| J. Kyte and R. F. Doolittle. A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology, 157:105-132, 1982. |
.... as indicated by comparisons of Kyte and Doolittle hydrophobicity scores of each residue [137] A strong 156 correlation has been shown between hydrophobic clusters and protein binding sites [136] In addition, using hydrophobicity as a guide, sites of protein interaction have been identified [138, 139]. The similar values and patterns of the hydrophobic peaks within residues 34 67 and 287 315, as determined by the Kyte and Doolittle measurments, may be indicative of some similarity in secondary structure. In addition the hydropathy profiles are consistent with IFNAR2(287 315) recognition of ....
Kyte J., Doolittle, R.F. A Simple Method for Displaying the Hydropathic Character of a Protein. J Mol Biol. 1982. 157:105132.
....of 20 amino acids. Using the signal peptides as positive examples, and all others as negative examples, we searched for the best pair k# with maximum length of 10 using PMMs. To limit the alphabet size, we classify the amino acids into 3 classes 0, 1, 2 , according to the hydropathy index [48]. The most hydrophobic amino acids M, C, F, L, V, I (hydropathy 0.0) are converted to 0, P,Y,W,S,T,G ( 3.0 hydropathy 0.0 ) to 1, and R, K, D, E, N, Q, H (hydropathy 3.0 ) to 2. We obtained the pair #0#00#00000#, 26#, which occurs in 213 269 = 79.2 of the sequences with ....
J. Kyte and R. Doolittle. A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology, 157:105--132, 1982.
....For each family of sequences with marked regions of a specific type, some programs have been developed for predicting such marked regions on unknown sequences. For example, ChouFasman s method [1] is well known for predicting the ff helices and fi sheets. The hydropathy plot of Kyte and Doolittle [2] predicts transmembrane domains on amino acid sequences of membrane proteins. For coding region prediction in DNA sequences, GRAIL [5] and GRAIL II [6] are known as successful systems. Instead of designing a prediction program individually for a specific family of sequences, we are developing a ....
J. Kyte and R. F. Doolittle, "A Simple Method for Displaying the Hydropathic Character of a Protein," J. Mol. Biol.,Vol. 157, pp. 105--132, 1982.
....sequences for hits. 2. 2 QFC C4.5 In the QFC algorithm [14] the physical chemical properties of the amino acids in the molecules are statically characterized using various indices and standard measurements, such as GES hydropathy index [8, 11] solubility [3] polarity, pI, Kyte Doolittle index [15], # helix index [6] and molecular weight. A protein sequence is described by a set of variables x 1 through x n , and for each x i , there is a value x ij for the ith amino acid index value at the jth position. Thus x i1 through x ik constitutes a profile of the protein in terms of the ith ....
J. Kyte and R. F. Doolittle. A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology, 157:105--132, 1982.
.... Solvent accessibility consists of 75 MCV constraints on residues with extreme DSSP ACC values (same as the exact large set of MCV constraints For the purpose of discussion in this chapter, hydrophobic residues are defined to be those with positive values on the Kyte Doolittle hydrophobicity scale [56]. 43 described in Section 4.2) Hydrophobic packing consists of two moment matching constraints we have just discussed to separate hydrophobic and hydrophilic residues. Compute a structure using the baseline data augmented with secondary structure information. We use a manually constructed ....
J. Kyte and R. F. Doolittle, "A Simple Method for Displaying the Hydropathic Character of a Protein", J. Mol. Biol., vol. 157, no. 1, pp. 105-132, 1982.
....In this work, twotypes of attributes are used: compositional and numerical. A compositional attribute is the number of a specified amino acid, or the number of a set of amino acids, divided by the length of the window. A numerical attribute is value of some amino acid parameter, such as hydropathy [10] or flexibility index [18] averaged over the amino acids in a given window. Here wehave used windows of 21 amino acids. This value was selected in previous studies [12] as a reasonable compromise between the increased noisiness of smaller windows and the lower resolution of larger ones. A ....
....( correlation) order promoting ( correlation) or complex. Sets of amino acids were chosen as attributes to determine the relationships between disorder order and various classes of amino acids such as aromatic, polar, nonpolar, etc. Finally, two numerical attributes, hydropathy [10] and flexibility index [18] were included because these attributes were selected in our previous investigations as being important for predicting disorder [12] 4 Discussion 4.1 Prior Neural Network Prediction of Order and Disorder Upon noticing that many proteins contain essential, functional ....
