Abstract:
:The x-ray crystal structure of an oligomeric miniprotein has been determined to a 1.2-A resolution by means of multiwavelength anomalous diffraction phasing with selenomethionine analogs that retain the biophysical characteristics of the native peptide. Peptide 1, comprising alpha and beta secondary structure elements with only 21 aa per monomer, associates as a discrete tetramer. The peptide adopts a previously uncharacterized quaternary structure in which alpha and beta components interact to form a tightly packed and well defined hydrophobic core. The structure provides insight into the origins of the unusual thermal stability of the oligomer. The miniprotein shares many characteristics of larger proteins, including cooperative folding, lack of 1-anilino-8-naphthalene sulfonate binding, and limited deuterium exchange, and possesses a buried surface area typical of native proteins.
journal_name
Proc Natl Acad Sci U S Aauthors
Ali MH,Peisach E,Allen KN,Imperiali Bdoi
10.1073/pnas.0401245101keywords:
subject
Has Abstractpub_date
2004-08-17 00:00:00pages
12183-8issue
33eissn
0027-8424issn
1091-6490pii
0401245101journal_volume
101pub_type
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