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  • 1
    Electronic Resource
    Electronic Resource
    Influence of the Ionic Environment on the Conformation of Aspartic Acid and Possible Relevance to Its Neurotransmitter Action (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 40 (1983), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The conformational changes of aspartic acid, a possible neurotransmitter, induced by increasing ionic strength were investigated by means of NMR spectros-copy. The effects of Li, Na, K, and Cs chlorides in basic and neutral conditions were characterized. The effects of the presence of both Ca2+ and Na+ or K+ were also examined. The results always showed a relative stabilization of the two conformers with gauche carboxylates at the expense of the anticonformer. The significant quantitative difference found between Na+ and K+ in basic solutions, as well as between calcium-free and calcium-containing solutions, may bear some relevance for the role of aspartate as a CNS neurotransmitter.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1983.tb08071.x
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  • 2
    Electronic Resource
    Electronic Resource
    High-resolution proton NMR study of the solution structure of alamethicin (1987)
    s.l. : American Chemical Society
    Biochemistry 26 (1987), S. 1043-1050 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00378a010
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  • 3
    Electronic Resource
    Electronic Resource
    NMR structural characterization of the reaction product between d(GpG) and the octahedral antitumor complex trans-RuCl2(DMSO)4 (1992)
    s.l. : American Chemical Society
    Biochemistry 31 (1992), S. 7094-7103 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00146a010
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  • 4
    Electronic Resource
    Electronic Resource
    Hydrogen–deuterium exchange studies of the rat thyroid transcription factor 1 homeodomain (1997)
    Springer
    Journal of biomolecular NMR 9 (1997), S. 397-407 
    Details
    ISSN: 1573-5001
    Keywords: Thyroid transcription factor 1 homeodomain ; Homeodomain ; DNA-binding proteins ; Protein NMR; ; Hydrogen–deuterium exchange ; Secondary structure thermal stability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The 1H NMR solution structure of the rat thyroidtranscription factor 1 homeodomain (TTF-1 HD) showed that the molecule foldslike classical homeodomains. The C-terminal extension of helix III (fragment51–59) appeared to adopt a helical geometry, albeit not as rigid asthe preceding portion, but the hydrogen–deuterium exchange of backboneamides and the NOE data provided evidence of a discontinuity between the twomoieties of helix III at the highly conserved fragmentAsn51–His52–Arg53.Analysis of quantitative measurements of isotope exchange rates allows oneto recognize the general occurrence, in that region of HD motifs, ofopposite effects to helix III stability. Asparagine, histidine and arginineresidues occur most frequently at the beginning and end of protein helices.In TTF-1 HD a local fluctuation is observed in the fragment 51–53which either kinks or tightens the α-helix. A search through theprotein structure database reveals that the three most common variants of HDfragments 51–53 are often involved in helices and, frequently, inhelix initiation or termination. For homeodomains in general, the nature ofthe fragment 51–53 may be related to the conformational dynamics oftheir DNA-recognition helix (helix III). Besides the specific results onfragment 51–53, the complete isotope exchange analysis of TTF-1 HDdata shows that the partially solvent-exposed recognition helix isstabilized by hydrophobic interactions, like most of the structured regionsof the molecule. Hydrophobic stabilization of the contacting regions meetsthe requirements of a DNA-interaction mechanism which, as shown with otherDNA-protein complexes, should entail negative heat capacity variations dueto changes in solvent exposure of the nonpolar protein surface.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018350611521
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  • 5
    Electronic Resource
    Electronic Resource
    Tendamistat surface accessibility to the TEMPOL paramagnetic probe (1999)
    Springer
    Journal of biomolecular NMR 15 (1999), S. 125-133 
    Details
    ISSN: 1573-5001
    Keywords: molecular presentation ; protein structure ; spin-labels ; surface accessibility ; tendamistat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract TEMPOL, the soluble spin-label 4-hydroxy-2,2,6,6-tetramethyl-piperidine-1-oxyl, has been used to determine the surface characteristics of tendamistat, a small protein with a well-characterised structure both in solution and in the crystal. A good correlation has been found between predicted regions of exposed protein surface and the intensity attenuations induced by the probe on 2D NMR TOCSY cross peaks of tendamistat in the paramagnetic water solution. All the high paramagnetic effects have been interpreted in terms of more efficient competition of TEMPOL with water molecules at some surface positions. The active site of tendamistat coincides with the largest surface patch accessible to the probe. A strong hydration of protein N and C termini can also be suggested by this structural approach, as these locations exhibit reduced paramagnetic perturbations. Provided that the solution structure is known, the use of this paramagnetic probe seems to be well suited to delineate the dynamic behaviour of the protein surface and, more generally, to gain relevant information about the molecular presentation processes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008319507565
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  • 6
    Electronic Resource
    Electronic Resource
    Distance evaluation via heteronuclear SQC-NOESY experiments (1992)
    Springer
    Journal of biomolecular NMR 2 (1992), S. 289-299 
    Details
    ISSN: 1573-5001
    Keywords: Distance evaluation ; SQC-NOESY NMR ; Heteronuclear
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A method for the quantitative determination of interproton distances from1H NOE relayed heteronuclear correlation is presented. Model compounds are investigated. Accurate distances are obtained if all the factors affecting such distance measurements, such as the local mobility and the presence of strong coupling in heteronuclear systems, are properly taken into account.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01875322
