the least occurrence frequently, with the relationship ofa 2〉t 2〉c 2〉g 2. As to the third codon position, the values ofg 3+c 3 vary from 0.27 to 1, roughly keeping the relationship ofc 3〉g 3〉a 3=t 3 for the majority of cases. Interestingly, if the average frequencies for bases A, C, G, and T are defined as $$\bar a = {{(a_1 + a_2 + a_3 )} \mathord{\left/ {\vphantom {{(a_1 + a_2 + a_3 )} 3}} \right. \kern-\nulldelimiterspace} 3}, \bar c = {{(c_1 + c_2 + c_3 )} \mathord{\left/ {\vphantom {{(c_1 + c_2 + c_3 )} 3}} \right. \kern-\nulldelimiterspace} 3}, \bar g = {{(g_1 + g_2 + g_3 )} \mathord{\left/ {\vphantom {{(g_1 + g_2 + g_3 )} 3}} \right. \kern-\nulldelimiterspace} 3} and \bar t = {{(t1 + t2 + t3)} \mathord{\left/ {\vphantom {{(t1 + t2 + t3)} 3}} \right. \kern-\nulldelimiterspace} 3}$$ , respectively, we find that $$\bar a^2 + \bar c^2 + \bar g^2 + \bar t^2〈 \tfrac{1}{3}$$ is valid almost without exception. Such a characteristic inequality might reflect some inherent rule of codon usage, although its biological implications is unclear. An important advantage by introducing graphic methods is to make it possible to catch essential features from a huge amount of data by a direct and intuitive examination. The method used here allows one to see means and variances, and also spot outliers. This is particularly useful for finding and classifying similarity patterns and relationships in data sets of long sequences, such as DNA coding sequences. The current method also holds a great potential for the study of molecular evolution from the viewpoint of genetic code whose data have been accumulated rapidly and are to continue growth at a much faster pace.
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    The protein journal 17 (1998), S. 261-272 
    ISSN: 1573-4943
    Keywords: Protein structure prediction ; α-helix content ; β-strand content ; structural classes ; resubstitution analysis ; jackknife analysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The prediction of the secondary structural contents (those of α-helix and β-strand) of a globular protein is of great use in the prediction of protein structure. In this paper, a new prediction algorithm has been proposed based on Chou's database [Chou (1995), Proteins 21, 319–344]. The new algorithm is an improved multiple linear regression method, taking into account the nonlinear and coupling terms of the frequencies of different amino acids and the length of the protein. The prediction is also based on the structural classes of proteins, but instead of four classes, only three classes are considered, the α class, β class, and the mixed α+β and α/β class or simply the αβ class. Thus the ambiguity that usually occurs between α+β proteins and α/β proteins is eliminated. A resubstitution examination for the algorithm shows that the average absolute errors are 0.040 and 0.035 for the prediction of α-helix content and β-strand content, respectively. An examination of cross-validation, the jackknife analysis, shows that the average absolute errors are 0.051 and 0.045 for the prediction of α-helix content and β-strand content, respectively. Both examinations indicate the self-consistency and the extrapolating effectiveness of the new algorithm. Compared with other methods, ours has the merits of simplicity and convenience for use, as well as high prediction accuracy. By incorporating the prediction of the structural classes, the only input of our method is the amino acid composition and the length of the protein to be predicted.
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    The protein journal 15 (1996), S. 721-729 
    ISSN: 1573-4943
    Keywords: Vector projection method ; protein ; supersecondary motif ; prediction ; cutoff
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract For the 11 types of most frequently occurring supersecondary motifs, we used a new method—the vector projection method—to predict a protein's supersecondary structure. In a training set of peptides and a test set of peptides we obtained a satisfactory result, with a prediction accuracy of about 90%. The high prediction accuracy indicates that this method is reasonable for predicting the folding motifs of proteins. This work provides insight into the problem of predicting a protein's local structure accurately, and is of particular value in protein modeling, prediction, and molecule design.
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