Related ArticlesReconstitution of a native-like SH2 domain from disordered peptide fragments examined by multidimensional heteronuclear NMR.
Protein Sci. 2001 Nov;10(11):2162-75
Authors: Ojennus DD, Fleissner MR, Wuttke DS
The N-terminal SH2 domain from the p85alpha subunit of phosphatidylinositol 3' kinase is cleaved specifically into 9- and 5-kD fragments by limited proteolytic digestion with trypsin. The noncovalent SH2 domain complex and its constituent tryptic peptides have been investigated using high-resolution heteronuclear magnetic resonance (NMR). These studies have established the viability of the SH2 domain as a fragment complementation system. The individual peptide fragments are predominantly unstructured in solution. In contrast, the noncovalent 9-kD + 5-kD complex shows a native-like (1)H-(15)N HSQC spectrum, demonstrating that the two fragments fold into a native-like structure on binding. Chemical shift analysis of the noncovalent complex compared to the native SH2 domain reveals that the highest degree of perturbation in the structure occurs at the cleavage site within a flexible loop and along the hydrophobic interface between the two peptide fragments. Mapping of these chemical shift changes on the structure of the domain reveals changes consistent with the reduction in affinity for the target peptide ligand observed in the noncovalent complex relative to the intact protein. The 5-kD fragment of the homologous Src protein is incapable of structurally complementing the p85 9-kD fragment, either in complex formation or in the context of the full-length protein. These high-resolution structural studies of the SH2 domain fragment complementation features establish the suitability of the system for further protein-folding and design studies.
Expression, purification, and reconstitution of the transmembrane domain of the human amyloid precursor protein for NMR studies.
Expression, purification, and reconstitution of the transmembrane domain of the human amyloid precursor protein for NMR studies.
Expression, purification, and reconstitution of the transmembrane domain of the human amyloid precursor protein for NMR studies.
Protein Expr Purif. 2011 Aug 31;
Authors: Chen W, Gamache E, Richardson D, Du Z, Wang C
Abstract
Alzheimer's disease (AD) is the most common type of dementia in elderly people. Senile plaques, a pathologic hallmark of AD, are composed of amyloid ? peptide (A?). A? aggregation produces...
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Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Biomol NMR Assign. 2011 Jun 7;
Authors: Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA
Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we...
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06-08-2011 11:30 AM
[NMR paper] Conformational properties of peptide fragments homologous to the 106-114 and 106-126
Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study.
Related Articles Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study.
Org Biomol Chem. 2005 Feb 7;3(3):490-7
Authors: Di Natale G, Impellizzeri G, Pappalardo G
Two peptide fragments, corresponding to the amino acid residues 106-126 (PrP) and 106-114 (PrP) of the human prion protein have...
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[NMR paper] Microscopic stability of cold shock protein A examined by NMR native state hydrogen e
Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide.
Related Articles Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide.
Protein Sci. 2000 Feb;9(2):290-301
Authors: Jaravine VA, Rathgeb-Szabo K, Alexandrescu AT
Native state hydrogen exchange of cold shock protein A (CspA) has been characterized as a function of the denaturant urea and of the stabilizing agent...
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11-18-2010 09:15 PM
19F NMR analysis of the antimicrobial peptide PGLa bound to native cell membranes fro
19F NMR analysis of the antimicrobial peptide PGLa bound to native cell membranes from bacterial protoplasts and human erythrocytes.
Related Articles 19F NMR analysis of the antimicrobial peptide PGLa bound to native cell membranes from bacterial protoplasts and human erythrocytes.
J Am Chem Soc. 2010 Jul 7;132(26):8822-4
Authors: Ieronimo M, Afonin S, Koch K, Berditsch M, Wadhwani P, Ulrich AS
(19)F NMR is a unique tool to examine the structure of fluorine-labeled peptides in their native cellular environment, due to an exquisite sensitivity...
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10-05-2010 12:11 PM
[NMR paper] High helicity of peptide fragments corresponding to beta-strand regions of beta-lacto
High helicity of peptide fragments corresponding to beta-strand regions of beta-lactoglobulin observed by 2D-NMR spectroscopy.
Related Articles High helicity of peptide fragments corresponding to beta-strand regions of beta-lactoglobulin observed by 2D-NMR spectroscopy.
Fold Des. 1996;1(4):255-63
Authors: Kuroda Y, Hamada D, Tanaka T, Goto Y
BACKGROUND: Whereas protein fragments, when they are structured, adopt conformations similar to that found in the native state, the high helical propensity of beta-lactoglobulin, a predominantly beta-sheet...
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[NMR paper] Orientation of peptide fragments from Sos proteins bound to the N-terminal SH3 domain
Orientation of peptide fragments from Sos proteins bound to the N-terminal SH3 domain of Grb2 determined by NMR spectroscopy.
Related Articles Orientation of peptide fragments from Sos proteins bound to the N-terminal SH3 domain of Grb2 determined by NMR spectroscopy.
Biochemistry. 1994 Nov 22;33(46):13531-9
Authors: Wittekind M, Mapelli C, Farmer BT, Suen KL, Goldfarb V, Tsao J, Lavoie T, Barbacid M, Meyers CA, Mueller L
NMR spectroscopy has been used to characterize the protein-protein interactions between the mouse Grb2 (mGrb2) N-terminal...
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[NMR paper] 1H NMR analysis of fibril-forming peptide fragments of transthyretin.
1H NMR analysis of fibril-forming peptide fragments of transthyretin.
Related Articles 1H NMR analysis of fibril-forming peptide fragments of transthyretin.
Int J Pept Protein Res. 1994 Oct;44(4):388-98
Authors: Jarvis JA, Kirkpatrick A, Craik DJ
Peptide fragments of the protein transthyretin, previously shown to form cross beta-sheet amyloid-like fibrils in vitro, were investigated using 1H 1D and 2D NMR techniques. TTR 10-20, TTR 105-115 as well as a substituted analogue, (TTR 105-115Met111) all formed amyloid-like fibrils readily in 20-30%...
Reconstitution of a native-like SH2 domain from disordered peptide fragments examined
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