MersV1, PubMed, Corpus, bibRecord, 002291

Structure and interaction in protein solutions as studied by small-angle neutron scattering.

Identifieur interne : 002291 ( PubMed/Corpus ); précédent : 002290; suivant : 002292

Structure and interaction in protein solutions as studied by small-angle neutron scattering.

Auteurs : S. Chodankar ; V K Aswal

Source :

Physical review. E, Statistical, nonlinear, and soft matter physics [ 1539-3755 ] ; 2005.

RBID : pubmed:16383444

English descriptors

KwdEn :
- Computer Simulation, Crystallization (methods), Models, Chemical, Models, Molecular, Multiprotein Complexes (chemistry), Multiprotein Complexes (ultrastructure), Muramidase (chemistry), Muramidase (ultrastructure), Neutron Diffraction (methods), Protein Binding, Protein Conformation, Salts (chemistry), Solutions.
MESH :
- chemical , chemistry : Multiprotein Complexes, Muramidase, Salts.
- methods : Crystallization, Neutron Diffraction.
- chemical , ultrastructure : Multiprotein Complexes, Muramidase.
- Computer Simulation, Models, Chemical, Models, Molecular, Protein Binding, Protein Conformation, Solutions.

Abstract

Small-angle neutron scattering (SANS) measurements have been performed to compare the effect of the salts KF, KCl, and KBr on crystallization in aqueous solution of lysozyme protein. It is found that the propensity of the salt to crystallize protein follows the Hoffmeister series (KF
DOI: 10.1103/PhysRevE.72.041931
PubMed: 16383444

Links to Exploration step

pubmed:16383444

Le document en format XML

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<affiliation><nlm:affiliation>Solid State Physics Division, Bhabha Atomic Research Centre, Mumbai-400 085, India.</nlm:affiliation>
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<author><name sortKey="Aswal, V K" sort="Aswal, V K" uniqKey="Aswal V" first="V K" last="Aswal">V K Aswal</name>
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<term>Muramidase (chemistry)</term>
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<term>Neutron Diffraction (methods)</term>
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<term>Muramidase</term>
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<keywords scheme="MESH" xml:lang="en"><term>Computer Simulation</term>
<term>Models, Chemical</term>
<term>Models, Molecular</term>
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<front><div type="abstract" xml:lang="en">Small-angle neutron scattering (SANS) measurements have been performed to compare the effect of the salts KF, KCl, and KBr on crystallization in aqueous solution of lysozyme protein. It is found that the propensity of the salt to crystallize protein follows the Hoffmeister series (KF</div>
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<Month>Oct</Month>
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<Title>Physical review. E, Statistical, nonlinear, and soft matter physics</Title>
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<ArticleTitle>Structure and interaction in protein solutions as studied by small-angle neutron scattering.</ArticleTitle>
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<Abstract><AbstractText>Small-angle neutron scattering (SANS) measurements have been performed to compare the effect of the salts KF, KCl, and KBr on crystallization in aqueous solution of lysozyme protein. It is found that the propensity of the salt to crystallize protein follows the Hoffmeister series (KF</AbstractText>
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Structure and interaction in protein solutions as studied by small-angle neutron scattering.

Structure and interaction in protein solutions as studied by small-angle neutron scattering.

Source :

English descriptors

Abstract

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki