(Q47631461)

4 February 2018

title

Intrinsic phi, psi propensities of amino acids, derived from the coil regions of known structures (English)

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author

Janet Thornton

series ordinal

3

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author name string

Swindells MB

series ordinal

1

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MacArthur MW

series ordinal

2

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publication date

1 July 1995

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4 February 2018

Nature structural biology

published in

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4 February 2018

volume

2

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4 February 2018

issue

7

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4 February 2018

page(s)

596-603

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4 February 2018

Relative helix-forming tendencies of nonpolar amino acids

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Measurement of the β-sheet-forming propensities of amino acids

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Context is a major determinant of β-sheet propensity

21 January 2018

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A thermodynamic scale for the beta-sheet forming tendencies of the amino acids.

21 January 2018

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Structural basis of amino acid alpha helix propensity

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Influence of the local amino acid sequence upon the zones of the torsional angles phi and psi adopted by residues in proteins

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Elucidating the folding problem of helical peptides using empirical parameters

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Conformational analysis of the 20 naturally occurring amino acid residues using ECEPP

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A theory of protein molecule self-organization. IV. Helical and irregular local structures of unfolded protein chains

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Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: comparison with experimental scales.

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Conformation of amino acid side-chains in proteins

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Conformational analysis of the backbone-dependent rotamer preferences of protein sidechains

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Primary structure effects on peptide group hydrogen exchange

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Hydrogen bond strength and beta-sheet propensities: the role of a side chain blocking effect

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Beta-turns and their distortions: a proposed new nomenclature

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Identifiers

DOI

10.1038/NSB0795-596

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4 February 2018

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4 February 2018