Favourable native-like helical local interactions can accelerate protein folding.
about
NMR solution structure of the activation domain of human procarboxypeptidase A2Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic powerProtein secondary structure and stability determined by combining exoproteolysis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.Folding propensities of synthetic peptide fragments covering the entire sequence of phage 434 Cro protein.Thermodynamic analysis of helix-engineered forms of the activation domain of human procarboxypeptidase A2.Hydrogen exchange monitored by MALDI-TOF mass spectrometry for rapid characterization of the stability and conformation of proteins.Cloning, sequencing and functional expression of a cDNA encoding porcine pancreatic preprocarboxypeptidase A1.Monitoring disappearance of monomers and generation of resistance to proteolysis during the formation of the activation domain of human procarboxypeptidase A2 (ADA2h) amyloid fibrils by matrix-assisted laser-desorption ionization-time-of-flight-MS.A test of the relationship between sequence and structure in proteins: excision of the heme binding site in apocytochrome b5.Context-independent, temperature-dependent helical propensities for amino acid residues.Experimental evaluation of topological parameters determining protein-folding rates.Protein folding and unfolding in microseconds to nanoseconds by experiment and simulationTransition state heterogeneity in GCN4 coiled coil folding studied by using multisite mutations and crosslinking.Investigation of routes and funnels in protein folding by free energy functional methods.An autonomous folding unit mediates the assembly of two-stranded coiled coilsProtein engineering as a strategy to avoid formation of amyloid fibrilsA conformational equilibrium in a protein fragment caused by two consecutive capping boxes: 1H-, 13C-NMR, and mutational analysis.Synthesis, folding, and structure of the beta-turn mimic modified B1 domain of streptococcal protein G.Native like structure in the unfolded state of the villin headpiece helical subdomain, an ultrafast folding proteinPrediction of a new class of RNA recognition motif.Disulfide driven folding for a conditionally disordered protein.Dynamics of the minimally frustrated helices determine the hierarchical folding of small helical proteins.Unified understanding of folding and binding mechanisms of globular and intrinsically disordered proteins.Intrahelical side chain interactions in alpha-helices: poor correlation between energetics and frequency.Folding and aggregation are selectively influenced by the conformational preferences of the alpha-helices of muscle acylphosphatase.
P2860
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P2860
Favourable native-like helical local interactions can accelerate protein folding.
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
Favourable native-like helical local interactions can accelerate protein folding.
@en
Favourable native-like helical local interactions can accelerate protein folding.
@nl
type
label
Favourable native-like helical local interactions can accelerate protein folding.
@en
Favourable native-like helical local interactions can accelerate protein folding.
@nl
prefLabel
Favourable native-like helical local interactions can accelerate protein folding.
@en
Favourable native-like helical local interactions can accelerate protein folding.
@nl
P1433
P1476
Favourable native-like helical local interactions can accelerate protein folding.
@en
P2093
P356
10.1016/S1359-0278(97)00003-5
P577
1997-01-01T00:00:00Z