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| Hauptseite > Publikationsdatenbank > Conformational dynamics of a protein in the folded and unfolded state > print |
| Hauptseite > Publikationsdatenbank > Conformational dynamics of a protein in the folded and unfolded state > print |
| 001 | 30449 | ||
| 005 | 20200402210520.0 | ||
| 024 | 7 | _ | |2 DOI |a 10.1016/S0301-0104(03)00144-7 |
| 024 | 7 | _ | |2 WOS |a WOS:000184511200032 |
| 037 | _ | _ | |a PreJuSER-30449 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 540 |
| 084 | _ | _ | |2 WoS |a Chemistry, Physical |
| 084 | _ | _ | |2 WoS |a Physics, Atomic, Molecular & Chemical |
| 100 | 1 | _ | |a Fitter, J. |b 0 |u FZJ |0 P:(DE-Juel1)131961 |
| 245 | _ | _ | |a Conformational dynamics of a protein in the folded and unfolded state |
| 260 | _ | _ | |a Amsterdam [u.a.] |b Elsevier Science |c 2003 |
| 300 | _ | _ | |a 405 - 411 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |a Chemical Physics |x 0301-0104 |0 9841 |v 292 |
| 500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
| 520 | _ | _ | |a In a quasielastic neutron scattering experiment, the picosecond dynamics of alpha-amylase was investigated for the folded and the unfolded state of the protein. In order to ensure a reasonable interpretation of the internal protein dynamics, the protein was measured in D2O-buffer solution. The much higher structural flexibility of the pH induced unfolded state as compared to the native folded state was quantified using a simple analytical model, describing a local diffusion inside a sphere. In terms of this model the conformational volume, which is explored mainly by confined protein side-chain movements, is parameterized by the radius of a sphere (folded state, r = 1.2 Angstrom; unfolded state, 1.8 Angstrom). Differences in conformational dynamics between the folded and the unfolded state of a protein are of fundamental interest in the field of protein science, because they are assumed to play an important role for the thermodynamics of folding/unfolding transition and for protein stability. (C) 2003 Elsevier Science B.V. All rights reserved. |
| 536 | _ | _ | |a Neurowissenschaften |c L01 |2 G:(DE-HGF) |0 G:(DE-Juel1)FUEK255 |x 0 |
| 588 | _ | _ | |a Dataset connected to Web of Science |
| 650 | _ | 7 | |a J |2 WoSType |
| 653 | 2 | 0 | |2 Author |a alpha-amylase |
| 653 | 2 | 0 | |2 Author |a quasielastic incoherent neutron scattering |
| 653 | 2 | 0 | |2 Author |a protein dynamics |
| 653 | 2 | 0 | |2 Author |a proteins in solution |
| 653 | 2 | 0 | |2 Author |a protein stability |
| 773 | _ | _ | |a 10.1016/S0301-0104(03)00144-7 |g Vol. 292, p. 405 - 411 |p 405 - 411 |q 292<405 - 411 |0 PERI:(DE-600)1501546-4 |t Chemical physics |v 292 |y 2003 |x 0301-0104 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1016/S0301-0104(03)00144-7 |
| 909 | C | O | |o oai:juser.fz-juelich.de:30449 |p VDB |
| 913 | 1 | _ | |k L01 |v Neurowissenschaften |l Funktion und Dysfunktion des Nervensystems |b Leben |0 G:(DE-Juel1)FUEK255 |x 0 |
| 914 | 1 | _ | |y 2003 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |k IBI-2 |l Biologische Strukturforschung |d 31.12.2006 |g IBI |0 I:(DE-Juel1)VDB58 |x 0 |
| 970 | _ | _ | |a VDB:(DE-Juel1)28924 |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a ConvertedRecord |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-Juel1)ISB-2-20090406 |
| 980 | _ | _ | |a UNRESTRICTED |
| 980 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
| 981 | _ | _ | |a I:(DE-Juel1)ISB-2-20090406 |
| 981 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
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