Backbone-Backbone H-Bonds Make Context-Dependent Contributions to Protein Folding Kinetics and Thermodynamics: Lessons from Amide-to-Ester Mutations.
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Interplay among side chain sequence, backbone composition, and residue rigidification in polypeptide folding and assemblyStructural Consequences of β-Amino Acid Preorganization in a Self-Assembling α/β-Peptide: Fundamental Studies of Foldameric Helix BundlesUsing protein backbone mutagenesis to dissect the link between ion occupancy and C-type inactivation in K+ channelsContribution of hydrogen bonds to protein stabilityConsecutive isocyanide-based multicomponent reactions: synthesis of cyclic pentadepsipeptoids.Sub-nanoscale surface ruggedness provides a water-tight seal for exposed regions in soluble protein structure.Influence of hPin1 WW N-terminal domain boundaries on function, protein stability, and foldingThe role of backbone hydrogen bonds in the transition state for protein folding of a PDZ domain.Native chemical ligation of thioamide-containing peptides: development and application to the synthesis of labeled α-synuclein for misfolding studiesIndividual Ion Binding Sites in the K(+) Channel Play Distinct Roles in C-type Inactivation and in Recovery from Inactivation.Localized thermodynamic coupling between hydrogen bonding and microenvironment polarity substantially stabilizes proteins.Probing the folding transition state structure of the villin headpiece subdomain via side chain and backbone mutagenesis.An evaluation of peptide-bond isosteres.Forces stabilizing proteinsToward quantification of protein backbone-backbone hydrogen bonding energies: An energetic analysis of an amide-to-ester mutation in an alpha-helix within a protein.Surveying the sequence diversity of model prebiotic peptides by mass spectrometry.Amide-to-ester substitution allows fine-tuning of the cyclopeptide conformational ensemble.Design and Synthesis of Peptide YY Analogues with C-terminal Backbone Amide-to-Ester Modifications.Effects of cyclic lipodepsipeptide structural modulation on stability, antibacterial activity, and human cell toxicity.Amide-to-E-olefin versus amide-to-ester backbone H-bond perturbations: Evaluating the O-O repulsion for extracting H-bond energies.Contribution of hydrophobic interactions to protein stability.Sequence determinants of thermodynamic stability in a WW domain--an all-beta-sheet protein.Using Cooperatively Folded Peptides To Measure Interaction Energies and Conformational Propensities.Probing backbone hydrogen bonding in PDZ/ligand interactions by protein amide-to-ester mutations.Effects of isosteric substitutions on the conformational preference and cis–trans isomerization of proline-containing peptides
P2860
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P2860
Backbone-Backbone H-Bonds Make Context-Dependent Contributions to Protein Folding Kinetics and Thermodynamics: Lessons from Amide-to-Ester Mutations.
description
2005 nî lūn-bûn
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2005年の論文
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2005年学术文章
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2005年学术文章
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2005年学术文章
@zh-hans
2005年学术文章
@zh-my
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@zh-sg
2005年學術文章
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name
Backbone-Backbone H-Bonds Make ...... from Amide-to-Ester Mutations.
@ast
Backbone-Backbone H-Bonds Make ...... from Amide-to-Ester Mutations.
@en
type
label
Backbone-Backbone H-Bonds Make ...... from Amide-to-Ester Mutations.
@ast
Backbone-Backbone H-Bonds Make ...... from Amide-to-Ester Mutations.
@en
prefLabel
Backbone-Backbone H-Bonds Make ...... from Amide-to-Ester Mutations.
@ast
Backbone-Backbone H-Bonds Make ...... from Amide-to-Ester Mutations.
@en
P1476
Backbone-Backbone H-Bonds Make ...... from Amide-to-Ester Mutations
@en
P2093
Songpon Deechongkit
P356
10.1016/S0065-3233(05)72002-7
P577
2005-01-01T00:00:00Z