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dc.contributor.author | Orzáez Calatayud, María del Mar | |
dc.contributor.author | Pérez Payá, Enrique | |
dc.contributor.author | Mingarro Muñoz, Ismael | |
dc.date.accessioned | 2018-04-17T14:03:51Z | |
dc.date.available | 2018-04-17T14:03:51Z | |
dc.date.issued | 2000 | |
dc.identifier.citation | Orzáez Calatayud, María del Mar Pérez Payá, Enrique Mingarro Muñoz, Ismael 2000 Influence of the C‐terminus of the glycophorin A transmembrane fragment on the dimerization process Protein Science 9 6 1246 1253 | |
dc.identifier.uri | http://hdl.handle.net/10550/65752 | |
dc.description.abstract | The monomer-dimer equilibrium of the glycophorin A (GpA) transmembrane (TM) fragment has been used as a model system to investigate the amino acid sequence requirements that permit an appropriate helix-helix packing in a membrane‐mimetic environment. In particular, we have focused on a region of the helix where no crucial residues for packing have been yet reported. Various deletion and replacement mutants in the C‐terminal region of the TM fragment showed that the distance between the dimerization motif and the flanking charged residues from the cytoplasmic side of the protein is important for helix packing. Furthermore, selected GpA mutants have been used to illustrate the rearrangement of TM fragments that takes place when leucine repeats are introduced in such protein segments. We also show that secondary structure of GpA derivatives was independent from dimerization, in agreement with the two‐stage model for membrane protein folding and oligomerization. | |
dc.language.iso | eng | |
dc.relation.ispartof | Protein Science, 2000, vol. 9, num. 6, p. 1246-1253 | |
dc.subject | Proteïnes de membrana | |
dc.title | Influence of the C‐terminus of the glycophorin A transmembrane fragment on the dimerization process | |
dc.type | journal article | es_ES |
dc.date.updated | 2018-04-17T14:03:51Z | |
dc.identifier.doi | 10.1110/ps.9.6.1246 | |
dc.identifier.idgrec | 003978 | |
dc.rights.accessRights | open access | es_ES |