[Article contains additional citation context not shown here]
Kyte, J., Doolittle, R.F., A simple method for displaying the hydropathic character of a protein, J. Mol. Biol., 157(1):105--132, 1982.
....this work, two types of attributes are used: compositional and numerical. A compositional attribute is the number of a specified amino acid, or the number of a set of amino acids, divided by the length of the window. A numerical attribute is value of some amino acid parameter, such as hydropathy [10] or flexibility index [18] averaged over the amino acids in a given window. Here we have used windows of 21 amino acids. This value was selected in previous studies [12] as a reasonable compromise between the increased noisiness of smaller windows and the lower resolution of larger ones. A ....
....( correlation) order promoting ( correlation) or complex. Sets of amino acids were chosen as attributes to determine the relationships between disorder order and various classes of amino acids such as aromatic, polar, nonpolar, etc. Finally, two numerical attributes, hydropathy [10] and flexibility index [18] were included because these attributes were selected in our previous investigations as being important for predicting disorder [12] 4 Discussion 4.1 Prior Neural Network Prediction of Order and Disorder Upon noticing that many proteins contain essential, functional ....
[Article contains additional citation context not shown here]
Kyte, J., Doolittle, R.F., A simple method for displaying the hydropathic character of a protein, J. Mol. Biol., 157(1):105--132, 1982.
....Sequence attributes are numerical values calculated from an amino acid sequence over a specified window [4] For these studies, 24 attributes provided the initial pool, the first 20 of which are the compositions of the 20 amino acids within the specified sequence windows. The last 4 are hydropathy [33], flexibility index [50] helix amphipathic moment [21] and sheet amphipathic moment [22] The NMR and X ray disordered datasets were each matched with an equal number of ordered amino acids taken from the NRL 3 [40] which is a subset of PDB containing only ordered structures. A feed forward ....
Kyte, J., Doolittle, R.F., A simple method for displaying the hydropathic character of a protein, J. Mol. Biol., 157(1):105--132, 1982.
....19 residues long, around each position. In transmembrane helices, which are present in many neural proteins, the hydropathy index is high for a number of consecutive positions in the sequence. The grand average of hydropathicity is the average value of the hydropathy index at each position. See [19] for more details. 5) Instability index. Certain dipeptides occur more frequently in unstable proteins than in stable ones. The inventors of this index have assigned a weight value of instability to each of the 400 different dipeptides [15] The values obtained for a whole protein tend to fall ....
Kyte, J. and Doolittle, R.F., "A simple method for displaying the hydropathic character of a protein", J Mol Biol 157, (1982) 105-32
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J. Kyte and R. F. Doolittle. A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology, 157:105-132, 1982.
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Kyte, J., and Doolittle, R.F. (1982). A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105--132.
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Kyte,J. and Doolittle,R.F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol., 157, 105--132.
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Kyte, J. & Doolittle, R. F. (1982). A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105 -- 132.
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Kyte, J. and Doolittle, R.F., A simple method for displaying the hydropathic character of a protein, J. Mol. Biol., 157:105--132, 1982.
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Kyte, J. and Doolittle, R.F., A simple method for displaying the hydropathic character of a protein, J. Mol. Biol., 157:105--132, 1982.
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J. Kyte and R.F. Doolittle, "A simple method for displaying the hydropathic character of a protein", J. Mol. Biol., 157, 105 (1982).
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Kyte, J. and Doolittle, R.F., A simple method for displaying the hydropathic character of a protein, J. Mol. Biol., 157:105--132, 1982.
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Kyte, J., Doolittle, R. A simple method for displaying the hydropathic character of proteins. Journal of Molecular Biology, vol. 157, pp. 105-132, 1982.
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J. Kyte and R. F. Doolittle. A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology, 157:105--132, 1982.
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Kyte, J., Doolittle, R.F.: A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 (1982) 105--132
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J. Kyte and R. Doolittle. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol., 157:105--132, 1982.
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J. Kyte and R.F. Doolitle, A simple method for displaying the hydropathic character of proteins. J. Mol. Biol. 157:105-132, 1982.
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Kyte, J. & Doolittle, R. F. (1982). A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157,105--132.
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Kyte J and Doolittle R. A simple method for displaying the hydropathic character of a protein. J Mol Biol 1982, 157: 105--132.
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Kyte J, Doolittle RF. A simple method for displaying the hydropathic character of proteins. J Mol Biol. 1982;157:105-132.
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