Literature DB >> 6876837

The dependence of the Chou-Fasman parameters on amino acid side chain structure.

M Charton, B I Charton.   

Abstract

The Chou-Fasman conformational parameters, P, for amino acid residues in proteins are shown to be a linear function of intermolecular force and steric parameters. For alpha- helix, coil and turn parameters, steric effects are predominant; whereas for beta-sheet parameters, intramolecular forces are predominant. Turn and coil parameters show little or no difference in their dependence which is different from that of alpha-helix and in some ways almost reciprocal. Factors which increase the probability of finding an amino acid residue in an alpha-helix usually decrease the probability of finding it in coil or turn. Values of P were calculated for several of the less common amino acids.

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Year:  1983        PMID: 6876837     DOI: 10.1016/0022-5193(83)90265-5

Source DB:  PubMed          Journal:  J Theor Biol        ISSN: 0022-5193            Impact factor:   2.691


  16 in total

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2.  Electron capture dissociation product ion abundances at the X amino acid in RAAAA-X-AAAAK peptides correlate with amino acid polarity and radical stability.

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8.  Exploring the sequence features determining amyloidosis in human antibody light chains.

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Review 9.  Some methods of obtaining quantitative structure-activity relationships for quantities of environmental interest.

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Journal:  Environ Health Perspect       Date:  1985-09       Impact factor: 9.031

10.  Nature of protein family signatures: insights from singular value analysis of position-specific scoring matrices.

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Journal:  PLoS One       Date:  2008-04-09       Impact factor: 3.240

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