A simple model for polyproline II structure in unfolded states of alanine-based peptides.
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LEA (late embryogenesis abundant) proteins and their encoding genes in Arabidopsis thalianaA backbone-based theory of protein foldingAssignment of PolyProline II conformation and analysis of sequence--structure relationshipMultivalency in the Assembly of Intrinsically Disordered Dynein Intermediate ChainExploring 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.IMPIPS: the immune protection-inducing protein structure concept in the search for steric-electron and topochemical principles for complete fully-protective chemically synthesised vaccine developmentPhysical-chemical determinants of coil conformations in globular proteins.The polyproline II conformation in short alanine peptides is noncooperativeOrigin of the neighboring residue effect on peptide backbone conformation.Construction and comparison of the statistical coil states of unfolded and intrinsically disordered proteins from nearest-neighbor corrected conformational propensities of short peptides.A novel method reveals that solvent water favors polyproline II over beta-strand conformation in peptides and unfolded proteins: conditional hydrophobic accessible surface area (CHASA).Role of backbone solvation and electrostatics in generating preferred peptide backbone conformations: distributions of phi.Building native protein conformation from highly approximate backbone torsion angles.Hydrogen-bonded turns in proteins: the case for a recount.Polar or apolar--the role of polarity for urea-induced protein denaturationUnusual compactness of a polyproline type II structure.Polyproline II helix conformation in a proline-rich environment: a theoretical study.Measuring unfolding of proteins in the presence of denaturant using fluorescence correlation spectroscopy.Polyproline II conformation is one of many local conformational states and is not an overall conformation of unfolded peptides and proteins.The intrinsic conformational features of amino acids from a protein coil library and their applications in force field development.Toward an accurate theoretical framework for describing ensembles for proteins under strongly denaturing conditionsSecondary structure provides a template for the folding of nearby polypeptides.Preferred peptide backbone conformations in the unfolded state revealed by the structure analysis of alanine-based (AXA) tripeptides in aqueous solution.Is there or isn't there? The case for (and against) residual structure in chemically denatured proteins.Reducing the dimensionality of the protein-folding search problem.Revisiting the Ramachandran plot: hard-sphere repulsion, electrostatics, and H-bonding in the alpha-helix.The relationship between water bridges and the polyproline II conformation: a large-scale analysis of molecular dynamics simulations and crystal structures.Reassessing random-coil statistics in unfolded proteins.Quantum Mechanics Approach to Hydration Energies and Structures of Alanine and Dialanine.Human Antimicrobial Peptides in Bodily Fluids: Current Knowledge and Therapeutic Perspectives in the Postantibiotic Era.Secondary-structure analysis of denatured proteins by vacuum-ultraviolet circular dichroism spectroscopySalt dependence of an alpha-helical peptide folding energy landscapes.A classical molecular dynamics investigation of the free energy and structure of short polyproline conformers.The structure of tri-proline in water probed by polarized Raman, Fourier transform infrared, vibrational circular dichroism, and electric ultraviolet circular dichroism spectroscopy.The polypeptide biophysics of proline/alanine-rich sequences (PAS): Recombinant biopolymers with PEG-like properties.A natively unfolded toxin domain uses its receptor as a folding template.Spectroscopic evidence revealing polyproline II structure in hydrophobic, putatively elastomeric sequences encoded by specific exons of human tropoelastin.Unified perspective on proteins: a physics approach.Conformational distributions of denatured and unstructured proteins are similar to those of 20 × 20 blocked dipeptides.
P2860
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P2860
A simple model for polyproline II structure in unfolded states of alanine-based peptides.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
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2002年學術文章
@zh-hant
name
A simple model for polyproline II structure in unfolded states of alanine-based peptides.
@en
type
label
A simple model for polyproline II structure in unfolded states of alanine-based peptides.
@en
prefLabel
A simple model for polyproline II structure in unfolded states of alanine-based peptides.
@en
P2860
P356
P1433
P1476
A simple model for polyproline II structure in unfolded states of alanine-based peptides.
@en
P2093
George D Rose
Rohit V Pappu
P2860
P304
P356
10.1110/PS.0217402
P577
2002-10-01T00:00:00Z