Conformation and molecular dynamics calculations on uteroglobin fragment 18-47.
The conformational properties of fragment 18-47 of rabbit uteroglobin in aqueous solution containing SDS micelles were investigated by two-dimensional nmr spectroscopy and molecular dynamics calculations. The fragment comprises helices II and III and the beta-turn connecting the two helices. The nmr results and nmr-restrained molecular dynamics calculations showed that in the isolated fragment the elements of secondary structure present in the intact protein are preserved only in part. Specifically, a well-defined alpha-helix was found in the sequence 33-44, corresponding to helix III of uteroglobin, while the regions of helix II and beta-turn are characterized by high flexibility in the fragment.
Department of Organic Chemistry, University of Padova, Italy.
S
S
Improta
A
A
Pastore
S
S
Mammi
E
E
Peggion
D000595:Amino Acid Sequence; D000818:Animals; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008432:Mathematical Computing; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011817:Rabbits; D012996:Solutions; D013816:Thermodynamics; D014598:Uteroglobin / Q000737:chemistry*
D010446:Peptide Fragments; D012996:Solutions; D014598:Uteroglobin