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Complete ¹H nuclear magnetic resonance assignments and structural characterization of a fusion protein of the alpha-amylase inhibitor tendamistat with the activation domain of the human immunodeficiency virus type 1 Tat protein

Freund, J. and Vértesy, L. and Koller, K. P. and Wolber, V. and Heintz, D. and Kalbitzer, Hans Robert (1995) Complete ¹H nuclear magnetic resonance assignments and structural characterization of a fusion protein of the alpha-amylase inhibitor tendamistat with the activation domain of the human immunodeficiency virus type 1 Tat protein. Journal of molecular biology: JMB 250 (5), pp. 672-688.

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Abstract

Complete sequence-specific assignments of the1H-NMR spectrum of a fusion protein of the α-amylase inhibitor tendamistat fromStreptomyces tendaeand the activation domain of Tat from human immunodeficiency virus type 1 (HIV-1) was obtained by homonuclear two-dimensional NMR methods. The protein behaves as expected for an ideal fusion protein: the flexible linker allows an almost completely ...

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Item Type:Article
Date:1995
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
7623384PubMed ID
10.1006/jmbi.1995.0407DOI
Classification:
NotationType
Amino Acid SequenceMESH
Escherichia coliMESH
Gene Products, tat/geneticsMESH
HIV-1/geneticsMESH
HumansMESH
Hydrogen BondingMESH
Hydrogen-Ion ConcentrationMESH
Magnetic Resonance SpectroscopyMESH
Molecular Sequence DataMESH
Molecular StructureMESH
Peptides/geneticsMESH
Recombinant Fusion Proteins/chemistryMESH
Streptomyces/chemistryMESH
Sulfur/chemistryMESH
TemperatureMESH
alpha-Amylases/antagonists & inhibitorsMESH
tat Gene Products, Human Immunodeficiency VirusMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:08 Sep 2010 08:02
Last Modified:08 Sep 2010 08:02
Item ID:16512
Owner Only: item control page
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