Zobrazeno 1 - 7
of 7
pro vyhledávání: '"L K, Tamm"'
Publikováno v:
Nature structural biology. 8(8)
The N-terminal domain of the influenza hemagglutinin (HA) is the only portion of the molecule that inserts deeply into membranes of infected cells to mediate the viral and the host cell membrane fusion. This domain constitutes an autonomous folding u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8799d53605b472c39655f6cd06ee528a
https://pubmed.ncbi.nlm.nih.gov/11473248
https://pubmed.ncbi.nlm.nih.gov/11473248
Publikováno v:
Nature structural biology. 8(4)
We have determined the three-dimensional fold of the 19 kDa (177 residues) transmembrane domain of the outer membrane protein A of Escherichia coli in dodecylphosphocholine (DPC) micelles in solution using heteronuclear NMR. The structure consists of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5fc3038d253a11b090a1505082dc2b4a
https://pubmed.ncbi.nlm.nih.gov/11276254
https://pubmed.ncbi.nlm.nih.gov/11276254
Publikováno v:
Journal of microscopy. 171(Pt 3)
Summary Recent developments in the biological applications of atomic force microscopy are reviewed, and the great potential of this novel, high-resolution imaging technique, including its limitations and possible future directions for biological rese
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ba8ca408fcfcb2be6664f3dc66e0515
https://pubmed.ncbi.nlm.nih.gov/8246269
https://pubmed.ncbi.nlm.nih.gov/8246269
Publikováno v:
Journal of molecular biology. 229(2)
We demonstrate that supported synthetic phospholipid bilayers, which are stabilized by lateral cross-linking in both leaflets, can be used for specimen preparation for atomic force microscopy of purified membrane proteins with high stability and exce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::af178cdebb64d40aca397fb4a73d3a5f
https://pubmed.ncbi.nlm.nih.gov/8429547
https://pubmed.ncbi.nlm.nih.gov/8429547
Publikováno v:
The Journal of biological chemistry. 267(16)
Peptides which correspond to the NH2-terminal 23 or 22 residues of the mannitol and glucitol permeases (enzymes IImtl and IIgut of the bacterial phosphotransferase system; mtl-23 and gut-22) and which are believed to function in envelope targeting we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b16ebb4c24c7fdd2f56b32bf6c6ba5df
https://pubmed.ncbi.nlm.nih.gov/1597443
https://pubmed.ncbi.nlm.nih.gov/1597443
Publikováno v:
The Journal of biological chemistry. 264(5)
The 22-residue synthetic signal peptide of the glucitol permease (Enzyme IIgut of the bacterial phosphotransferase system; gut22), which in the intact protein is believed to function in envelope targeting, was found to insert into phospholipid monola
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::427ce0c118be74c9b315ba7493c7b954
https://pubmed.ncbi.nlm.nih.gov/2644265
https://pubmed.ncbi.nlm.nih.gov/2644265
Publikováno v:
Scopus-Elsevier
The 22-residue synthetic signal peptide of the glucitol permease (Enzyme IIgut of the bacterial phosphotransferase system; gut22), which in the intact protein is believed to function in envelope targeting, was found to insert into phospholipid monola
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4d136e1c8e684c243eb171c3e665495
http://www.scopus.com/inward/record.url?eid=2-s2.0-0024503511&partnerID=MN8TOARS
http://www.scopus.com/inward/record.url?eid=2-s2.0-0024503511&partnerID=MN8TOARS
