About: Helix-helix interaction patterns in membrane proteins

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An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Helix-helix interaction patterns in membrane proteins
Creator	Fuchs, Angelika Herrmann, Jana Langosch, Dieter Unterreitmeier, Stephanie
Source	PMC
abstract	Membrane-spanning α-helices represent major sites of protein-protein interaction in membrane protein oligomerization and folding. As such, these interactions may be of exquisite specificity. Specificity often rests on a complex interplay of different types of residues forming the helix-helix interfaces via dense packing and different non-covalent forces, including van der Waal’s forces, hydrogen bonding, charge-charge interactions, and aromatic interactions. These interfaces often contain complex residue motifs where the contribution of constituent amino acids depends on the context of the surrounding sequence. Moreover, transmembrane helix-helix interactions are increasingly recognized as being dynamic and dependent on the functional state of a given protein.
has issue date	2011-01-04(xsd:dateTime)
bibo:doi	10.1007/978-3-7091-0045-5_10
has license	no-cc
sha1sum (hex)	6cbf1b1dcf911e7fd8a88870d8b6c94aebbd369b
schema:url	https://doi.org/10.1007/978-3-7091-0045-5_10
resource representing a document's title	Helix-helix interaction patterns in membrane proteins
has PubMed Central identifier	PMC7123687
schema:publication	Structural Bioinformatics of Membrane Proteins
resource representing a document's body	covid:6cbf1b1dcf911e7fd8a88870d8b6c94aebbd369b#body_text
is schema:about of	named entity 'MEMBRANE PROTEINS' named entity 'van' named entity 'packing' named entity 'INTERACTION' named entity 'SITES' named entity 'GIVEN' named entity 'HELIX' named entity 'HYDROGEN BONDING' named entity 'DER' named entity 'MAY BE' named entity 'BEING' named entity 'NON-' named entity 'CONTEXT' named entity 'ESE' named entity 'PROTEIN OLIGOMERIZATION' named entity 'TRANSMEMBRANE HELIX' named entity 'CITY' named entity 'DENSE' named entity 'CHARGE' named entity 'SURROUNDING' named entity 'CONTRIBUTION' named entity 'AMINO ACIDS' named entity 'CONTAIN' named entity 'RESIDUE' named entity 'MOTIFS' named entity 'OFT' named entity 'FORCES' named entity 'PATTERNS' named entity 'HELIX' named entity 'MAJOR' named entity 'VAN' named entity 'THESE' named entity 'WAAL' named entity 'REPRESENT' named entity 'FOLDING' named entity 'PROTEIN-PROTEIN INTERACTION' named entity 'COMPLEX' named entity 'INTERACTIONS' named entity 'FUNCTIONAL STATE' named entity 'TYPES' named entity 'COVALENT' named entity 'CONSTITUENT' named entity 'AROMATIC' named entity 'PROTEIN' named entity 'FORMING' named entity 'PACKING' named entity 'DYNAMIC' named entity 'MEMBRANE' named entity 'INCLUDING' named entity 'WHERE' named entity 'MEMBRANE PROTEIN' named entity '27S' named entity 'HELICES' named entity 'SEQUENCE' named entity 'DEPENDENT' named entity 'RESTS' named entity 'city' named entity 'transmembrane' named entity 'sequence' named entity 'folding' named entity 'amino acids' named entity 'dynamic' named entity 'oligomerization' named entity 'amino acids' named entity 'H-bond' named entity 'atom' named entity 'dimerization' named entity 'Trp' named entity 'mutagenesis' named entity 'Phe' named entity 'TMDs' named entity 'growth factor receptors' named entity 'oligomer' named entity 'Asp' named entity 'aromatic' named entity 'protonation' named entity 'motif' named entity 'N-terminal' named entity 'biological function' named entity 'Ser'

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