Oligomeric 
详细信息 查看全文
- 作者：Kevin A. McDonnell and Barbara Imperiali
- 刊名：Journal of the American Chemical Society
- 出版年：2002
- 出版时间：January 23, 2002
- 年：2002
- 卷：124
- 期：3
- 页码：428 - 433
- 全文大小：98K
- 年卷期：v.124,no.3(January 23, 2002)
- ISSN：1520-5126
文摘
The role of a single glycine hinge residue in the structure of BBAT1, a 
peptide that formsa discrete homotrimeric structure in solution, was evaluated with 11 new peptide sequences which differonly in the identity of the residue at the hinge position. The integrity of the structure and oligomeric stateof the peptides was evaluated by using a combination of analytical ultracentrifugation and circular dichroismspectroscopy. Initially, it was discovered that the glycine hinge adopts backbone dihedral angles favoredin D-amino acids and that incorporation of D-alanine at the hinge position stabilizes the trimer species.Subsequently, the effect of the side chains of different D-amino acids at the hinge position was evaluated.While incorporation of polar amino acids led to a destabilization of the oligomeric form of the peptide, onlypeptides including D-Ser or D-Asp at the hinge position were able to achieve a discrete trimer species.Incorporation of hydrophobic amino acids D-Leu and D-Phe led to oligomerization beyond a trimer to atetrameric form. The dramatic differences among the thermodynamic stabilities and oligomeric states ofthese peptides illustrates the pivotal role of the hinge residue in the oligomerization of the peptides.
peptide that formsa discrete homotrimeric structure in solution, was evaluated with 11 new peptide sequences which differonly in the identity of the residue at the hinge position. The integrity of the structure and oligomeric stateof the peptides was evaluated by using a combination of analytical ultracentrifugation and circular dichroismspectroscopy. Initially, it was discovered that the glycine hinge adopts backbone dihedral angles favoredin D-amino acids and that incorporation of D-alanine at the hinge position stabilizes the trimer species.Subsequently, the effect of the side chains of different D-amino acids at the hinge position was evaluated.While incorporation of polar amino acids led to a destabilization of the oligomeric form of the peptide, onlypeptides including D-Ser or D-Asp at the hinge position were able to achieve a discrete trimer species.Incorporation of hydrophobic amino acids D-Leu and D-Phe led to oligomerization beyond a trimer to atetrameric form. The dramatic differences among the thermodynamic stabilities and oligomeric states ofthese peptides illustrates the pivotal role of the hinge residue in the oligomerization of the peptides.