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Type of protein secondary structure
polyproline helix is a type of protein secondary structure which occurs in proteins comprising repeating proline residues. A left-handed polyproline II
Polyproline_helix
Set of three congruent geometrical helices with the same axis
helix is made of three collagen peptides, each of which forms its own left-handed polyproline helix. When the three chains combine, the triple helix adopts
Triple_helix
Chemical compound
chain. Multiple prolines and/or hydroxyprolines in a row can create a polyproline helix, the predominant secondary structure in collagen. The hydroxylation
Proline
General three-dimensional form of local segments of proteins
unfavorable backbone packing in the center of the helix. Other extended structures such as the polyproline helix and alpha sheet are rare in native state proteins
Protein_secondary_structure
Insect protein
structure exon 1 and exon 3 corresponding peptides may take on is the polyproline helix (PPII), indicated by the high occurrence of proline and glycine in
Resilin
Most abundant structural protein in animals
Amino acids are bound together to form a triple helix of elongated fibril known as a collagen helix. It is mostly found in cartilage, bones, tendons
Collagen
Croatian chemist
his co-worker Vladimir Kubyshkin, the new-to-nature hydrophobic polyproline-II helix foldamer was designed. Along with Budisa's previous work on bioexpression
Nediljko_Budisa
Primary cholinesterase in the body
FASCICULIN-II 1vzj: STRUCTURE OF THE TETRAMERIZATION DOMAIN OF ACETYLCHOLINESTERASE: FOUR-FOLD INTERACTION OF A WWW MOTIF WITH A LEFT-HANDED POLYPROLINE HELIX
Acetylcholinesterase
located from P185 to P188 has the secondary structure of a type II polyproline helix. This gene is found in primates but is also found at a very poor E-values
C2orf27
Topics referred to by the same term
PPI may refer to: PPi, the anion P2O74−, a pyrophosphate Polyproline I helix Protein–protein interaction Patient and public involvement Prepulse inhibition
PPI
Protein-coding gene in the species Homo sapiens
interesting secondary structure as a cluster of proline can form a polyproline helix. PRR12 contains a possible nuclear import signal starting at P1794
Proline-rich_12
Class of proteins
Proline-Rich 12, Proline-Rich Protein 30, and Proline-Rich Protein 21. Polyproline helix SH3 domain Canon, Francis; Paté, Franck; Meudec, Emmanuelle; Marlin
Proline_rich_protein
Small motifs in proteins and polypeptides
the polypeptide has the conformation of beta sheet or of type II polyproline helix (PPII). A number of glutamines and asparagines help bind short peptides
Amide_ring
Class of enzymes
domains. Binding of the enzyme to the thylakoid membrane involves a polyproline type II helix created between two FNR monomers and several proline rich integral
Ferredoxin—NADP(+)_reductase
Type of synthetic peptide
share the defining structural feature known as the triple helix, where three left handed polyproline II-type (PPII) helices assemble to form a right-handed
Collagen_hybridizing_peptide
Polymers of N-substituted glycines
C-α-branched side chains are known to adopt structure analogous to polyproline I helix. Different strategies have been employed to predict and characterize
Peptoid
Visual representation of allowable protein conformations
most common regions are labeled: α for α helix, Lα for left-handed helix, β for β-sheet, and ppII for polyproline II. Such a clustering is alternatively
Ramachandran_plot
Protein spanning across a biological membrane
dimeric transmembrane β-helix. This peptide is secreted by gram-positive bacteria as an antibiotic. A transmembrane polyproline-II helix has not been reported
Transmembrane_protein
Chain molecule which folds in predictable ways while in solution
N-substituted polyglycines that utilize steric interactions to fold into polyproline type-I-like helical structures. Aedamers that fold in aqueous solutions
Foldamer
monomers are soluble and contain short regions of beta sheet and polyproline II helix secondary structures in solution, though they are largely alpha helical
Biochemistry of Alzheimer's disease
Biochemistry_of_Alzheimer's_disease
Stinging cell used by cnidarians
short genes containing the characteristic collagen-triple helix sequence, as well as polyproline domains and cysteine-rich domains. Trimeres of mini collagen
Cnidocyte
research on synthetic peptides derived from abductin were found to have polyproline II helix structure in aqueous solutions and type II β-turn structure in hydrophobic
Abductin
Protein-coding gene in humans
"The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix". EMBO J. 23 (22): 4394–405. doi:10.1038/sj.emboj.7600425. PMC 526459
COLQ
Class of kinase enzymes
residues) and binds proline-containing sequences capable of forming a polyproline type II helix. Some nRTKs without SH2 and SH3 domains possess some subfamily-specific
Non-receptor_tyrosine_kinase
Unusual regions in protein sequences
2020-11-03. Adzhubei AA, Sternberg MJ, Makarov AA (June 2013). "Polyproline-II Helix in Proteins: Structure and Function". Journal of Molecular Biology
Low complexity regions in proteins
Low_complexity_regions_in_proteins
Class of peptides which help cells survive freezing conditions
any amino acid. Each 3-amino-acid repeat forms one turn of a polyproline type II helix. The helices then fold together, to form a bundle that is two
Antifreeze_protein
Protein domain
ligands. A subset of WH1 domains has been termed the EVH1 domain bind a polyproline motif. The EVH1 domain (also known as the WH1, RanBP1-WASP, or enabled/VASP
WH1_domain
Chemical compound
receptor by Pro-Leu-Gly-NH2 peptidomimetics constrained in either a polyproline II helix or a type II beta-turn conformation". Journal of Medicinal Chemistry
Melanocyte-inhibiting_factor
Protein-coding gene in the species Homo sapiens
in motility and invasion. The SH3 domain is a point of contact with polyproline sequences on focal adhesion kinase (FAK). or the related kinase PTK2B
Embryonal fyn-associated substrate
Embryonal_fyn-associated_substrate
Protein found in humans
MLXIP) and ChREBP (MondoB, MLXIPL). Both are characterized by a basic helix-loop-helix leucine zipper (bHLH-ZIP) structure, and form heterodimers with MLX
Carbohydrate-responsive element-binding protein
Carbohydrate-responsive_element-binding_protein
1961 scientific experiment instrumental in deciphering the genetic code
with other synthetic RNAs, they found that poly-C directed synthesis of polyproline. Nirenberg recounts that the labs of Severo Ochoa and James Watson had
Nirenberg and Matthaei experiment
Nirenberg_and_Matthaei_experiment
Protein found in humans
LIM 4 domains of paxillin are required for the association to a novel polyproline region (Pro 2) of protein-tyrosine phosphatase-PEST". The Journal of
Paxillin
Protein-coding gene in the species Homo sapiens
This highly conserved N-terminal domain mediates NEDD9 binding to the polyproline motifs of a number of important interacting proteins, with some well-studied
NEDD9
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