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1 l-established heuristics based on charge and hydropathy.
2 has led to the use of proxies, most notably, hydropathy.
3 will readily compare data other than protein hydropathy.
4 ase search and pairwise alignment of protein hydropathy.
5 with residues of different charge, size and hydropathy.
6 ition and not molecular volume, polarity, or hydropathy.
11 12 transmembrane helices (TMHs), confirming hydropathy analyses of the majority of (prokaryotic and
14 8% predicted from the amino acid sequence by hydropathy analysis (12 membrane-spanning helices) for t
24 of right-side-out vesicles with trypsin and hydropathy analysis of the predicted amino acid sequence
31 ructure prediction of NuoM using the Toppred hydropathy analysis showed that the Q-binding peptide ov
37 DTT on membranes were obtained using a novel hydropathy analysis that considers the relative free ene
38 d sixth of these are short, not predicted by hydropathy analysis, do not insert independently into mi
51 take (-0.92), a moderate correlation between hydropathy and Pf (0.73), and a minimal correlation betw
54 let change-point performs well for smoothing hydropathy and transmembrane profiles generated using di
55 f glucose uptake and Pf (-0.93), and between hydropathy and uptake (-0.92), a moderate correlation be
56 50 to residues of different size, charge and hydropathy, and examined the effects on adenine nucleoti
57 fields, such as electrostatic potential and hydropathy, are smoothed to further reduce visual comple
59 ane domains was previously proposed based on hydropathy, charge dispersion, and homology to other tra
61 a for predicting intrinsic disorder, such as hydropathy, combined with significant net charge, the ve
62 perimental assignments, the empirical charge/hydropathy correlation for the prediction of natively un
65 These methods are based on the net charge-hydropathy distribution and disorder prediction score di
69 ures, isoelectric point and grand average of hydropathy (GRAVY) values of the 7 most abundant protein
70 eractions but differ in the grand average of hydropathy (GRAVY), solubility, and hydrophobic contacts
71 ly significant differences in Kyte-Doolittle hydropathy in the signal peptide, C2, V3, and C3 regions
73 ts into a single plot, information about the hydropathy index, Van der Waals volume, chemical propert
75 isoelectric point, sequence length, average hydropathy, low complexity regions (SEG), and combinatio
76 different classification methods, the charge-hydropathy measure and the cumulative distribution funct
77 ne in a manner consistent with the predicted hydropathy model for Na+- and Cl--dependent transporters
78 with the homology model than an alternative hydropathy model of VAChT that likely locates E309 far f
80 s with exceptionally high net charge and low hydropathy near the cytoplasmic end of the central chann
81 L containing human apos is due to the higher hydropathy of human apo A-I, particularly its C-terminus
82 ence descriptors: the number of domains, the hydropathy of terminal domains, and the patchiness (dens
83 esults suggest that the molecular volume and hydropathy of the amino acid at position 288 in TM3 regu
84 ns revealed a strong correlation between the hydropathy of the amino acid at this position and the GA
85 orrelation between DW dynamics and the local hydropathy of the CheY protein surface, empirically dete
91 ribes the use of the concept of inversion of hydropathy patterns to the de novo design of peptides ta
92 distribution function (CDF) analysis, charge-hydropathy plot (CH plot) analysis, and alpha-helical mo
97 id sequence of mdr1b P-glycoprotein, and its hydropathy plot analysis, our data indicated that the 3'
98 ere based primarily on the somewhat atypical hydropathy plot for MerF and related transport proteins.
100 IDPs and folded proteins in Uversky's charge-hydropathy plot may behave as "marginal IDPs" and sensit
101 e for genomic analysis is the ability of the hydropathy plot method to distinguish membrane from solu
102 QPs3 is a very hydrophobic protein; the hydropathy plot of the amino acid sequence reveals three
103 ural model of SdhC, constructed based on the hydropathy plot of the deduced amino acid sequence of th
107 ifs, transmembrane regions, signal peptides, hydropathy plots and profile hits using several popular
109 50 1A2c); these all show slightly dissimilar hydropathy plots compared to the MALLLAVFL... sequence.
111 e Ytp1 protein appears by computer analysis (hydropathy plots in conjunction with the combined predic
115 nty of TM helix prediction by sliding-window hydropathy plots of membrane protein (MP) amino acid seq
118 nsmembrane segments seen in n-block-averaged hydropathy plots while leaving the remaining hydrophobic
119 V) is considerably smaller than predicted by hydropathy plots, extending only from about Val132 to Ph
120 n to be more accurate than the use of charge hydropathy plots, which are frequently used to predict d
123 In silico analysis (homology searching, hydropathy plotting, and codon usage assessment) strongl
124 ured segments in transmembrane proteins were hydropathy, polarity, and flexibility, and used the resu
127 which shares a similar transmembrane domain hydropathy profile as well as transporter-specific amino
130 ochondrial membrane is proposed based on the hydropathy profile of the amino acid sequence, on the pr
132 hu1 cleavability by PI-PLC and its predicted hydropathy profile strongly suggested that Shu1 is a gly
135 emical properties, such as molecular weight, hydropathy profile, and predicted secondary structure, a
136 This cDNA encodes 354 amino acids that, by hydropathy profile, could form seven transmembrane domai
137 nt containing an H-domain which, in terms of hydropathy profile, is identical to that of a delta pH-d
141 been proposed based on the similarity of the hydropathy profiles and the homology of sequences betwee
143 de datasets, including amino acid sequences, hydropathy profiles, gene expression data and known prot
146 dings are consistent with a central role for hydropathy rather than size at position 310 of this muta
147 find that an experiment-based whole-residue hydropathy scale (WW scale), which includes the backbone
150 that thermodynamic analyses based on current hydropathy scales do not account for the significant and
151 as the commonly used surface area models or hydropathy scales for characterizing biomolecular hydrop
152 Experiment-based whole-residue free-energy (hydropathy) scales for amino acids in unfolded peptides,
153 phobic interface allowed benchmarking of the hydropathy sequence analysis, an important structural ge
154 odes a protein with significant sequence and hydropathy similarity to mammalian acyloxyacyl hydrolase
157 that significant variations in polarity and hydropathy values among the Akt isoforms in both the ple
158 including one that differed in polarity and hydropathy, were located in the peak signatures and defi