Zobrazeno 1 - 10
of 124
pro vyhledávání: '"Rudy A. Demel"'
Publikováno v:
Biochimica et Biophysica Acta. Biomembranes 1615 (2003) 1-2
Biochimica et Biophysica Acta. Biomembranes, 1615(1-2), 84-92
Biochimica et Biophysica Acta. Biomembranes, 1615(1-2), 84-92
Clavanin A is a special antimicrobial peptide that acts at the level of the membrane via a pH-dependent mechanism. At neutral pH, clavanin disrupts biological and model membranes in a nonspecific manner, causing efflux of large molecules. At mildly a
Publikováno v:
Chemistry and Physics of Lipids. 117:75-81
We have previously shown that proteins such as b-lactoglobulin and lysozyme insert into monoglyceride monolayers and are able to induce an Lb to coagel phase transition in monoglyceride bilayers. These studies gave a first indication that protein sta
Publikováno v:
European Journal of Biochemistry. 268:4036-4043
Toc75 is an outer envelope membrane protein of chloroplasts. It is unusual among the outer membrane proteins in that its precursor form has a bipartite transit peptide. The N-terminal portion of the Toc75 transit peptide is sufficient to target the p
Publikováno v:
Biochimica et Biophysica Acta. Biomembranes 1511 (2001)
Biochimica et Biophysica Acta. Biomembranes, 1511, 309-316
Biochimica et Biophysica Acta. Biomembranes, 1511, 309-316
Gene 9 minor coat protein from bacteriophage M13 is known to be located in the inner membrane after phage infection of Escherichia coli. The way of insertion of this small protein (32 amino acids) into membranes is still unknown. Here we show that th
Anionic phospholipids are involved in membrane association of FtsY and stimulate its GTPase activity
Autor:
Irmgard Sinning, K. te Kaat, B. de Kruijff, Claudio Moser, Joen Luirink, Bauke Oudega, E. de Leeuw, G. Menestrina, Rudy A. Demel
Publikováno v:
ResearcherID
FtsY, the Escherichia coli homologue of the eukaryotic signal recognition particle (SRP) receptor alpha-subunit, is located in both the cytoplasm and inner membrane. It has been proposed that FtsY has a direct targeting function, but the mechanism of
Publikováno v:
European Journal of Biochemistry. 259:96-103
The Skp protein of Escherichia coli has been proposed to be a periplasmic molecular chaperone involved in the biogenesis of outer membrane proteins. In this study, evidence is obtained that Skp exists in two different states characterized by their di
Publikováno v:
ResearcherID
Bacterial fructans with a high degree of polymerisation cause a very large increase in surface pressure of lipid monolayers at the air–water interface with a broad range of lipids, including phosphatidylethanolamine and several types of phosphatidy
Autor:
Eefjan Breukink, Oscar P. Kuipers, Rudy A. Demel, Annemieke van Dalen, Ben de Kruijff, Roland J. Siezen, Cindy van Kraaij
Publikováno v:
Biochemistry, 37(22), 8153-8162. AMER CHEMICAL SOC
Nisin is a 34 residue long peptide belonging to the group A lantibiotics with antimicrobial activity against Gram-positive bacteria. The antimicrobial activity is based on pore formation in the cytoplasmic membrane of target organisms. The mechanism
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1330(1):61-70
The interactions between beta-lactoglobulin and 1-monostearoyl-glycerol were studied in order to gain insight into protein-gel-phase monoglyceride interactions. Using a monomolecular layer at the air-water interface, we determined the insertion of be
Autor:
Geerten Verberkmoes, Eefjan Breukink, R.C.A. Keller, Anne L. J. Van Raalte, Rudy A. Demel, Ben de Kruijff
Publikováno v:
BASE-Bielefeld Academic Search Engine
Scopus-Elsevier
Scopus-Elsevier
To investigate in a direct way the interaction between a precursor protein and phospholipids, monolayer studies were performed using the purified precursor of Escherichia coli outer‐membrane protein PhoE. It was demonstrated that prePhoE can insert