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Formation of fibrous aggregates from a non-native intermediate: the isolated P22 tailspike beta-helix domain

Schuler, B. and Rachel, Reinhard and Seckler, R. (1999) Formation of fibrous aggregates from a non-native intermediate: the isolated P22 tailspike beta-helix domain. The Journal of biological chemistry 274 (26), pp. 18589-18596.

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Abstract

In the assembly pathway of the trimeric P22 tailspike protein, the protein conformation critical for the partitioning between productive folding and off-pathway aggregation is a monomeric folding intermediate. The central domain of tailspike, a large right-handed parallel beta-helix, is essentially structured in this species. We used the isolated beta-helix domain (Bhx), expressed with a ...

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Item Type:Article
Date:1999
Institutions:Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie > Prof. Dr. Michael Thomm
Identification Number:
ValueType
10373469PubMed ID
Classification:
NotationType
Bacteriophage P22/chemistryMESH
Chromatography, GelMESH
Crystallography, X-RayMESH
Glycoside Hydrolases/chemistryMESH
LightMESH
Models, MolecularMESH
Molecular Sequence DataMESH
Osmolar ConcentrationMESH
Protein ConformationMESH
Protein FoldingMESH
Protein Structure, SecondaryMESH
Scattering, RadiationMESH
UltracentrifugationMESH
Viral Tail Proteins/chemistryMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:15 Mar 2010 08:12
Last Modified:15 Mar 2010 08:12
Item ID:13305
Owner Only: item control page
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