Related ArticlesCalcium-induced peptide association to form an intact protein domain: 1H NMR structural evidence.
Science. 1990 Jul 20;249(4966):280-3
Authors: Shaw GS, Hodges RS, Sykes BD
The 70-residue carboxyl-terminal domain of the muscle contractile protein troponin-C contains two helix-loop-helix calcium (Ca)-binding sites that are related to each other by approximate twofold rotational symmetry. Hydrophobic residues from the helices and a short three residue beta sheet at the interface of the two sites act to stabilize the protein domain in the presence of Ca. A synthetic 34-residue peptide representing one of these sites (site III) has been synthesized and studied by H-1 nuclear magnetic resonance (NMR) spectroscopy. In solution this peptide undergoes a Ca-induced conformational change to form the helix-loop-helix Ca-binding motif. Two-dimensional nuclear Overhauser effect spectra have provided evidence for the formation of a beta sheet and interactions between several hydrophobic residues from opposing helices as found in troponin-C. It is proposed that a symmetric two-site dimer similar in tertiary structure to the carboxyl-terminal domain of troponin-C forms from the assembly of two site III peptides in the Ca-bound form.
NMR study of the structure and self-association of Core peptide in aqueous solution and DPC micelles.
NMR study of the structure and self-association of Core peptide in aqueous solution and DPC micelles.
NMR study of the structure and self-association of Core peptide in aqueous solution and DPC micelles.
Biopolymers. 2011;96(2):177-80
Authors: Zheng G, Torres AM, Ali M, Manolios N, Price WS
Core peptide is a hydrophobic peptide derived from the T-cell antigen receptor-alpha chain (TCR-alpha) transmembrane region with therapeutic potential. The mechanism by which the peptide inserts into the membrane, including any requirements to change...
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[NMR paper] NMR assignment of the apo and peptide-bound SH2 domain from the Rous sarcoma viral protein Src.
NMR assignment of the apo and peptide-bound SH2 domain from the Rous sarcoma viral protein Src.
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J Biomol NMR. 2005 Aug;32(4):339
Authors: Taylor JD, Fawaz RR, Ababou A, Williams MA, Ladbury JE
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[NMR paper] NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein
NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein that is selectively cytotoxic to cancer cells.
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Biochemistry. 2004 Feb 24;43(7):1854-61
Authors: Rosal R, Pincus MR, Brandt-Rauf PW, Fine RL, Michl J, Wang H
We have recently found that a peptide from the mdm-2 binding domain of the p53 protein induced rapid membranolytic necrosis of a variety of different human...
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[NMR paper] Micelle-induced curvature in a water-insoluble HIV-1 Env peptide revealed by NMR dipo
Micelle-induced curvature in a water-insoluble HIV-1 Env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel.
Related Articles Micelle-induced curvature in a water-insoluble HIV-1 Env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel.
J Am Chem Soc. 2002 Mar 20;124(11):2450-1
Authors: Chou JJ, Kaufman JD, Stahl SJ, Wingfield PT, Bax A
The structure of a water-insoluble fragment encompassing residues 282-304 of the HIV envelope protein gp41 is studied when solubilized by...
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[NMR paper] Calcium-induced refolding of the calmodulin V136G mutant studied by NMR spectroscopy:
Calcium-induced refolding of the calmodulin V136G mutant studied by NMR spectroscopy: evidence for interaction between the two globular domains.
Related Articles Calcium-induced refolding of the calmodulin V136G mutant studied by NMR spectroscopy: evidence for interaction between the two globular domains.
Biochemistry. 2000 Dec 26;39(51):15920-31
Authors: Fefeu S, Biekofsky RR, McCormick JE, Martin SR, Bayley PM, Feeney J
The Ca(2+) titration of the (15)N-labeled mutant V136G calmodulin has been monitored using (1)H-(15)N HSQC NMR spectra. Up...
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[NMR paper] Secondary structure and calcium-induced folding of the Clostridium thermocellum docke
Secondary structure and calcium-induced folding of the Clostridium thermocellum dockerin domain determined by NMR spectroscopy.
Related Articles Secondary structure and calcium-induced folding of the Clostridium thermocellum dockerin domain determined by NMR spectroscopy.
Arch Biochem Biophys. 2000 Jul 15;379(2):237-44
Authors: Lytle BL, Volkman BF, Westler WM, Wu JH
Assembly of the cellulosome, a large, extracellular cellulase complex, depends upon docking of a myriad of enzymatic subunits to homologous receptors, or cohesin domains, arranged...
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[NMR paper] Crystal structure of the SH2 domain from the adaptor protein SHC: a model for peptide
Crystal structure of the SH2 domain from the adaptor protein SHC: a model for peptide binding based on X-ray and NMR data.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Crystal structure of the SH2 domain from the adaptor protein SHC: a model for peptide binding based on X-ray and NMR data.
J Mol Biol. 1995 Nov 17;254(1):86-95
Authors: Mikol V, Baumann G, Zurini MG, Hommel U
Src homology 2 domains (SH2) are protein molecules found within a wide variety of cytoplasmic...
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[NMR paper] How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR s
How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in coagulation factor X.
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J Biol Chem. 1992 Sep 25;267(27):19642-9
Authors: Selander-Sunnerhagen M, Ullner M, Persson E, Teleman O, Stenflo J, Drakenberg T
Domains homologous to the epidermal growth factor...
Calcium-induced peptide association to form an intact protein domain: 1H NMR structur
Linear Mode
