Structural Achievability of an NH–π Interaction between Gln and Phe in a Crystal Structure of a Collagen-like Peptide
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 c...
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| Published in | Biomolecules (Basel, Switzerland) Vol. 12; no. 10; p. 1433 |
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| 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. |
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| AbstractList | 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. 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.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. |
| Audience | Academic |
| Author | Lan, Jun Fan, Shilong Xu, You Huang, Jing Xu, Fei Zhang, Ruixue |
| AuthorAffiliation | 1 Ministry of Education Key Laboratory of Industrial Biotechnology, School of Biotechnology, Jiangnan University, Wuxi 214122, China 3 Westlake AI Therapeutics Lab, Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou 310024, China 2 Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou 310024, China 4 Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China |
| AuthorAffiliation_xml | – name: 2 Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou 310024, China – name: 1 Ministry of Education Key Laboratory of Industrial Biotechnology, School of Biotechnology, Jiangnan University, Wuxi 214122, China – name: 4 Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China – name: 3 Westlake AI Therapeutics Lab, Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou 310024, China |
| Author_xml | – sequence: 1 fullname: Zhang, Ruixue – sequence: 2 fullname: Xu, You – sequence: 3 fullname: Lan, Jun – sequence: 4 fullname: Fan, Shilong – sequence: 5 fullname: Huang, Jing – sequence: 6 fullname: Xu, Fei |
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| CitedBy_id | crossref_primary_10_1021_acscatal_3c02629 crossref_primary_10_1002_biot_202300453 crossref_primary_10_1016_j_bmcl_2023_129431 crossref_primary_10_1016_j_csbj_2024_02_026 |
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| Snippet | NH–π interactions between polar and aromatic residues are well distributed in proteins whose stabilizing effects have been investigated in globular and fibrous... NH-π interactions between polar and aromatic residues are well distributed in proteins whose stabilizing effects have been investigated in globular and fibrous... |
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| SubjectTerms | Bioinformatics Collagen Crystal structure Crystals Data collection Energy Glutamine Hydrophobicity Interfaces Molecular dynamics NH–π interactions Peptides Phenylalanine Physiological aspects Protein engineering Proteins quantum chemistry side chain interactions Software Solvents Structure X-ray crystallography |
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| Title | Structural Achievability of an NH–π Interaction between Gln and Phe in a Crystal Structure of a Collagen-like Peptide |
| URI | https://www.proquest.com/docview/2728434480/abstract/ https://www.proquest.com/docview/2729523936/abstract/ https://pubmed.ncbi.nlm.nih.gov/PMC9599227 https://doaj.org/article/d95e9857912d4e3a8ac5f1c4877e403e |
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