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  • 7
    Electronic Resource
    Electronic Resource
    Structural comparison between retro-inverso and parent peptides: Molecular basis for the biological activity of a retro-inverso analogue of the immunodominant fragment of VP1 coat protein from foot-and-mouth disease virus (1997)
    New York : Wiley-Blackwell
    Biopolymers 41 (1997), S. 569-590 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Antibodies induced against intact foot-and-mouth disease Virus (FMDV) particles bind to the retro-inverso analogue of fragment 141-159 of the viral coat protein VP1 of FMDV, variant A, equally well as to the parent peptide. A conformational investigation of this retro-inverso peptide was carried out by nmr spectroscopy and restrained molecular modeling in order to identify the structural basis for the antigenic mimicry between these retro-inverso and parent peptides. In 100% trifluoroethanol a well-defined left-handed α-helical region exists from residue 150 to residue 159, which is consistently present in all conformational families obtained from restrained modelling. A less-defined left-handed helical region is present in the tract 144-148, which is also consistent for all structures. Conformational flexibility exists about Gly149, which leads to two types of structures, either bent or linear. In the bent structures, a three-residue inverse tight turn is found, which can be classified as an inverse γ-turn centered at Gly149. The overall structural features of the retro-inverso peptide are shown to be similar to those of the parent L-peptide. The two molecules, however, are roughly mirror images because they share inherently chiral secondary structure elements. By comparing these conformational conclusions with the x-ray structure of the Fab complex of a corresponding VP1 antigenic fragment, a rationale is proposed to account for the topological requirements of specific recognition that are implied by the equivalent antigenic activity of the natural and retro-inverso compounds. © 1997 John Wiley & Sons, Inc. Biopoly 41: 569-590, 1997.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Solution structure of regioselectively addressable functionalized templates: An NMR and restrained molecular dynamics investigation (1996)
    New York : Wiley-Blackwell
    Biopolymers 39 (1996), S. 297-308 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Three cyclic peptides that are Regioselectively Addressable Functionalized Templates (RAFT) for use in protein de novo design have been investigated using a combination of nmr, restrained molecular dynamics, and CD spectroscopy. These peptides contain up to four selectively addressable sites (orthogonally protected lysine side chains) or have selectively addressable faces. The results show a common stable conformation for templates of this kind based on two type II β-turns and an associated β-sheet structure. A preferential orientation for the side chains is also demonstrated. The significance of these findings is discussed in the context of applications of RAFT that rely on their conformational rigidity and ability to present functionalities in a defined spatial arrangement. © 1996 John Wiley & Sons, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Probing protein structure by solvent perturbation of nmr spectra. II. Determination of surface and buried residues in homologous proteins (1993)
    New York : Wiley-Blackwell
    Biopolymers 33 (1993), S. 839-846 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The experimental assignment of most residues in a protein to the surface or interior is in principle possible without prior solution of a complete three-dimensional structure. The method described is based on nmr measurements that determine the amino acid composition of the surface of a protein [A. Petros, L. Mueller, and K. D. Kopple (1990) Biochemistry, Vol. 29, pp. 10041-10048; G. Esposito, A. M. Lesk, H. Molinari, A. Motta, N. Niccolai, and A. Pastore (1992) Journal of Molecular Biology, Vol. 224, pp. 659-670]. If these measurements are carried out on several homologous proteins of known sequence, it is possible to combine the results to determine, in most cases, which positions in the sequence contain exposed residues. © 1993 John Wiley & Sons, Inc.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360330512
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  • 10
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    COMMD7 as a novel NEMO interacting protein involved in the termination of NF-κBsignaling (2015)
    Wiley-Blackwell
    Details
    Publication Date: 2015-06-09
    Description: NEMO/IKKγ is the regulatory subunit of the IκB Kinase (IKK) complex, required for the activation of the NF-κB pathway, which is involved in a variety of key processes, including immunity, inflammation, differentiation and cell survival. Termination of NF-κB activity on specific -κB responsive genes, which is crucial for the resolution of inflammatory responses, can be achieved by direct degradation of the chromatin-bound NF-κB subunit RelA/p65, a process mediated by a protein complex that contains Copper Metabolism Murr1 Domain 1 (COMMD1). In this study, we identify COMMD7, another member of the COMMDs protein family, as a novel NEMO-interacting protein. We show that COMMD7 exerts an inhibitory effect on NF-κB activation upon TNFα stimulation. COMMD7 interacts with COMMD1 and together they cooperate to down-regulate NF-κB activity. Accordingly, termination of TNFα-induced NF-κB activity on the -κB responsive gene, Icam1, is defective in cells silenced for COMMD7 expression. Furthermore, this impairment is not greatly increased when we silence the expression of both COMMD7 and COMMD1 indicating that the two proteins participate in the same pathway of termination of TNFα-induced NF-κB activity. Importantly, we have demonstrated that COMMD7's binding to NEMO does not interfere with the binding to the IKKs, and that the disruption of the IKK complex through the use of the NBP competitor impairs the termination of NF-κB activity. We propose that an intact IKK complex is required for the termination of NF-κB-dependent transcription and that COMMD7 acts as a scaffold in the IKK-mediated NF-κB termination. This article is protected by copyright. All rights reserved
    Electronic ISSN: 1097-4652
    Topics: Biology , Medicine
    Published by Wiley-Blackwell
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