curcumin-peptide The peptide hydrogen bond is a fundamental interaction critical for the structure, stability, and function of peptides and proteins.作者：H Gong·2010·被引用次数：29—When the protein is folded, these groups form approximatelytwo hydrogen bonds per peptide unit, one donor or acceptor for each carbonyl oxygen or amide ... These non-covalent bonds, formed between a hydrogen atom covalently bonded to an electronegative atom (like nitrogen or oxygen) and another electronegative atom, play a pivotal role in dictating the three-dimensional conformations of biomolecules.I understand thathydrogen bonds form between polar side chains of amino acidsto help stabilize the tertiary structure of a polypeptide chain. Understanding the nature and strength of peptide hydrogen bonds is essential for comprehending protein folding, molecular recognition, and the development of novel peptide-based materials.
A peptide bond itself is an amide linkage formed between the carboxyl group of one amino acid and the amino group of another, releasing a molecule of water. While the peptide bond itself is a covalent linkage, the atoms within the peptide backbone and side chains possess polar characteristics that enable hydrogen bonding.Peptide bond | chemistry Specifically, the carbonyl oxygen (C=O) of one peptide bond acts as a hydrogen bond acceptor, while the amide hydrogen (N-H) of another peptide bond serves as a hydrogen bond donorIntramolecular H-bonds govern the recognition of a flexible .... This recurring pattern is central to the formation of secondary structures like alpha-helices and beta-sheets, where extensive hydrogen bonding networks stabilize these ordered arrangements作者：RL Baldwin·2003·被引用次数：171—Because thepeptideCO and NH groups form competinghydrogen bonds(H-bonds) to water when a protein is unfolded it was evident, however, ....
Beyond the backbone, amino acid side chains also participate in hydrogen bonding. For instance, hydroxyl groups in serine and threonine, and the amino groups in lysine, can act as both donors and acceptors, contributing to the intricate hydrogen bond landscape within a peptide or proteinPeptide bond contains partial positive charge groups(polar hydrogen atoms of amino groups) and partial negative charge groups (polar oxygen atoms of carboxyl .... These interactions, though individually weak compared to covalent bonds, collectively provide significant stability.
The significance of peptide hydrogen bonds is most evident in their role in stabilizing protein secondary structures.Types of Chemical Bonds in Proteins: In an alpha-helix, hydrogen bonds form between the carbonyl oxygen of an amino acid and the amide hydrogen of the amino acid four residues ahead in the sequence.How strong are hydrogen bonds in the peptide model? In a beta-sheet, hydrogen bonds form between adjacent polypeptide strands, either parallel or antiparallel to each other. These ordered structures are the building blocks of the overall protein architecture.Apparently, a significant role for the phenolic sidechain of Tyr97 is the formation of ahydrogen bondthat raises the barrier to prolylpeptidebond ...
Furthermore, intramolecular H-bonds can greatly influence the binding affinity of peptides, sometimes by up to 2 kcal/mol of free energy. In unfolded proteins, peptide groups form competing hydrogen bonds with water molecules. The transition to a folded state involves the formation of internal hydrogen bonds, which are energetically favorable and contribute to the protein's stable conformation. The strength and geometry of these hydrogen bonds are crucial for maintaining the correct protein fold, and disruptions can lead to misfolding and loss of function, as seen in various diseases.
Recent research has explored novel applications leveraging the properties of peptide hydrogen bonds. For example, peptide hydrogen-bonded organic frameworks (P-HPFs) are being developed for applications such as gas storage, utilizing the self-assembly of peptides driven by intermolecular hydrogen bond networksHydrogen-Bond-Driven Peptide Nanotube Formation. Researchers are also investigating various types of hydrogen bonds, including bifurcated hydrogen bonds, to understand their impact on crystal structures and material properties.作者：SY Sheu·2003·被引用次数：469—Hydrogen bonds and their relative strengths in proteinsare of importance for understanding protein structure and protein motions. The correct strength of ...
The study of hydrogen bonding in peptides also extends to understanding their behavior in different environments, such as their interactions with waterHydrogen Bonding Stiffens Peptide Amphiphile .... The strength of these interactions can influence the peptide's conformation and biological activity. For instance, in aqueous solutions, hydrogen bonds can be insufficient for stabilizing specific peptide conformations, leading to reduced biological activity unless the conformation is otherwise constrained作者：S Shekhar·2024—The main chainhydrogen bonds(H-bonds) are one of the fundamental non-covalent interactions that stabilize protein andpeptidesecondary ....
The peptide hydrogen bond is a cornerstone of molecular biology, underpinning the structural integrity and functional capabilities of peptides and proteins.作者：T Vijayakanth·2024·被引用次数：42—This review highlights recent developments in P-HPFs using ultra-shortpeptides, foldedpeptides, and foldamers, showcasing their utility for gas storage. From dictating secondary structures to influencing binding affinities and enabling the design of novel materials, these seemingly weak interactions exert a profound influence.作者：L Russo·2025—Here, we provide direct NMR spectroscopic evidence for the existence of anNH-π interaction in an intrinsically disordered peptide(E22G-Aβ40). Continued research into the energetics, geometry, and diverse roles of peptide hydrogen bonds promises to deepen our understanding of biological systems and unlock new avenues for technological innovation.Types of Chemical Bonds in Proteins:
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