Abstract:
:Substance P, one of the mammalian tachykinins, is known to interact strongly with lipid bilayers and this interaction may play a role in the receptor-peptide recognition process. The conformation of substance P bound to vesicles consisting of perdeuterated phosphatidylcholine has been investigated by means of two-dimensional transferred nuclear Overhauser (trNOE) spectroscopy. Nuclear magnetic resonance data analysis resulted in a unique conformational family characterized by a well-defined conformation of the last seven C-terminal amino acids, which consists of a sequence of nonstandard turns following each other in a helix-like manner. The absence of short- or medium-range trNOE in the N-terminal part indicates its structural flexibility.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Augé S,Bersch B,Tropis M,Milon Adoi
10.1002/1097-0282(20001015)54:5<297::AID-BIP10>3.0subject
Has Abstractpub_date
2000-10-15 00:00:00pages
297-306issue
5eissn
0006-3525issn
1097-0282pii
10.1002/1097-0282(20001015)54:5<297::AID-BIP10>3.0journal_volume
54pub_type
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