Conformational Space of Flexible Biological Macromolecules from Average Data.
The concept of maximum occurrence (MO), i.e., the maximum percent of time that flexible proteins can spend in any given conformation, is introduced, and a rigorous method is developed to extensively sample the conformational space and to construct MO maps from experimental data. The method is tested...
| Publicado en: | Journal of the American Chemical Society Vol. 132; no. 38; pp. 13553 - 13559 |
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| Autores principales: | , , , , , , , |
| Formato: | Artículo |
| Publicado: |
American Chemical Society
9/29/2010
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| Materias: | |
| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=hlh&AN=54273091&site=ehost-live header: @attributes: shortDbName: hlh uiTerm: 54273091 longDbName: Humanities International Complete uiTag: AN controlInfo: bkinfo: jinfo: jid: 00027863 ACS jtl: Journal of the American Chemical Society issn: 00027863 maglogo: N pubinfo: dt: 9/29/2010 vid: 132 iid: 38 pid: 997 pub: American Chemical Society artinfo: ui: 54273091 10.1021/ja1063923 ppf: 13553 ppct: 6 formats: tig: atl: Conformational Space of Flexible Biological Macromolecules from Average Data. aug: au: Bertini, Ivano Giachetti, Andrea Luchinat, Claudio Parigi, Giacomo Petoukhov, Maxim V. Pierattelli, Roberta Ravera, Enrico Svergun, Dmitri I. affil: CERM, University of Florence, Via L. Sacconi 6, University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino, Italy Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino, Italy EMBL, Hamburg Outstation, Notkestrasse 85, D-22603 Hamburg, Germany Institute of Crystallography, Russian Academy of Sciences, Leninsky pr. 59, 117333 Moscow, Russia su: Biomacromolecules Calmodulin antagonists Conformational analysis Magnetic properties of rare earth metals Computer software Grid computing Nuclear magnetic resonance Web portals sug: subj: Biomacromolecules Calmodulin antagonists Conformational analysis Magnetic properties of rare earth metals Computer software Grid computing Nuclear magnetic resonance Web portals ab: The concept of maximum occurrence (MO), i.e., the maximum percent of time that flexible proteins can spend in any given conformation, is introduced, and a rigorous method is developed to extensively sample the conformational space and to construct MO maps from experimental data. The method is tested in a case study, the flexible two-domain protein calmodulin (CaM), using SAXS and NMR data (i.e., pseudocontact shifts and self-orientation residual dipolar couplings arising from the presence of paramagnetic lanthanide ions), revealing that the "closed" and "fully extended" conformations trapped in the crystalline forms of CaM have MOs of only 5 and 15%, respectively. Compact conformations in general have small MOs, whereas some extended conformations have MO as high as 35%, strongly suggesting these conformations to be most abundant in solution. The method is universally applicable as it requires only standard SAXS data and specific NMR data on lanthanide derivatives of the protein (using native metal sites or lanthanide tagging). The computer program is publicly available using the grid computing infrastructure through the authors' Web portal. pubtype: Academic Journal doctype: Article src: R language: English refInfo: copyright: @attributes: flag: Y dt: @attributes: year: 2010 holdings: @attributes: islocal: N |
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