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Molecular dynamics simulations of HPr under hydrostatic pressure

Canalia, Muriel and Malliavin, Thérèse E. and Kremer, Werner and Kalbitzer, Hans Robert (2004) Molecular dynamics simulations of HPr under hydrostatic pressure. Biopolymers 74 (5), pp. 377-388.

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Abstract

The histidine-containing protein (HPr) plays an important role in the phosphotransferase system (PTS). The deformations induced on the protein structure at high hydrostatic pressure values (4, 50, 100, 150, and 200 MPa) were previously (H. Kalbitzer, A. Görler, H. Li, P. Dubovskii, A. Hengstenberg, C. Kowolik, H. Yamada, and K. Akasaka, Protein Science 2000, Vol. 9, pp. 693-703) analyzed by NMR ...

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Item Type:Article
Date:2004
Additional information (public):Erratum in: Biopolymers Bd. 74, Nr. 6, S. 495
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
15222017PubMed ID
10.1002/bip.20089DOI
Classification:
NotationType
AlgorithmsMESH
AnimalsMESH
Bacterial Proteins/physiologyMESH
Computer SimulationMESH
Hydrostatic PressureMESH
Magnetic Resonance Spectroscopy/methodsMESH
Models, MolecularMESH
Phosphoenolpyruvate Sugar Phosphotransferase System/physiologyMESH
Protein ConformationMESH
Structure-Activity RelationshipMESH
Water/chemistryMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:16 Sep 2010 09:26
Last Modified:16 Sep 2010 09:26
Item ID:16608
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