scholarly journals A19F-NMR study of the membrane-binding region of D-lactate dehydrogenase ofescherichia coli

1993 ◽  
Vol 2 (11) ◽  
pp. 1938-1947 ◽  
Author(s):  
Zhen-Yu Sun ◽  
Hoai-Thu N. Truong ◽  
E. A. Pratt ◽  
David C. Sutherland ◽  
Christine E. Kulig ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Membrane Binding ◽  
Ofescherichia Coli ◽  
Binding Region ◽  
Nmr Study

A19F-NMR Study of the Equilibrium Unfolding of Membrane-Associatedd-Lactate Dehydrogenase ofEscherichia coli†

Biochemistry ◽  
1996 ◽  
Vol 35 (51) ◽  
pp. 16502-16509 ◽  
Author(s):  
Zhen-Yu Sun ◽  
E. Ann Pratt ◽  
Virgil Simplaceanu ◽  
Chien Ho
Keyword(s):  
Lactate Dehydrogenase ◽  
Ofescherichia Coli ◽  
Nmr Study ◽  
Equilibrium Unfolding

scholarly journals A 1H-NMR study of the activity expressed by lactate dehydrogenase in the human erythrocyte

1986 ◽  
Vol 158 (2) ◽  
pp. 299-305 ◽  
Author(s):  
Kevin M. BRINDLE ◽  
Iain D. CAMPBELL ◽  
Robert J. SIMPSON
Keyword(s):  
Lactate Dehydrogenase ◽  
1H Nmr ◽  
Human Erythrocyte ◽  
Nmr Study

Subunit composition and substrate binding region of potato l-lactate dehydrogenase

1982 ◽  
Vol 21 (3) ◽  
pp. 627-631 ◽  
Author(s):  
Ulrich Mayr ◽  
Reinhard Hensel ◽  
Otto Kandler
Keyword(s):  
Lactate Dehydrogenase ◽  
Substrate Binding ◽  
Subunit Composition ◽  
Binding Region

Immunologic evidence that staphylococcal alpha toxin is oriented on membranes

1979 ◽  
Vol 25 (6) ◽  
pp. 686-692 ◽  
Author(s):  
C. Y. Lo ◽  
H. B. Fackrell
Keyword(s):  
Membrane Binding ◽  
The Other ◽  
Erythrocyte Membranes ◽  
Alpha Toxin ◽  
Binding Region ◽  
Indirect Hemagglutination

Antibodies to staphylococcal alpha toxin were separated into two distinct populations. One population prevented binding of alpha toxin onto erythrocyte membranes. The other population neutralized after the toxin was bound onto erythrocytes and thereby brought about an indirect hemagglutination reaction.The data suggest that alpha toxin has a membrane-binding region.

scholarly journals Highly potent antimicrobial peptides from N-terminal membrane-binding region of E. coli MreB

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Karabi Saikia ◽  
Yalavarthi Durga Sravani ◽  
Vibin Ramakrishnan ◽  
Nitin Chaudhary
Keyword(s):  
Antimicrobial Peptides ◽  
Membrane Binding ◽  
Binding Region ◽  
E Coli

scholarly journals Mutants of the membrane-binding region of Semliki Forest virus E2 protein. I. Cell surface transport and fusogenic activity.

1986 ◽  
Vol 102 (3) ◽  
pp. 889-901 ◽  
Author(s):  
D F Cutler ◽  
H Garoff
Keyword(s):  
Cell Surface ◽  
Semliki Forest Virus ◽  
Membrane Binding ◽  
Binding Region ◽  
Hydrophobic Region ◽  
E2 Protein ◽  
Mutant Proteins ◽  
Surface Transport ◽  
Charged Amino Acids ◽  
Charge Cluster

Three mutations of the membrane-binding region of the Semliki Forest virus (SFV) p62 polypeptide (the precursor for virion E3 and E2) have been made by oligonucleotide-directed mutagenesis of a cDNA clone encoding the SFV structural proteins. One of the mutations (A2) substitutes a Glu for an Ala in the middle of the hydrophobic stretch which spans the bilayer. A1 and A3 alter the two basic charged amino acids in the cytoplasmic domain next to the hydrophobic region. The wild-type charge cluster of Arg-Ser-Lys (+2) has been changed to Gly-Ser-Met (0;A3) or to Gly-Ser-Glu (-1;A1). The mutant p62 proteins have been analyzed both in the presence and the absence of E1, the other half of the heterodimer spike complex of SFV. The mutant proteins expressed in COS-7 cells are glycosylated and are of the expected sizes. When co-expressed with E1, all three mutants are cleaved to yield the E2 protein and transported to the surface of COS-7 cells. When expressed in the absence of E1, the mutant p62 proteins remain uncleaved but still reach the cell surface. Once at the cell surface, all three mutants, when co-expressed with E1, can promote low pH-triggered cell-cell fusion. These results show that the three mutant p62/E2 proteins are still membrane associated in a functionally unaltered way.

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