Zobrazeno 1 - 10
of 18
pro vyhledávání: '"D. F. Mierke"'
Autor:
D F Mierke, Carla Isernia, Michele Saviano, P. Di Lello, E Benedetti, Stefania Galdiero, C Pedone, C Bassarello
Publikováno v:
The Journal of Peptide Research. 65:200-208
The Antennapedia homeodomain structure consists of four helices. The helices II and III are connected by a tripeptide that forms a turn, and constitute the well-known helix-turn-helix motif. The recognition helix penetrates the DNA major groove, give
Autor:
C, Giragossian, D F, Mierke
Publikováno v:
Biochemistry. 40:3804-3809
The interaction of the C-terminal octapeptide of cholecystokinin, CCK-8, with the third extracellular loop of human cholecystokinin-A receptor, CCK(A)-R(329-357), has been probed by high-resolution NMR and extensive computer simulations. The structur
Autor:
J. Saulitis, Stephan Seip, Martin Will, S. Steuernagel, D. F. Mierke, Horst Kessler, Thomas Wein
Publikováno v:
Biopolymers. 32:427-433
The constitution and configuration of Ro 09-0198 (cinnamycin) have been determined in DMSO. Further investigations in aqueous solution, in SDS micelles and in a lipid bilayer have been done to study the influence of different environments on the conf
Autor:
BENEDETTI, ETTORE, C. ISERNIA, NASTRI, FLAVIA, C. PEDONE, M. SAVIANO, D. F. MIERKE, P. MELCHIORRI, L. NEGRI, R. L. POTENZA, C. SEVERINI, V. ERSPAMER
To identify the peptide conformation that is preferentially recognized by the receptor, we have synthetized by solidphase method a series of deltorphin I analogs with increasing selectivity for δ- and μ-opioid receptor. Structure-selectivity relati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::82a3030dbaadb089624cbed60d1fe0dc
http://hdl.handle.net/11591/184387
http://hdl.handle.net/11591/184387
Autor:
G, Saviano, F, Rossi, E, Benedetti, C, Pedone, D F, Mierke, A, Maione, G, Zanotti, T, Tancredi, M, Saviano
Publikováno v:
Chemistry (Weinheim an der Bergstrasse, Germany). 7(6)
The conformational features of both free and Ca2+-complexed cyclo[Pro-Phe-Phe-Ala-Xaa]2 (with Xaa= Glu(OtBu), Lys(CIZ), Leu, and Ala) in solution have been determined by NMR spectroscopy and extensive distance-geometry calculations. The decapeptides
Publikováno v:
The Journal of biological chemistry. 276(25)
Molecular models for the interaction of substance P (SP) with its G protein-coupled receptor, the neurokinin-1 receptor (NK-1R), have been developed. The ligand.receptor complex is based on experimental data from a series of photoaffinity labeling ex
Publikováno v:
Biopolymers. 42(7)
The structure and dynamics of the ionophoric antibiotic monensin in the presence of micelles have been determined. The conformation of monensin was derived from 50 nuclear Overhauser enhancement (NOE) derived distance restraints and metric-matrix bas
Autor:
M, Pellegrini, D F, Mierke
Publikováno v:
Biopolymers. 51(3)
The structural characterization of peptide hormones and their interaction with G-protein (guanine nucleotide-binding regulatory protein) coupled receptors by high-resolution nmr is described. The general approaches utilized can be categorized into th
Autor:
S G, Grdadolnik, D F, Mierke
Publikováno v:
Biopolymers. 42(6)
Publikováno v:
Biopolymers. 40(6)
The third-cytoplasmic loop of the G-protein coupled receptor responsible for the activity of parathyroid hormone and parathyroid hormone-related protein has been structurally characterized in aqueous solution in the presence of sodium dodecylsulfate