about
The 8 and 5 kDa fragments of plasma gelsolin form amyloid fibrils by a nucleated polymerization mechanism, while the 68 kDa fragment is not amyloidogenicHelix bundle quaternary structure from alpha/beta-peptide foldamersStructural Consequences of β-Amino Acid Preorganization in a Self-Assembling α/β-Peptide: Fundamental Studies of Foldameric Helix BundlesStructural and Energetic Basis of Carbohydrate–Aromatic Packing Interactions in ProteinsCriteria for selecting PEGylation sites on proteins for higher thermodynamic and proteolytic stability.Context-dependent effects of asparagine glycosylation on Pin WW folding kinetics and thermodynamics.N-glycosylation of enhanced aromatic sequons to increase glycoprotein stabilityHow PEGylation influences protein conformational stability.Conjugation Strategy Strongly Impacts the Conformational Stability of a PEG-Protein Conjugate.Impact of site-specific PEGylation on the conformational stability and folding rate of the Pin WW domain depends strongly on PEG oligomer length.Polyethylene Glycol Based Changes to β-Sheet Protein Conformational and Proteolytic Stability Depend on Conjugation Strategy and Location.Stabilizing impact of N-glycosylation on the WW domain depends strongly on the Asn-GlcNAc linkage.An Anion-π Interaction Strongly Stabilizes the β-Sheet Protein WW.Enhancing a long-range salt bridge with intermediate aromatic and nonpolar amino acids.Cys(i)-Lys(i+3)-Lys(i+4) triad: a general approach for PEG-based stabilization of α-helical proteins.Two structural scenarios for protein stabilization by PEG.Bulky Dehydroamino Acids Enhance Proteolytic Stability and Folding in β-Hairpin Peptides.PEGylation near a Patch of Nonpolar Surface Residues Increases the Conformational Stability of the WW DomainInfluence of PEGylation on the Strength of Protein Surface Salt BridgesStapling of two PEGylated side chains increases the conformational stability of the WW domain via an entropic effect
P50
Q24316253-92318D3D-C321-47F5-AEC5-56364E9080EFQ27644076-9BF09261-6896-4C2A-9D74-194FFFA7780AQ27664078-56A53B0C-FD5D-4201-B458-1270C6A443D0Q27678514-71868B6D-2FF9-4FCB-B71C-70B637DEDCA9Q30009279-E096930E-2EE3-440A-B25B-8D30A7A9E33AQ34249680-0C200E12-124D-4D55-A46F-D48BCA88EDEFQ36515262-EA5A08E1-AE1F-4D13-804B-43EE2B92D200Q38942496-8DF8D360-0097-4D9C-9A51-7000539A4767Q41594896-20764824-63EB-4BC9-AE81-9A0921931423Q44455467-08656075-23D6-4B45-90B7-3B8C00ED1B6AQ47708613-2466E705-518B-4D93-BE01-4531C4C00593Q47797028-7B171ABF-B90C-4980-A2EE-ED519510FCE7Q47833805-4182B6FE-C47E-40DC-85DE-24F140DAD317Q47983057-76965405-8DCE-4C2D-A22B-2247BD5040DEQ51036182-788FDA7D-A6A9-406E-A352-6B1AE5215005Q52650152-C166C462-D179-46A2-8F4F-A61F8CF49D54Q53725826-0DA42568-7688-4E81-97BA-2902F5280222Q91365635-4F5B272A-8349-4868-A50E-DAEBB5355F02Q92681790-0A4D7B81-11CF-4493-BD30-8F718EF810C8Q93171425-AD2AE5A0-FC05-4B8A-8EC0-65F6ED307CE1
P50
description
onderzoeker
@nl
researcher, ORCID id # 0000-0002-0116-0968
@en
name
Joshua L Price
@ast
Joshua L Price
@en
Joshua L Price
@es
Joshua L Price
@nl
type
label
Joshua L Price
@ast
Joshua L Price
@en
Joshua L Price
@es
Joshua L Price
@nl
prefLabel
Joshua L Price
@ast
Joshua L Price
@en
Joshua L Price
@es
Joshua L Price
@nl
P106
P31
P496
0000-0002-0116-0968