AbstractDistinct amino acid sequences have been described to mediate oligomerization of transmembrane α-helices. However, as the sequence context is crucial to determine specificity in transmembrane helix–helix interaction, the question arises how small a sequence can be without losing specificity. In the present analysis, six amino acids have been identified in the PsbF transmembrane helix dimer, which form the contact region of two interacting helices and are directly involved in helix–helix interactions. However, individual amino acids within the complex sequence pattern only together ensure sequence specificity of the analyzed transmembrane helix–helix interactions by mediating close packing and inter-helical hydrogen bonding
AbstractThe GxxxG sequence motif mediates the association of transmembrane (TM) helices by providing...
SummaryWe identify a structural feature of transmembrane helical proteins that restricts their confo...
AbstractThe nature and distribution of amino acids in the helix interfaces of four polytopic membran...
AbstractDistinct amino acid sequences have been described to mediate oligomerization of transmembran...
AbstractFolding of polytopic transmembrane proteins involves interactions of individual transmembran...
The monomer-dimer equilibrium of the glycophorin A (GpA) transmembrane (TM) fragment has been used a...
AbstractStudies of the dimerization of transmembrane (TM) helices have been ongoing for many years n...
Amino acids with small side chains and motifs of small residues in a distance of four are rather abu...
The activity of apoptosis protein BNIP3 has been associated with its ability to form homodimeric and...
The principles that govern the folding and packing of membrane proteins are still not completely und...
AbstractFolding of polytopic transmembrane proteins involves interactions of individual transmembran...
AbstractStudies of the dimerization of transmembrane (TM) helices have been ongoing for many years n...
AbstractDimerization of the transmembrane domain of glycophorin A is mediated by a seven residue mot...
AbstractWe present what we believe to be a novel statistical contact potential based on solved struc...
ABSTRACT: While several reports have suggested a role for helix-helix interactions in membrane prote...
AbstractThe GxxxG sequence motif mediates the association of transmembrane (TM) helices by providing...
SummaryWe identify a structural feature of transmembrane helical proteins that restricts their confo...
AbstractThe nature and distribution of amino acids in the helix interfaces of four polytopic membran...
AbstractDistinct amino acid sequences have been described to mediate oligomerization of transmembran...
AbstractFolding of polytopic transmembrane proteins involves interactions of individual transmembran...
The monomer-dimer equilibrium of the glycophorin A (GpA) transmembrane (TM) fragment has been used a...
AbstractStudies of the dimerization of transmembrane (TM) helices have been ongoing for many years n...
Amino acids with small side chains and motifs of small residues in a distance of four are rather abu...
The activity of apoptosis protein BNIP3 has been associated with its ability to form homodimeric and...
The principles that govern the folding and packing of membrane proteins are still not completely und...
AbstractFolding of polytopic transmembrane proteins involves interactions of individual transmembran...
AbstractStudies of the dimerization of transmembrane (TM) helices have been ongoing for many years n...
AbstractDimerization of the transmembrane domain of glycophorin A is mediated by a seven residue mot...
AbstractWe present what we believe to be a novel statistical contact potential based on solved struc...
ABSTRACT: While several reports have suggested a role for helix-helix interactions in membrane prote...
AbstractThe GxxxG sequence motif mediates the association of transmembrane (TM) helices by providing...
SummaryWe identify a structural feature of transmembrane helical proteins that restricts their confo...
AbstractThe nature and distribution of amino acids in the helix interfaces of four polytopic membran...