The role of PII conformations in the calculation of peptide fractional helix content.
about
Post-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivoIdentification of polyproline II regions derived from the proline-rich nuclear receptor coactivators PNRC and PNRC2: new insights for ERα coactivator interactions.Exploring the impact of polyproline II (PII) conformational bias on the binding of peptides to the SEM-5 SH3 domain.The effect of the polyproline II (PPII) conformation on the denatured state entropy.Temperature-induced extended helix/random coil transitions in a group 1 late embryogenesis-abundant protein from soybean.The intrinsically disordered structural platform of the plant defence hub protein RPM1-interacting protein 4 provides insights into its mode of action in the host-pathogen interface and evolution of the nitrate-induced domain protein family.A group 6 late embryogenesis abundant protein from common bean is a disordered protein with extended helical structure and oligomer-forming properties.Multiple protein interactions involving proposed extracellular loop domains of the tight junction protein occludinPolyproline II structure in a sequence of seven alanine residues.A survey of left-handed polyproline II helicesCell-cell membrane fusion induced by p15 fusion-associated small transmembrane (FAST) protein requires a novel fusion peptide motif containing a myristoylated polyproline type II helix.Preferred peptide backbone conformations in the unfolded state revealed by the structure analysis of alanine-based (AXA) tripeptides in aqueous solution.Helix formation and the unfolded state of a 52-residue helical protein.Polyproline II helical structure in protein unfolded states: lysine peptides revisited.Identification of the Abundant Hydroxyproline-Rich Glycoproteins in the Root Walls of Wild-Type Arabidopsis, an ext3 Mutant Line, and Its Phenotypic Revertant.High-order oligomers of intrinsically disordered brain proteins BASP1 and GAP-43 preserve the structural disorder.Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3.Zinc-binding and structural properties of the histidine-rich loop of Arabidopsis thaliana vacuolar membrane zinc transporter MTP1.Three intrinsically unstructured mussel adhesive proteins, mfp-1, mfp-2, and mfp-3: analysis by circular dichroismAnalysis of secondary structure and self-assembly of amelogenin by variable temperature circular dichroism and isothermal titration calorimetry.Ab initio quantum mechanical models of peptide helices and their vibrational spectra.Conformation of a group 2 late embryogenesis abundant protein from soybean. Evidence of poly (L-proline)-type II structure.The structure of tri-proline in water probed by polarized Raman, Fourier transform infrared, vibrational circular dichroism, and electric ultraviolet circular dichroism spectroscopy.CD80 binding polyproline helical peptide inhibits T cell activation.Equilibrium unfolding of neuronal calcium sensor-1: N-terminal myristoylation influences unfolding and reduces protein stiffening in the presence of calcium.Disordered Conformation with Low Pii Helix in Phosphoproteins Orchestrates Biomimetic Apatite Formation.Polyproline II structure is critical for the enzyme protective function of soybean Em (LEA1) conserved domains.A natively unfolded toxin domain uses its receptor as a folding template.Structural investigation of disordered stress proteins. Comparison of full-length dehydrins with isolated peptides of their conserved segments.Pliable natural biocide: Jaburetox is an intrinsically disordered insecticidal and fungicidal polypeptide derived from jack bean urease.
P2860
Q28141258-55FB911B-7FBE-4980-8D62-1410D6D86684Q30009591-F93BE07B-33B3-4CAD-9601-E4A921923CEBQ30157656-6CA1DE1F-1A9D-4925-A095-4FA210287584Q30164889-D88A02DC-48E1-4EC1-B817-507B88541FEBQ30329954-92805048-0ED2-4960-B0F1-01DDAA4A662BQ30364875-472AAE36-186C-40A3-8DAD-7004F6847313Q30367338-F3D1455E-3B03-45A0-AA2F-E82FF294A668Q33734527-3D1CDDF7-A0E9-4E29-BE42-09E488F0393BQ34034318-A5C49FE6-A300-42A2-8B74-8619E81BD585Q34646317-D110DED5-412B-4F9F-934E-A274A24E9F3AQ35728426-4FC720E6-2657-4E46-A0CB-F8267C90597CQ35970945-13D5165F-29BF-4AAB-A363-96C90A19900AQ36526195-C640C915-D8FC-4C9D-B2F9-E0F72C5D69BFQ36639178-A50EF9B0-C385-4B4A-A1B4-B4B6BB4E2944Q36833708-128D623C-C0F3-4569-A619-8C8685CA6415Q39966175-64CD2FFD-8854-4902-8500-03BFE4849C4EQ40896817-65B98C41-E0B2-468F-A6A1-45EF3BDD796DQ41262820-972F97C0-A748-4393-88B8-FBE0470B5F17Q42424692-BB575719-B2FE-44D2-8035-519848BFCDC8Q42537687-7B6FC2C1-7DFE-45C7-8CBD-466E559A5580Q44124039-26CD5DB1-1F0C-4631-B804-931B1985C049Q44367261-712BF021-F5AD-4252-A14E-49E4AB3E1B54Q44667145-6CC871E6-4C3A-428F-90F5-EAF46C0C0A9AQ45186960-1F7C940C-38FD-4287-920C-FD97E5F0AF72Q45256085-6CA6DADB-8220-496E-A893-89C5E4BBD6F0Q46274637-B2192493-6E3F-4D07-B76A-010F09F461FDQ46802129-66FB886F-DD3A-43F6-B37B-8BEB7EF3DE62Q47992335-01F05747-5266-4E8B-A4EB-E574CC16194CQ48094911-B81B48E8-0D87-41DC-A988-127E3B377843Q52789293-35493183-FB60-4C14-85F3-0A316C436C63
P2860
The role of PII conformations in the calculation of peptide fractional helix content.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh
1997年學術文章
@zh-hant
name
The role of PII conformations in the calculation of peptide fractional helix content.
@ast
The role of PII conformations in the calculation of peptide fractional helix content.
@en
type
label
The role of PII conformations in the calculation of peptide fractional helix content.
@ast
The role of PII conformations in the calculation of peptide fractional helix content.
@en
prefLabel
The role of PII conformations in the calculation of peptide fractional helix content.
@ast
The role of PII conformations in the calculation of peptide fractional helix content.
@en
P2093
P2860
P356
P1433
P1476
The role of PII conformations in the calculation of peptide fractional helix content.
@en
P2093
E Stellwagen
W Shalongo
P2860
P304
P356
10.1002/PRO.5560060809
P577
1997-08-01T00:00:00Z