Flexibility observed in high resolution structures of Streptomyces aureofaciens ribonucleases determined by diffraction methods
Abstract: It has been widely accepted to distinguish between static structures determined by diffraction methods and dynamic structures determined by nuclear magnetic resonance (NMR). The dynamics of NMR structures is demonstrated by an ensemble of a number of overlaid structures. This cannot be seen in one structure determined by diffraction methods. However, it is possible to see the flexibility of a protein molecule in a number of structures of the same protein determined by X-ray techniques which is manifested by different conformations of main-chain. Multiple protein structure determination does not provide identical structures as a result of various factors including flexibility. Overlap of structures of a protein determined at atomic resolution with high accuracy shows that the root-mean-square deviations (rmsd) of main-chain atoms exceed several fold the accuracy of the positional parameters of each structure. Overlap of a number of structures of a protein determined by diffraction methods shows a similar distribution as that determined by NMR. These observations are demonstrated using high resolution structures of Streptomyces aureofaciens ribonucleases, their mutants and complexes with ligands.
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Erschienen in
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Flexibility observed in high resolution structures of Streptomyces aureofaciens ribonucleases determined by diffraction methods ; volume:65 ; number:4 ; year:2010 ; pages:569-576 ; extent:8
Biologia ; 65, Heft 4 (2010), 569-576 (gesamt 8)
- Urheber
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Ševčík, Jozef
- DOI
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10.2478/s11756-010-0076-9
- URN
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urn:nbn:de:101:1-2409221652456.158317256646
- Rechteinformation
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
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15.08.2025, 07:39 MESZ
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Beteiligte
- Ševčík, Jozef
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