Structure and interaction in protein solutions as studied by small-angle neutron scattering.
Identifieur interne : 000390 ( Ncbi/Curation ); précédent : 000389; suivant : 000391Structure and interaction in protein solutions as studied by small-angle neutron scattering.
Auteurs : S. Chodankar [Inde] ; V K AswalSource :
- Physical review. E, Statistical, nonlinear, and soft matter physics [ 1539-3755 ] ; 2005.
Descripteurs français
- KwdFr :
- MESH :
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
DOI: 10.1103/PhysRevE.72.041931
PubMed: 16383444
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pubmed:16383444Le document en format XML
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<term>Crystallization (methods)</term>
<term>Models, Chemical</term>
<term>Models, Molecular</term>
<term>Multiprotein Complexes (chemistry)</term>
<term>Multiprotein Complexes (ultrastructure)</term>
<term>Muramidase (chemistry)</term>
<term>Muramidase (ultrastructure)</term>
<term>Neutron Diffraction (methods)</term>
<term>Protein Binding</term>
<term>Protein Conformation</term>
<term>Salts (chemistry)</term>
<term>Solutions</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Complexes multiprotéiques ()</term>
<term>Complexes multiprotéiques (ultrastructure)</term>
<term>Conformation des protéines</term>
<term>Cristallisation ()</term>
<term>Diffraction de neutrons ()</term>
<term>Liaison aux protéines</term>
<term>Lysozyme ()</term>
<term>Lysozyme (ultrastructure)</term>
<term>Modèles chimiques</term>
<term>Modèles moléculaires</term>
<term>Sels ()</term>
<term>Simulation numérique</term>
<term>Solutions</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Multiprotein Complexes</term>
<term>Muramidase</term>
<term>Salts</term>
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<term>Neutron Diffraction</term>
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<keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Multiprotein Complexes</term>
<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>
<term>Protein Binding</term>
<term>Protein Conformation</term>
<term>Solutions</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Complexes multiprotéiques</term>
<term>Conformation des protéines</term>
<term>Cristallisation</term>
<term>Diffraction de neutrons</term>
<term>Liaison aux protéines</term>
<term>Lysozyme</term>
<term>Modèles chimiques</term>
<term>Modèles moléculaires</term>
<term>Sels</term>
<term>Simulation numérique</term>
<term>Solutions</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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