7veg

Understanding NH-pi interaction between Gln and Phe

spinqualitylabelsall models 7veg, resolution 1.39Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7veg is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.39Å Ligands: ACE, HYP, NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed NH-pi 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-pi interactions, we solved a crystal structure of a collagen-like peptide containing Gln-Phe pairs. The Gln-Phe NH-pi interactions were further characterized by quantum calculations, molecular simulations, and structural bioinformatics. The analyses indicated that the NH-pi 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-pi interactions can play a versatile role in protein design, including engineering hydrophobic cores, solvent accessible surfaces, and protein-protein interfaces. Structural Achievability of an NH-pi Interaction between Gln and Phe in a Crystal Structure of a Collagen-like Peptide.,Zhang R, Xu Y, Lan J, Fan S, Huang J, Xu F Biomolecules. 2022 Oct 6;12(10):1433. doi: 10.3390/biom12101433. PMID:36291642 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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