guest ::
| Home > Publications database > Dynamics of apo-myoglobin in the alpha-to-beta transition and of partially unfolded aggregated protein > print |
| Home > Publications database > Dynamics of apo-myoglobin in the alpha-to-beta transition and of partially unfolded aggregated protein > print |
| 001 | 4699 | ||
| 005 | 20200402205616.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:18853152 |
| 024 | 7 | _ | |2 DOI |a 10.1007/s00249-008-0375-z |
| 024 | 7 | _ | |2 WOS |a WOS:000262671600010 |
| 037 | _ | _ | |a PreJuSER-4699 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biophysics |
| 100 | 1 | _ | |0 P:(DE-HGF)0 |a Fabiani, E. |b 0 |
| 245 | _ | _ | |a Dynamics of apo-myoglobin in the alpha-to-beta transition and of partially unfolded aggregated protein |
| 260 | _ | _ | |a Berlin |b Springer |c 2009 |
| 300 | _ | _ | |a 237 - 244 |
| 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 | |0 10441 |a European Biophysics Journal : with Biophysics Letters |v 38 |x 0175-7571 |y 2 |
| 500 | _ | _ | |a The authors acknowledge the IN13 and IRIS staffs for their support during the experiment at ILL and ISIS facilities. Thanks are due to Dr. Felix Fernandez-Alonso and Dr. Franz Demmel for helpful discussions. Technical and financial support from the ILL and ISIS facilities is gratefully acknowledged. The WAXS measurement was done under the approval of the JASRI Program Advisory Committee ( Proposal #2006A1339). M. Tehei acknowledges the ILL, the AINSE, the CNRS and the Institut de Biologie Structurale (UMR 5075) for financial support of this work. |
| 520 | _ | _ | |a Changes of molecular dynamics in the alpha-to-beta transition associated with amyloid fibril formation were explored on apomyoglobin (ApoMb) as a model system. Circular dichroism, neutron and X-ray scattering experiments were performed as a function of temperature on the protein, at different solvent conditions. A significant change in molecular dynamics was observed at the alpha-to-beta transition at about 55 degrees C, indicating a more resilient high temperature beta structure phase. A similar effect at approximately the same temperature was observed in holo-myoglobin, associated with partial unfolding and protein aggregation. A study in a wide temperature range between 20 and 360 K revealed that a dynamical transition at about 200 K for motions in the 50 ps time scale exists also for a hydrated powder of heat-denatured aggregated ApoMb. |
| 536 | _ | _ | |0 G:(DE-Juel1)FUEK443 |2 G:(DE-HGF) |a Programm Biosoft |c N03 |x 0 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Amyloidosis: physiopathology |
| 650 | _ | 2 | |2 MeSH |a Apoproteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Circular Dichroism |
| 650 | _ | 2 | |2 MeSH |a Crystallography, X-Ray |
| 650 | _ | 2 | |2 MeSH |a Models, Molecular |
| 650 | _ | 2 | |2 MeSH |a Myoglobin: chemistry |
| 650 | _ | 2 | |2 MeSH |a Neutron Diffraction |
| 650 | _ | 2 | |2 MeSH |a Pharmaceutical Solutions |
| 650 | _ | 2 | |2 MeSH |a Protein Folding |
| 650 | _ | 2 | |2 MeSH |a Protein Multimerization |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Tertiary |
| 650 | _ | 2 | |2 MeSH |a Temperature |
| 650 | _ | 2 | |2 MeSH |a Thermodynamics |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Apoproteins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Myoglobin |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Pharmaceutical Solutions |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a apomyoglobin |
| 650 | _ | 7 | |2 WoSType |a J |
| 653 | 2 | 0 | |2 Author |a Amyloid former |
| 653 | 2 | 0 | |2 Author |a Protein dynamics |
| 653 | 2 | 0 | |2 Author |a Neutron |
| 653 | 2 | 0 | |2 Author |a Circular dichroism |
| 700 | 1 | _ | |0 P:(DE-Juel1)VDB78506 |a Stadler, A.M. |b 1 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Madern, D. |b 2 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Hirai, M. |b 3 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Zaccai, G. |b 4 |
| 773 | _ | _ | |0 PERI:(DE-600)1398349-0 |a 10.1007/s00249-008-0375-z |g Vol. 38, p. 237 - 244 |p 237 - 244 |q 38<237 - 244 |t European biophysics journal |v 38 |x 0175-7571 |y 2009 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1007/s00249-008-0375-z |
| 909 | C | O | |o oai:juser.fz-juelich.de:4699 |p VDB |
| 913 | 1 | _ | |0 G:(DE-Juel1)FUEK443 |a DE-HGF |b Schlüsseltechnologien |k N03 |l BioSoft |v Programm Biosoft |x 0 |z entfällt |
| 914 | 1 | _ | |y 2009 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |0 I:(DE-Juel1)ISB-2-20090406 |d 31.12.2010 |g ISB |k ISB-2 |l Molekulare Biophysik |x 0 |
| 970 | _ | _ | |a VDB:(DE-Juel1)111889 |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a ConvertedRecord |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
| 980 | _ | _ | |a UNRESTRICTED |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
| 981 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
| 981 | _ | _ | |a I:(DE-Juel1)ISB-2-20090406 |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|