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Polyproline Helix | Stereoelectronic effects on polyproline conformation

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The polyproline II helix (PPII) is stabilized by n→π* interactions. The ability to tune PPII structure in water via changes in the electronic properties of the acyl capping group is demonstrated here Hier sollte eine Beschreibung angezeigt werden, diese Seite lässt dies jedoch nicht zu. The polyproline-II (PPII) structure domain is crucial in organisms‘ signal transduction, transcription, cell metabolism, and immune response. It is also a critical structural domain for specific vital disease-associated proteins. Recognizing PPII is essential for understanding protein structure and

Molecular insights into protein synthesis with proline residues

Background: The polyproline II helix (PPIIH) is an extended protein left-handed secondary structure that usually but not necessarily involves prolines. Short PPIIHs are frequently, but not exclusively, found in disordered protein regions, where they Proline is a unique amino acid in that its side-chain is cyclised to the backbone, thus giving proline an exceptional rigidity and a considerably restricted conformational space. Polyproline forms

Super Secondary Structure Consisting of a Polyproline II Helix and a β ...

Abstract The left-handed polyproline II (PPII) helix gives rise to a circular dichroism spectrum that is remarkably similar to that of unfolded proteins. This similarity has been used as the basis for the hypothesis that unfolded proteins possess considerable PPII helical content. It has long been known that homopolymers of lysine adopt the PPII helical conformation at neutral pH, Poly (proline) II helical motifs located at the protein–water interface stabilize the three-dimensional structures of natural proteins. Reported here is the first example of synthetic biomimetic poly (proline)-stabilized polypeptide nanostructures obtained by a straightforward ring-opening polymerization-induced self-assembly (ROPISA) process through consecutive N The poly(Pro)II (PII) conformation is increasingly recognized as an important element in peptide and protein conformation. Circular dichroism (CD) is one of the most useful methods for detecting and characterizing PII. Although the standard exciton-based model for predicting peptide CD spectra works well for α-helices and β-sheets, it fails to reproduce the PII

The polyproline helix type II (PPII) is a regular protein secondary structure with remarkable features. Many studies have highlighted different crucial biological Background: The polyproline II helix (PPIIH) is an extended protein left-handed secondary structure that usually but not necessarily involves prolines. Short PPIIHs are frequently, but not exclusively, found in disordered protein regions, where they may Abstract Multivalent ligands hold promise for enhancing avidity and selectivity to simultaneously target multimeric proteins, as well as potentially modulating receptor signaling in pharmaceutical applications. Essential for these manipulations are nanosized scaffolds that precisely control ligand display patterns, which can be achieved by using polyproline oligo-helix macrocyclic

Proline-rich peptides such as collagen commonly adopt a left-handed helix, the so-called polyproline type II (PPII) helix, despite Pro being a disruptor of the other secondary structures 57, 58, 59.

In proteins, a left-handed polyproline II helix (PPII, poly-Pro II) is formed when sequential residues all adopt (φ,ψ) backbone dihedral angles of roughly (-75°, 150°) and have trans isomers of their peptide bonds. Similarly, a more compact right-handed polyproline I helix (PPI, poly-Pro I) is formed when sequential residues all adopt (φ,ψ) backbone dihedral angles of roughly (-75°, Cell penetrating agents were designed and synthesized that introduce cationic and hydrophobic moieties along the backbone of a Also, peptides with consecutive proline residues fold into a characteristic polyproline helix (P II ‐helix), which constitutes a common protein–protein interaction motif and also endows proteins with unique mechanical properties 3, 4.

Stereoelectronic effects on polyproline conformation

  • Polyproline II structure in a sequence of seven alanine residues
  • Stereoelectronic effects on polyproline conformation
  • Hélice polyproline — Wikipédia

About half of the globular proteins are composed of regular secondary structures, α- helices and β-sheets while the rest are constituted of irregular secondary structures such as turns or coil conformations. Other regular secondary structures are often ignored, despite their importance in biological processes. Among such structures, the polyproline II helix (PPII) has interesting Interest centers here on whether a polyproline II helix can propagate through adjacent non-proline residues, and on shedding light on recent experimental observations suggesting the presence of significant PPII structure in a short alanine-based peptide with no proline in the sequence. PolyProline II (PPII) helix is yet another interesting repetitive structure which is less frequent and not usually associated with stabilizing interactions. Recent studies have shown that PPII frequency is higher than expected, and they could have an important role in protein – protein interactions.

