Folding of protein G B1 domain studied by the conformational characterization of fragments comprising its secondary structure elements.
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Energy landscape of a peptide consisting of alpha-helix, 3(10)-helix, beta-turn, beta-hairpin, and other disordered conformationsCombinatorial pattern discovery approach for the folding trajectory analysis of a beta-hairpin.Assembly of a polytopic membrane protein structure from the solution structures of overlapping peptide fragments of bacteriorhodopsin.The role of a beta-bulge in the folding of the beta-hairpin structure in ubiquitinSequence of events in folding mechanism: beyond the Gō modelThe geometry and efficacy of cation-pi interactions in a diagonal position of a designed beta-hairpin.Measuring the refolding of beta-sheets with different turn sequences on a nanosecond time scale.The free energy landscape for beta hairpin folding in explicit water.Conformational studies of the alpha-helical 28-43 fragment of the B3 domain of the immunoglobulin binding protein G from Streptococcus.Predicting protein folding pathways at the mesoscopic level based on native interactions between secondary structure elements.Conformational studies of the C-terminal 16-amino-acid-residue fragment of the B3 domain of the immunoglobulin binding protein G from Streptococcus.Mechanism of formation of the C-terminal beta-hairpin of the B3 domain of the immunoglobulin-binding protein G from Streptococcus. IV. Implication for the mechanism of folding of the parent protein.Structural order in Pannexin 1 cytoplasmic domainsThe interplay of turn formation and hydrophobic interactions on the early kinetic events in protein folding.Mechanism by which 2,2,2-trifluoroethanol/water mixtures stabilize secondary-structure formation in peptides: a molecular dynamics study.Dynamics and thermodynamics of beta-hairpin assembly: insights from various simulation techniques.Understanding beta-hairpin formation by molecular dynamics simulations of unfolding.Unfolding of globular proteins: monte carlo dynamics of a realistic reduced model.Can a continuum solvent model reproduce the free energy landscape of a beta -hairpin folding in water?Antibacterial activity of human neutrophil defensin HNP-1 analogs without cysteinesHydrophobic aided replica exchange: an efficient algorithm for protein folding in explicit solvent.Long dynamics simulations of proteins using atomistic force fields and a continuum representation of solvent effects: calculation of structural and dynamic properties.Molecular picture of folding of a small alpha/beta protein.Like-charged residues at the ends of oligoalanine sequences might induce a chain reversal.Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy.Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same foldA molecular dynamics study of the 41-56 beta-hairpin from B1 domain of protein GThe role of backbone conformational heat capacity in protein stability: temperature dependent dynamics of the B1 domain of Streptococcal protein G.Transition-path sampling of beta-hairpin folding.Soluble mimics of a chemokine receptor: chemokine binding by receptor elements juxtaposed on a soluble scaffoldA physical basis for protein secondary structure.Characterization of the free-energy landscapes of proteins by NMR-guided metadynamicsInfrared evidence of a beta-hairpin peptide structure in solution.A molecular dynamics simulation study of segment B1 of protein G.Carbohydrate-pi interactions: what are they worth?The origins of asymmetry in the folding transition states of protein L and protein G.Thermodynamic and structural effect of urea and guanidine chloride on the helical and on a hairpin fragment of GB1 from molecular simulations.Kinetic pathways of beta-hairpin (un)folding in explicit solvent.Finding pathways between distant local minima.Predictions suggesting a participation of beta-sheet configuration in the M2 domain of the P2X(7) receptor: a novel conformation?
P2860
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P2860
Folding of protein G B1 domain studied by the conformational characterization of fragments comprising its secondary structure elements.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Folding of protein G B1 domain ...... secondary structure elements.
@ast
Folding of protein G B1 domain ...... secondary structure elements.
@en
type
label
Folding of protein G B1 domain ...... secondary structure elements.
@ast
Folding of protein G B1 domain ...... secondary structure elements.
@en
prefLabel
Folding of protein G B1 domain ...... secondary structure elements.
@ast
Folding of protein G B1 domain ...... secondary structure elements.
@en
P2860
P1433
P1476
Folding of protein G B1 domain ...... secondary structure elements.
@en
P2093
P2860
P304
P356
10.1111/J.1432-1033.1995.TB20605.X
P407
P577
1995-06-01T00:00:00Z