Related ArticlesNMR-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, Westley B, Chadwick M, May F, Carr MD, Feeney J
NMR spectroscopy measurements have been used to obtain structural information about the pNR-2/pS2 single-domain trefoil peptide. NMR data from 2D (two dimensional) double-quantum-filtered correlation spectroscopy (DQF-COSY), total correlation spectroscopy (TOCSY), NOE spectroscopy (NOESY), rotating frame NOE spectroscopy (ROESY) and 2D 13C-1H heteronuclear single-quantum coherence (HSQC) and 13C-1H HSQC-TOCSY spectra have been analysed to provide essentially complete 1H and 13C sequence-specific assignments for the pNR-2/pS2 protein. From a consideration of the NOE intensities, 3J(NH-alpha CH) coupling constants, 1H and 13C chemical shifts of backbone atoms and amide-proton exchange rates, the pNR-2/pS2 was found to contain two short antiparallel beta-strands (32-35 and 43-46), a short helix (25-30) and a type I beta-turn (11-15). These elements of secondary structure are very similar to those found in the two trefoil domains of pSP for which detailed structural information is already available. Similar 1H chemical shifts were noted for several conserved residues in pNR-2/pS2 and pSP and a characteristic Phe residue with a slowly flipping ring was found in the pNR-2/pS2 variant and in both domains of pSP. The tertiary structures of the domains therefore appear to be very similar in the two proteins and it is likely that the pNR-2/pS2 has the same pattern of disulphide bonds (1-5, 2-4, 3-6) as pSP. Correlation time measurements derived from 1H-1H NOE measurements indicate that the Cys58-->Ser form of the pNR-2/pS2 protein used in this study is monomeric in solution at approximately 2 mM.
Expression and purification of (15)N- and (13)C-isotope labeled 40-residue human Alzheimer's ?-amyloid peptide for NMR-based structural analysis.
Expression and purification of (15)N- and (13)C-isotope labeled 40-residue human Alzheimer's ?-amyloid peptide for NMR-based structural analysis.
Expression and purification of (15)N- and (13)C-isotope labeled 40-residue human Alzheimer's ?-amyloid peptide for NMR-based structural analysis.
Protein Expr Purif. 2011 May 27;
Authors: Long F, Cho W, Ishii Y
Amyloid fibrils of Alzheimer's ?-amyloid peptide (A?) are a primary component of amyloid plaques, a hallmark of Alzheimer's disease (AD). Enormous attention has been given to the structural...
nmrlearner
Journal club
0
06-07-2011 11:05 AM
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...
nmrlearner
Journal club
0
02-08-2011 06:28 PM
[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...
nmrlearner
Journal club
0
11-24-2010 11:14 PM
[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...
nmrlearner
Journal club
0
11-24-2010 09:51 PM
[NMR paper] A novel view of domain flexibility in E. coli adenylate kinase based on structural mo
A novel view of domain flexibility in E. coli adenylate kinase based on structural mode-coupling (15)N NMR relaxation.
Related Articles A novel view of domain flexibility in E. coli adenylate kinase based on structural mode-coupling (15)N NMR relaxation.
J Mol Biol. 2002 Jan 11;315(2):155-70
Authors: Tugarinov V, Shapiro YE, Liang Z, Freed JH, Meirovitch E
Adenylate kinase from Escherichia coli (AKeco), consisting of a single 23.6 kDa polypeptide chain folded into domains CORE, AMPbd and LID, catalyzes the reaction AMP+ATP-->2ADP. In the...
nmrlearner
Journal club
0
11-24-2010 08:49 PM
[NMR paper] Structural studies by 1H NMR of a prototypic alpha-helical peptide (LYQELQKLTQTLK) an
Structural studies by 1H NMR of a prototypic alpha-helical peptide (LYQELQKLTQTLK) and homologs in trifluoroethanol/water and on sodium dodecyl sulfate micelles.
Related Articles Structural studies by 1H NMR of a prototypic alpha-helical peptide (LYQELQKLTQTLK) and homologs in trifluoroethanol/water and on sodium dodecyl sulfate micelles.
J Pept Res. 1997 Aug;50(2):122-31
Authors: Young JK, MarĂ* F, Xu M, Humphreys RE, Clemente NM, Stattel JM, Nelson DJ, Gambino J, Wright GE
The 1H NMR-determined structure and dynamics of a synthetic,...
nmrlearner
Journal club
0
08-22-2010 05:08 PM
[NMR paper] 1H-NMR structural studies of a cystine-linked peptide containing residues 71-93 of tr
1H-NMR structural studies of a cystine-linked peptide containing residues 71-93 of transthyretin and effects of a Ser84 substitution implicated in familial amyloidotic polyneuropathy.
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 1H-NMR structural studies of a cystine-linked peptide containing residues 71-93 of transthyretin and effects of a Ser84 substitution implicated in familial amyloidotic polyneuropathy.
Eur J Biochem. 1999 Jun;262(2):586-94
...
NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similari
Linear Mode
