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Specific aggregations of alanine tetrapeptide derivatives as studied by nuclear magnetic resonance
Author(s) -
Goodman M.,
Ueyama N.,
Naider F.,
Gilon C.
Publication year - 1975
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1975.360140503
Subject(s) - tetrapeptide , chemistry , tetramer , alanine , dimer , chloroform , derivative (finance) , hydrogen bond , stereochemistry , amine gas treating , resonance (particle physics) , side chain , crystallography , molecule , amino acid , peptide , organic chemistry , enzyme , biochemistry , polymer , physics , financial economics , economics , particle physics
By use of high resolution nuclear magnetic resonance and infrared spectroscopy, we have found evidence for specific folded forms for the methoxyethoxyethoxyacetyl‐blocked alanine tetramer ethyl ester. It appears that this tetrapeptide derivative exists in a folded form which is in rapid equilibrium with an extended structure (i.e., below 1% w/v). At high concentrations (i.e., above 1% w/v in chloroform) the folded form is stabilized by an association of the alanine tetrapeptide derivative into a side‐by‐side dimer which contains specific hydrogen bonds between the amine terminal regions of the two folded structures.