We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Structural Achievability of an NH–π Interaction between Gln and Phe in a Crystal Structure of a Collagen-like Peptide.
- Authors
Zhang, Ruixue; Xu, You; Lan, Jun; Fan, Shilong; Huang, Jing; Xu, Fei
- Abstract
NH–π interactions between polar and aromatic residues are well distributed in proteins whose stabilizing effects have been investigated in globular and fibrous proteins. In order to gain structural insights into side chain NH–π interactions, we solved a crystal structure of a collagen-like peptide containing Gln-Phe pairs. The Gln-Phe NH–π interactions were further characterized by quantum calculations, molecular simulations, and structural bioinformatics. The analyses indicated that the NH–π interactions are robust under various solvent conditions, can be distributed either on the protein surface or in its hydrophobic core and can form at a wide range of distances between residues. This study suggested that NH–π interactions can play a versatile role in protein design, including engineering hydrophobic cores, solvent accessible surfaces, and protein–protein interfaces.
- Subjects
PEPTIDES; CRYSTAL structure; STRUCTURAL bioinformatics; PROTEIN engineering; HYDROPHOBIC surfaces; GLOBULAR proteins
- Publication
Biomolecules (2218-273X), 2022, Vol 12, Issue 10, pN.PAG
- ISSN
2218-273X
- Publication type
Article
- DOI
10.3390/biom12101433