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Profil
| Derzeitige Stellung | Professor W-3 und Äquivalente |
|---|---|
| Fachgebiet | Biophysikalische Chemie,Biophysik |
| Keywords | Proteinfaltung, Proteinkonformation, Wasserstoffbrückenbindungen, entfaltete Proteine, Monte Carlo Simulationen zur Proteinfaltung |
Aktuelle Kontaktadresse
| Land | USA |
|---|---|
| Ort | Baltimore |
| Universität/Institution | Johns Hopkins University |
| Institut/Abteilung | Department of Biophysics |
Gastgeber*innen während der Förderung
| Prof. Dr. Thomas Kiefhaber | Lehrstuhl für Biophysikalische Chemie, Technische Universität München, Garching |
|---|---|
| Prof. Dr. Joachim Heberle | Fachbereich Physik, Arbeitsgruppe Experimentelle Molekulare Biophysik, Freie Universität Berlin, Berlin |
| Prof. Dr. Thomas Kiefhaber | Institut für Biochemie und Biotechnologie, Martin-Luther-Universität Halle-Wittenberg, Halle (Saale) |
| Beginn der ersten Förderung | 01.01.2012 |
Programm(e)
| 2011 | Humboldt-Forschungspreis-Programm für Naturwissenschaftler*innen aus den USA |
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Projektbeschreibung der*des Nominierenden
| Professor Rose is an internationally leading scientist in the field of protein chemistry and has made seminal contributions to the understanding of protein folding and stability. He introduced methods for identification and classification of protein secondary structure elements and developed a commonly used hydrophobicity scale for amino acids. In Germany, Professor Rose will study the structure and dynamics of unfolded polypeptide chains in order to test models for protein folding proposed by him. |
Publikationen (Auswahl)
| 2019 | George D. Rose: Ramachandran maps for side chains in globular proteins. In: Proteins, Structure, Function and Bioinformatics, 2019, |
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| 2013 | Robert L. Baldwin George D. Rose: Molten globules, entropy-driven conformational change and protein folding. In: Current Opinion in Structural Biology, 2013, 4-10 |
| 2013 | George D. Rose: THE OPEN-ENDED INTELLECTUAL LEGACY OF GNR. In: Manju Bansal N. Srinivasan, Biomolecular Forms and Functions. World Scientific, 2013. 38-45 |