In proteins, a left-handed polyproline II helix (PPII, poly-Pro II) is formed when sequential residues all adopt (φ,ψ) backbone dihedral angles of roughly (-75°, 150°) and have trans isomers of their peptide bonds. Similarly, a more compact right-handed polyproline I helix (PPI, poly-Pro I) is formed when sequential residues all adopt (φ,ψ) backbone dihedral angles of roughly (-75°,

The ability to rationally design biomaterials to form desired supramolecular constructs presents an ever-growing research field, with many burgeoning works within recent years providing exciting results; however, there exists a broad expanse of promising avenues of research yet to be investigated. As such we have set out to make use of the polyproline helix

(PDF) Super Secondary Structure Consisting of a Polyproline II Helix ...

The structure of the proline amino acid allows folded polyproline peptides to exist as both left- (PPII) and right-handed (PPI) helices. We have Interest centers here on whether a polyproline II helix can propagate through adjacent non-proline residues, and on shedding light on recent experimental observations suggesting the presence of significant PPII structure in a short alanine-based In the past 20 years, several proteins with domains composed of glycine-rich polyproline II helix bundles have been uncovered, but the basis of their conformational stability is still not

Polyproline II (PPII) peptide sequences are recognized as promising biomaterials because of their attractive antifouling properties. However, the mechanisms behind their antifouling behavior have not been fully characterized. In this work we show that PPII peptide coverage, controlled by adsorption time, significantly reduces the fouling of bovine serum 聚脯氨酸螺旋 是由重複的 脯氨酸 殘基構成的一種 蛋白質 二級結構。 [1] 當連續的殘基與主鏈的 二面角 （φ,ψ）都大約為（-75°, 150°），並且它們的 肽鍵 是 反式 構型時，就會形成左旋的 聚脯氨酸II型螺旋 （PPII， 聚-脯II）。除了脯氨酸以外的其他胺基酸的蛋白質和多肽中也常見這種PPII構 A polyproline helix is a type of protein secondary structure which occurs in proteins comprising repeating proline residues. A left-handed polyproline II helix (PPII, poly-Pro II, κ-helix) is formed when sequential residues all adopt (φ,ψ) backbone dihedral angles of roughly (-75°, 150°) and have trans isomers of their peptide bonds. This PPII conformation is also common in

Polyprolines are well known for adopting a regular polyproline type II helix in aqueous solution, rendering them a popular standard as molecular ru Secondary structure elements often mediate protein-protein interactions. Despite their low abundance in folded proteins, polyproline II (PPII) and its variant, the triple helix, are frequently involved in protein-protein interactions, likely due to their

PolyprOnline: polyproline helix II and secondary structure

Classical descriptions of the three-dimensional shapes of proteins usually invoke three main structures: α-helix, β-sheet, and β-turn. More recently, the polyproline II (PPII) structure has been implicated in diverse biological activities including signal transduction, transcription, cell motility, and immune response. Concurrently, evidence is accumulating that

Hélice polyproline de type I Vue latérale d’une hélice PP I, illustrant sa plus grande compacité. L’hélice polyproline de type I est bien plus dense que l’hélice polyproline II en raison de la configuration cis de ses liaisons peptidiques.

Here we investigate high molecular weight polyproline as an ice recrystallization inhibitor (IRI). Low molecular weight polyproline is known to be a weak IRI. Its activity is hypothesized to be due to the unique PPI helix it adopts, but it has not been thoroughly investigated.

Aromatic rings exhibit defined interactions via the unique aromatic π face. Aromatic amino acids interact favorably with proline residues via both the hydrophobic effect and aromatic–proline interactions, C−H/π interactions between the aromatic π face and proline ring C–H bonds. The canonical aromatic amino acids Trp, Tyr, and Phe strongly disfavor a In both structures, a polyproline II helix and an α-helix combine to form an unusual tertiary structure in which Pro residues from the former dock into holes formed by regularly spaced aromatic

聚脯氨酸螺旋 是由重复的 脯氨酸 残基构成的一种 蛋白质 二级结构。 [1] 当连续的残基与主链的 二面角 （φ,ψ）都大约为（-75°, 150°），并且它们的 肽键 是 反式 构型时，就会形成左旋的 聚脯氨酸II型螺旋 （PPII， 聚-脯II）。除了脯氨酸以外的其他氨基酸的蛋白质和多肽中也常见这种PPII构