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Amino acid size, charge, hydropathy indices and matrices for protein structure analysis.

Biro JC.

Theor Biol Med Model. 2006 Mar 22;3:15.PMID: 16551371 [PubMed - indexed for MEDLINE]Related articlesFree article

Indications that "codon boundaries" are physico-chemically defined and that protein-folding information is contained in the redundant exon bases.

Biro JC.

Theor Biol Med Model. 2006 Aug 7;3:28.PMID: 16893453 [PubMed - indexed for MEDLINE]Related articlesFree article

Direct correlation between proteins' folding rates and their amino acid compositions: an ab initio folding rate prediction.

Ma BG, Guo JX, Zhang HY.

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A novel intra-molecular protein-protein interaction code based on partial complementary coding of co-locating amino acids.

Biro JC.

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Classification of amino acids based on statistical results of known structures and cooperativity of protein folding.

Chen H, Zhou X, Ou-Yang ZC.

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Nucleic acid chaperons: a theory of an RNA-assisted protein folding.

Biro JC.

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Thermodynamic propensities of amino acids in the native state ensemble: implications for fold recognition.

Wrabl JO, Larson SA, Hilser VJ.

Protein Sci. 2001 May;10(5):1032-45.PMID: 11316884 [PubMed - indexed for MEDLINE]Related articlesFree article

Use of variable selection in modeling the secondary structural content of proteins from their composition of amino acid residues.

Pilizota T, Lucić B, Trinajstić N.

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The unfoldomics decade: an update on intrinsically disordered proteins.

Dunker AK, Oldfield CJ, Meng J, Romero P, Yang JY, Chen JW, Vacic V, Obradovic Z, Uversky VN.

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A two-stage approach for improved prediction of residue contact maps.

Vullo A, Walsh I, Pollastri G.

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SeqX: a tool to detect, analyze and visualize residue co-locations in protein and nucleic acid structures.

Biro JC, Fördös G.

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Predicting residue-wise contact orders in proteins by support vector regression.

Song J, Burrage K.

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Analysis of amino acid indices and mutation matrices for sequence comparison and structure prediction of proteins.

Tomii K, Kanehisa M.

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Is it possible to predict the average surface hydrophobicity of a protein using only its amino acid composition?

Salgado JC, Rapaport I, Asenjo JA.

J Chromatogr A. 2005 May 20;1075(1-2):133-43.PMID: 15981340 [PubMed - indexed for MEDLINE]Related articles

Correlation between sequence hydrophobicity and surface-exposure pattern of database proteins.

Moelbert S, Emberly E, Tang C.

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Electronic properties of the amino acid side chains contribute to the structural preferences in protein folding.

Dwyer DS.

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Database-derived potentials dependent on protein size for in silico folding and design.

Dehouck Y, Gilis D, Rooman M.

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Toward high-resolution de novo structure prediction for small proteins.

Bradley P, Misura KM, Baker D.

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Effects of external interactions on protein sequence-structure relations of beta-trefoil fold.

Li M, Huang Y, Xiao Y.

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Accurate prediction for atomic-level protein design and its application in diversifying the near-optimal sequence space.

Fromer M, Yanover C.

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