Literature DB >> 21629590

Mean-squared atomic displacements in hydrated lysozyme, native and denatured.

Eugene Mamontov, Hugh O'Neill, Qiu Zhang.   

Abstract

We use elastic neutron scattering to demonstrate that a sharp increase in the mean-squared atomic displacements, commonly observed in hydrated proteins above 200 K and often referred to as the dynamical transition, is present in the hydrated state of both native and denatured lysozyme. A direct comparison of the native and denatured protein thus confirms that the presence of the transition in the mean-squared atomic displacements is not specific to biologically functional molecules.

Keywords:  Biomolecules; Dynamics; Neutron scattering

Year:  2010        PMID: 21629590      PMCID: PMC2868976          DOI: 10.1007/s10867-009-9184-6

Source DB:  PubMed          Journal:  J Biol Phys        ISSN: 0092-0606            Impact factor:   1.365


  42 in total

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Journal:  Phys Rev E Stat Nonlin Soft Matter Phys       Date:  2009-05-22

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Authors:  R M Daniel; J C Smith; M Ferrand; S Héry; R Dunn; J L Finney
Journal:  Biophys J       Date:  1998-11       Impact factor: 4.033

8.  Estimation of globular protein secondary structure from circular dichroism.

Authors:  S W Provencher; J Glöckner
Journal:  Biochemistry       Date:  1981-01-06       Impact factor: 3.162

9.  Protein dynamics. Mössbauer spectroscopy on deoxymyoglobin crystals.

Authors:  F Parak; E W Knapp; D Kucheida
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Journal:  J Phys Chem B       Date:  2009-01-08       Impact factor: 2.991

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2.  Mechanistic insight into the structure and dynamics of entangled and hydrated λ-phage DNA.

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3.  Dynamics of lysozyme and its hydration water under an electric field.

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  3 in total

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