proline peptide bond Pro incorporates in translation significantly more slowly than Phe or Ala - Glycine have been found to be hydrolyzed during exposure to low pH values The Unique Nature of the Proline Peptide Bond: Structure, Kinetics, and Biological Significance

Proline中文 The proline peptide bond occupies a unique position within the realm of protein chemistry, primarily due to proline's distinct structural characteristics作者：G Vanhoof·1995·被引用次数：623—When present inside an a-helix,prolinealso sterically prevents the amide nitrogen of its C-terminal neighbor from making a hydrogenbondwith a carbonyl in.. As the only proteinogenic amino acid that is a secondary amine, proline’s nitrogen atom is incorporated into a five-membered pyrrolidine ring, creating a rigid structure that significantly influences protein folding and function. This structural anomaly means that proline, unlike other amino acids, does not have a hydrogen on the α amino group, a feature that prevents it from donating a hydrogen bond, a crucial interaction for stabilizing secondary structures like α-helices and β-sheets.

This unique structure has profound implications for the formation and behavior of the proline peptide bond.Proline While most peptide bonds predominantly adopt the *trans* conformation, the proline amide bond can exist in both *cis* and *trans* isomersProline - Amino Acids. This conformational flexibility, or lack thereof in some contexts, is a key factor in protein folding kinetics. The isomerization of the proline peptide bond is widely recognized as a non-covalent modification of peptide backbone and a significant kinetic bottleneck in protein foldingSlow peptide bond formation by proline and other N ... - PubMed. This process is amplified in proteins that are rich in proline residues, as the energy barrier for rotation around the proline peptide bond is higher compared to other amino acids. Studies have shown that Pro incorporates in translation significantly more slowly than Phe or Ala, highlighting the kinetic challenges associated with proline incorporation into a growing polypeptide chain.Molecular insights into protein synthesis with proline residues - PMC

The cis/trans isomerization of proline peptide bonds is not merely a structural curiosity; it plays vital roles in biological processesAnomalous cleavage of aspartyl-proline peptide bonds .... For instance, the isomerization of the proline peptide bond between specific residues, such as tyrosine-92 and proline-93 in bovine pancreatic ribonuclease A, has been investigated in the context of protein unfolding. This isomerization can influence the rate at which proteins attain their functional three-dimensional structures.Proline Furthermore, the presence of proline residues confers unique structural constraints on peptide chains, markedly influencing the susceptibility of proximal peptide bonds to protease activity.作者：MD Farahani·2014·被引用次数：19—Proline residues are important inducers of peptide folding, yielding secondary structures with β-turn or alpha helix character. The proline ... This characteristic has led to the development of specific assays, such as Chemical Cleavage of Proline Peptide Bonds, to study peptide structure and processing.

The conformational preferences around proline are also influenced by the surrounding amino acids and the overall peptide environment. For example, loop formation tends to be significantly slower around trans prolyl peptide bonds and faster around glycine residues compared to any other amino acidPharmacokinetics, distribution, metabolism, and excretion of body .... This differential behavior underscores the importance of proline in dictating the dynamic properties of proteins. The isomers of peptide bonds in proline containing molecules can also be influenced by factors like pyrrolidine puckering changes, which can lower the isomerization barrier.

Beyond its role in protein structure and folding, proline itself is an amino acid obtained by hydrolysis of proteins and holds significance in various biological contexts. The proline amide bond can also exist in trans or cis conformations, and this conformational duality is critical for molecular recognition and signaling pathways.Role of proline peptide bond isomerization in unfolding ... The unique covalent bond between the backbone nitrogen and the proline side chain, forming a five-membered ring, is fundamental to its chemical properties. Research continues to explore the implications of proline, including its derivatives and analogs, in modulating biological functions作者：MD Farahani·2014·被引用次数：19—Proline residues are important inducers of peptide folding, yielding secondary structures with β-turn or alpha helix character. The proline .... For example, proline residues are recognized as important inducers of peptide folding, contributing to secondary structures with β-turn or alpha helix character作者：MD Farahani·2014·被引用次数：19—Proline residues are important inducers of peptide folding, yielding secondary structures with β-turn or alpha helix character. The proline ....

The study of proline's behavior in peptide chains extends to understanding its interaction with other moleculesProline Isomerization: From the Chemistry and Biology ... - PMC. Advanced computational tools, such as the AlphaFold Server, which provides accurate structure predictions for how proteins interact with other molecules, are instrumental in unraveling the complex roles of proline in protein structure and function.作者：J Alcantara·2021·被引用次数：17—Proline is a unique amino acid due to the covalent bondbetween the backbone nitrogen and the proline side chain. The resulting five-membered ring allows ... Furthermore, the peculiar nature of the proline peptide bond means it can be hydrolyzed under specific conditions, such as exposure to low pH values, where other aspartyl bonds remain stable, a phenomenon observed in anomalous cleavage of aspartyl-proline peptide bonds. Understanding these unique characteristics is crucial for fields ranging from biochemistry and molecular biology to drug design and materials science, where precise control over peptide and protein structure and dynamics is paramountMolecular insights into protein synthesis with proline residues - PMC. The ability of proline to contribute its amino group to bond formation in a manner distinct from other amino acids cements its status as a key player in the intricate world of biomolecular architecture.Cis/trans isomerization of proline peptide bonds in the ...