Related ArticlesStructural studies of the acidic transactivation domain of the Vmw65 protein of herpes simplex virus using 1H NMR.
Biochemistry. 1992 Apr 28;31(16):4150-6
Authors: O'Hare P, Williams G
We have overproduced and purified the carboxy-terminal transactivation domain of Vmw65 (VP16) of herpes simplex virus, and studied potential folding of the domain by 1H NMR. Two species of the acidic domain were obtained from the bacterial expression system, and we demonstrate that one of these represents read-through of the natural amber termination codon of the Vmw65 reading frame producing a larger polypeptide. Additional residues in the read-through product were identified by total amino acid analysis and by NMR. Study of the correctly terminated product by 1D NMR gave resonances which were clustered into groups around their random-coil chemical shift positions, and 2D NMR demonstrated that, even in mixed solvents containing up to 80% MeOH, there was very little evidence of secondary structure. Together these results indicate that the isolated acid domain has little if any alpha-helical content of any stable nature. We discuss these results with reference to the demonstrated activity of the acidic domain in a wide variety of polypeptide contexts.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Chem Biol Drug Des. 2011 Feb 5;
Authors: Gizachew D, Dratz E
Protein-protein interactions control signaling, specific adhesion and many other biological functions. The three dimensional structures of the interfaces and bound ligand can be...
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[NMR paper] NMR structural study of TcUBP1, a single RRM domain protein from Trypanosoma cruzi: c
NMR structural study of TcUBP1, a single RRM domain protein from Trypanosoma cruzi: contribution of a beta hairpin to RNA binding.
Related Articles NMR structural study of TcUBP1, a single RRM domain protein from Trypanosoma cruzi: contribution of a beta hairpin to RNA binding.
Biochemistry. 2005 Mar 15;44(10):3708-17
Authors: Volpon L, D'Orso I, Young CR, Frasch AC, Gehring K
TcUBP1 is a trypanosome cytoplasmic RNA-binding protein containing a single, conserved RNA-recognition motif (RRM) domain involved in selective destabilization of U-rich...
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[NMR paper] NMR structural studies of domain 1 of receptor-associated protein.
NMR structural studies of domain 1 of receptor-associated protein.
Related Articles NMR structural studies of domain 1 of receptor-associated protein.
J Biomol NMR. 2004 Jul;29(3):271-9
Authors: Wu Y, Migliorini M, Walsh J, Yu P, Strickland DK, Wang YX
The 39 kDa receptor-associated protein (RAP) is an endoplasmic reticulum resident protein that binds tightly to the low-density lipoprotein receptor-related protein (LRP) as well as to other members of the low-density lipoprotein receptor superfamily. The association of RAP with LRP prevents...
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[NMR paper] Structural analysis of the extracellular domain of vaccinia virus envelope protein, A
Structural analysis of the extracellular domain of vaccinia virus envelope protein, A27L, by NMR and CD spectroscopy.
Related Articles Structural analysis of the extracellular domain of vaccinia virus envelope protein, A27L, by NMR and CD spectroscopy.
J Biol Chem. 2002 Jun 7;277(23):20949-59
Authors: Lin TH, Chia CM, Hsiao JC, Chang W, Ku CC, Hung SC, Tzou DL
This study presents the molecular structure of the extracellular domain of vaccinia virus envelope protein, A27L, determined by NMR and CD spectroscopy. A recombinant protein, eA27L-aa,...
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[NMR paper] 15N NMR relaxation studies of free and ligand-bound human acidic fibroblast growth fa
15N NMR relaxation studies of free and ligand-bound human acidic fibroblast growth factor.
Related Articles 15N NMR relaxation studies of free and ligand-bound human acidic fibroblast growth factor.
J Biol Chem. 2000 Dec 15;275(50):39444-50
Authors: Chi Y, Kumar TK, Chiu IM, Yu C
15N NMR relaxation data have been used to characterize the backbone dynamics of the human acidic fibroblast growth factor (hFGF-1) in its free and sucrose octasulfate (SOS)-bound states. (15)N longitudinal (R(1)), transverse (R(2)) relaxation rates and (1H)-(15)N...
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[NMR paper] H-NMR and CD studies on the structural transition of serum albumin in the acidic regi
H-NMR and CD studies on the structural transition of serum albumin in the acidic region--the N-->F transition.
Related Articles H-NMR and CD studies on the structural transition of serum albumin in the acidic region--the N-->F transition.
J Pept Res. 1998 Dec;52(6):431-42
Authors: Era S, Sogami M
Helical content (f(alpha)) of bovine mercaptalbumin (BMA) showed the characteristic two-step decrease in the acidic region, one corresponding to the N-->F transition (pH 4.40-->3.75; f(alpha), 0.68-->0.58) and the other to the F-->E transition (the...
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[NMR paper] 2H NMR studies of a myristoylated peptide in neutral and acidic phospholipid bicelles
2H NMR studies of a myristoylated peptide in neutral and acidic phospholipid bicelles.
Related Articles 2H NMR studies of a myristoylated peptide in neutral and acidic phospholipid bicelles.
Biochemistry. 1998 Nov 3;37(44):15523-7
Authors: Struppe J, Komives EA, Taylor SS, Vold RR
Deuterium NMR spectra of Myr-d27-GNAAAAKKGSEQES (Cat14), the N-terminal 14-residue peptide from the catalytic subunit of cAMP-dependent protein kinase A (PKA), illustrate how magnetically aligned neutral and acidic phospholipid bicelles can be used to characterize...
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[NMR paper] NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similari
NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similarities to porcine spasmolytic peptide and evidence for a monomeric structure.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similarities to porcine spasmolytic peptide and evidence for a monomeric structure.
Eur J Biochem. 1995 Nov 1;233(3):847-55
Authors: Polshakov VI, Frenkiel TA,...
Structural studies of the acidic transactivation domain of the Vmw65 protein of herpe
Linear Mode
