Related ArticlesSequence-specific resonance assignments of the 1H-NMR spectra and structural characterization in solution of the HIV-1 transframe protein p6.
Eur J Biochem. 1996 Apr 15;237(2):383-92
Authors: Beissinger M, Paulus C, Bayer P, Wolf H, Rösch P, Wagner R
The frameshift protein p6* encoded directly upstream of the protease in the human immunodeficiency virus type 1 (HIV-1) pol reading frame is thought to be a natural inhibitor of protease activation and to play a role in the polyprotein processing of Gag and Gag-Pol precursors. To allow structural characterization of the p6* transframe protein, the p6* coding region was cloned into the vector pGEX-KG and expressed in Escherichia coli as a fusion protein with glutathione S-transferase (GST) under the control of the tac promoter. Thrombin cleavage of the construct resulted in a 70-amino-acid polypeptide which is extended by two additional residues at the N-terminus compared to the natural p6* sequence. The native purification procedure including an affinity and a size-exclusion chromatography step yielded sufficient amounts of highly pure protein suitable for NMR spectroscopy. Fluorescence, circular dichroism and 1H-NMR spectroscopy were applied to characterize the structure of protein. Two-dimensional NMR spectra provided essentially complete sequence-specific resonance assignments at pH 5.9. Although there is evidence for a helix-forming tendency in the N-terminus of the protein, the experiments indicate that p6* has no overall stable secondary or tertiary structure with the single tryptophan exposed in aqueous solution. However, the results reported herein open the way to characterize further the interaction of p6* with the HIV-1 protease in structural and functional in vitro studies.
[NMR paper] Sequence-specific NMR resonance assignments of the backbone atoms for the olfactory m
Sequence-specific NMR resonance assignments of the backbone atoms for the olfactory marker protein, OMP.
Related Articles Sequence-specific NMR resonance assignments of the backbone atoms for the olfactory marker protein, OMP.
J Biomol NMR. 2000 Aug;17(4):353-4
Authors: Baldisseri DM, Margolis JW, Omotosho PA, Volkman BF, Margolis FL
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[NMR paper] Sequence-specific 1H NMR resonance assignments and secondary structure of human apoli
Sequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulfate.
Related Articles Sequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulfate.
Biochem Cell Biol. 1998;76(2-3):267-75
Authors: Rozek A, Sparrow JT, Weisgraber KH, Cushley RJ
Apolipoprotein (apo) C-I is a 57-residue exchangeable plasma protein distributed mainly in high and very low density lipoprotein. In this report we...
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[NMR paper] Composition and sequence specific resonance assignments of the heterogeneous N-linked
Composition and sequence specific resonance assignments of the heterogeneous N-linked glycan in the 13.6 kDa adhesion domain of human CD2 as determined by NMR on the intact glycoprotein.
Related Articles Composition and sequence specific resonance assignments of the heterogeneous N-linked glycan in the 13.6 kDa adhesion domain of human CD2 as determined by NMR on the intact glycoprotein.
Biochemistry. 1995 Feb 7;34(5):1622-34
Authors: Wyss DF, Choi JS, Wagner G
CD2, a T cell specific surface adhesion receptor, is critically important for T...
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[NMR paper] Sequence-specific resonance assignments of the 1H-NMR spectra of a synthetic, biologi
Sequence-specific resonance assignments of the 1H-NMR spectra of a synthetic, biologically active EIAV Tat protein.
Related Articles Sequence-specific resonance assignments of the 1H-NMR spectra of a synthetic, biologically active EIAV Tat protein.
Biochemistry. 1993 Aug 24;32(33):8439-45
Authors: Willbold D, Krüger U, Frank R, Rosin-Arbesfeld R, Gazit A, Yaniv A, Rösch P
The equine infectious anemia virus (EIAV) trans-activating (Tat) protein is a close homologue of the human immunodeficiency virus (HIV) Tat protein. Both of these proteins...
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[NMR paper] Sequence-specific 1H NMR assignments and structural characterization of bovine semina
Sequence-specific 1H NMR assignments and structural characterization of bovine seminal fluid protein PDC-109 domain b.
Related Articles Sequence-specific 1H NMR assignments and structural characterization of bovine seminal fluid protein PDC-109 domain b.
Biochemistry. 1991 Feb 12;30(6):1663-72
Authors: Constantine KL, Ramesh V, Bányai L, Trexler M, Patthy L, Llinás M
Sequence-specific resonance assignments for the isolated second or b domain of the bovine seminal fluid protein PDC-109 have been obtained from analysis of two-dimensional 1H...
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[NMR paper] Sequence-specific 1H NMR resonance assignments of Bacillus subtilis HPr: use of spect
Sequence-specific 1H NMR resonance assignments of Bacillus subtilis HPr: use of spectra obtained from mutants to resolve spectral overlap.
Related Articles Sequence-specific 1H NMR resonance assignments of Bacillus subtilis HPr: use of spectra obtained from mutants to resolve spectral overlap.
Biochemistry. 1990 Aug 7;29(31):7191-200
Authors: Wittekind M, Reizer J, Klevit RE
On the basis of an analysis of two-dimensional 1H NMR spectra, the complete sequence-specific 1H NMR assignments are presented for the phosphocarrier protein HPr from the...
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[NMR paper] An efficient NMR approach for obtaining sequence-specific resonance assignments of la
An efficient NMR approach for obtaining sequence-specific resonance assignments of larger proteins based on multiple isotopic labeling.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles An efficient NMR approach for obtaining sequence-specific resonance assignments of larger proteins based on multiple isotopic labeling.
FEBS Lett. 1990 Jun 18;266(1-2):155-8
Authors: Ikura M, Krinks M, Torchia DA, Bax A
By simultaneously incorporating in a protein 13C-carbonyl- and...
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[NMR paper] Sequence-specific [1H]NMR resonance assignments and secondary structure identificatio
Sequence-specific NMR resonance assignments and secondary structure identification for 1- and 2-zinc finger constructs from SW15. A hydrophobic core involving four invariant residues.
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FEBS Lett. 1990 Mar 26;262(2):179-84
Authors: Neuhaus D, Nakaseko Y, Nagai K, Klug A
Complete NMR resonance assignments are presented for the second of the three...