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The origin of protein sidechain order parameter distributions

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The origin of protein sidechain order parameter distributions (English)

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3

Martin Karplus

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Robert B. Best

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Robert B Best

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1

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Jane Clarke

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2

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English

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publication date

30 June 2004

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published in

Journal of the American Chemical Society

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volume

126

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page(s)

7734-5

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issue

25

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Comparison of methyl rotation axis order parameters derived from model-free analyses of (2)H and (13)C longitudinal and transverse relaxation rates measured in the same protein sample

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Protein hydration elucidated by molecular dynamics simulation

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Backbone and methyl dynamics of the regulatory domain of troponin C: anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity.

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Dynamics and entropy of a calmodulin-peptide complex studied by NMR and molecular dynamics

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Backbone and side chain dynamics of uncomplexed human adipocyte and muscle fatty acid-binding proteins.

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Correlation between 2H NMR side-chain order parameters and sequence conservation in globular proteins

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Side-chain dynamics of the SAP SH2 domain correlate with a binding hot spot and a region with conformational plasticity

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The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site

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Methyl side-chain dynamics in proteins using selective enrichment with a single isotopomer

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The origin of protein sidechain order parameter distributions

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