Sidechain interactions in parallel beta sheets: the energetics of cross-strand pairings (Q73211830)

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2 November 2019

title

Sidechain interactions in parallel beta sheets: the energetics of cross-strand pairings (English)

1 reference

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2 November 2019

author name string

J S Merkel

series ordinal

1

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2 November 2019

J M Sturtevant

series ordinal

2

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2 November 2019

L Regan

series ordinal

3

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2 November 2019

publication date

1 November 1999

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2 November 2019

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2 November 2019

volume

7

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2 November 2019

page(s)

1333-1343

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2 November 2019

issue

11

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Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins

2 November 2019

cites work

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Intrinsic beta-sheet propensities result from van der Waals interactions between side chains and the local backbone

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Bayesian statistical analysis of protein side-chain rotamer preferences

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The β structure: Inter-strand correlations

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Specific recognition in the tertiary structure of beta-sheets of proteins

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An analysis of side chain interactions and pair correlations within antiparallel beta-sheets: the differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs.

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Guidelines for protein design: the energetics of beta sheet side chain interactions

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Electrostatic Interactions across a β-Sheet†

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A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G

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Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR

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Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques

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Identifiers

DOI

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2 November 2019

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