Zobrazeno 1 - 10
of 62
pro vyhledávání: '"W, Meijberg"'
Autor:
Paula J. Booth, W Meijberg
Publikováno v:
Journal of Molecular Biology. 319:839-853
The physical mechanisms that govern the folding and assembly of integral membrane proteins are poorly understood. It appears that certain properties of the lipid bilayer affect membrane protein folding in vitro , either by modulating helix insertion
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c731999534a3f786e16837dfdbbc25aa
https://doi.org/10.1016/s0022-2836(02)00342-x
https://doi.org/10.1016/s0022-2836(02)00342-x
Publikováno v:
Biochemistry. 35(51):16753-16759
The thermal denaturation of bovine alpha-lactalbumin (BLA) was studied at pH 7.5 and at various Ca2+ concentrations using near-UV circular dichroism and differential scanning calorimetry. The Ca2+ dependence of the denaturation equilibria proves that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2cc7f20b2cc58c81bc0f96e409fcbfd2
https://doi.org/10.1021/bi9608830
https://doi.org/10.1021/bi9608830
Publikováno v:
Journal of controlled release : official journal of the Controlled Release Society. 101(1-3)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a03f5967fd3391e279bbfecb4e301181
https://pubmed.ncbi.nlm.nih.gov/15822228
https://pubmed.ncbi.nlm.nih.gov/15822228
Publikováno v:
Journal of controlled release : official journal of the Controlled Release Society. 101(1-3)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a687a6dddda6d90f3da2e595bda9fc9b
https://pubmed.ncbi.nlm.nih.gov/15822222
https://pubmed.ncbi.nlm.nih.gov/15822222
Publikováno v:
Journal of controlled release : official journal of the Controlled Release Society. 101(1-3)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::954e16a68c4fbe9dd0e87694d7074ae2
https://pubmed.ncbi.nlm.nih.gov/15751183
https://pubmed.ncbi.nlm.nih.gov/15751183
Publikováno v:
Journal of molecular biology. 342(4)
Research into the folding mechanisms of integral membrane proteins lags far behind that of water-soluble proteins, to the extent that the term protein folding is synonymous with water-soluble proteins. Hydrophobic membrane proteins, and particularly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::472735aef446b21473cb37952d404597
https://pubmed.ncbi.nlm.nih.gov/15351652
https://pubmed.ncbi.nlm.nih.gov/15351652
Autor:
A. Meter-Arkema, W. Meijberg, H. Miedema, J. Wierenga, H. Hektor, Bob Eisenberg, M. Vrouenraets
Publikováno v:
Bio-, Micro-, and Nanosystems (IEEE Cat. No.03EX733).
Ion channels are transmembrane proteins that control large fluxes of ions across otherwise impermeable membranes. They can be seen as naturally occurring nanotubes whose properties can be controlled very precisely using the tools of molecular biology
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::971ebb938dab7f75180fbe52c735df05
https://doi.org/10.1109/bmn.2003.1220606
https://doi.org/10.1109/bmn.2003.1220606
Publikováno v:
Critical reviews in biochemistry and molecular biology. 36(6)
The study of membrane protein folding is a new and challenging research field. Consequently, there are few direct studies on the in vitro folding of membrane proteins. This review covers work aimed at understanding folding mechanisms and the intermol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9affbb757ea8e6826583f2e3078ecde
https://pubmed.ncbi.nlm.nih.gov/11798093
https://pubmed.ncbi.nlm.nih.gov/11798093
Publikováno v:
The Journal of biological chemistry. 273(33)
The thermal stability and domain interactions in the mannitol transporter from Escherichia coli, enzyme IImtl, have been studied by differential scanning calorimetry. To this end, the wild type enzyme, IICBAmtl, as well as IICBmtl and IICmtl, were re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d52e27f6cbedf0e30f071e91ebc691ea
https://pubmed.ncbi.nlm.nih.gov/9694823
https://pubmed.ncbi.nlm.nih.gov/9694823
Publikováno v:
Biochemical Society Transactions. 28:A50-A50
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::20b03f65f70985d8812bf32c955e7476
https://doi.org/10.1042/bst028a050
https://doi.org/10.1042/bst028a050