Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models
about
The Contribution of Entropy, Enthalpy, and Hydrophobic Desolvation to Cooperativity in Repeat-Protein FoldingDirect observation of parallel folding pathways revealed using a symmetric repeat protein system.General mechanism of two-state protein folding kinetics.Dissecting the critical factors for thermodynamic stability of modular proteins using molecular modeling approach.Optimization of designed armadillo repeat proteins by molecular dynamics simulations and NMR spectroscopy.Frustration in biomoleculesA disorder-induced domino-like destabilization mechanism governs the folding and functional dynamics of the repeat protein IκBαCapturing coevolutionary signals inrepeat proteins.A Naturally Occurring Repeat Protein with High Internal Sequence Identity Defines a New Class of TPR-like Proteins.Exploring the folding energy landscape of a series of designed consensus tetratricopeptide repeat proteins.Repeat protein engineering: creating functional nanostructures/biomaterials from modular building blocks.GADIS: Algorithm for designing sequences to achieve target secondary structure profiles of intrinsically disordered proteins.Synergistic enhancement of cellulase pairs linked by consensus ankyrin repeats: Determination of the roles of spacing, orientation, and enzyme identity.C-terminal deletion of leucine-rich repeats from YopM reveals a heterogeneous distribution of stability in a cooperatively folded protein.Ising Model Reprogramming of a Repeat Protein's Equilibrium Unfolding Pathway.Insertion of endocellulase catalytic domains into thermostable consensus ankyrin scaffolds: effects on stability and cellulolytic activity.Modulation of the multistate folding of designed TPR proteins through intrinsic and extrinsic factors.Modulating repeat protein stability: the effect of individual helix stability on the collective behavior of the ensemble.Broken TALEs: Transcription Activator-like Effectors Populate Partly Folded States.Removal of a consensus proline is not sufficient to allow tetratricopeptide repeat oligomerization.PyFolding: Open-Source Graphing, Simulation, and Analysis of the Biophysical Properties of Proteins.Extreme stability in de novo-designed repeat arrays is determined by unusually stable short-range interactions
P2860
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P2860
Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models
description
2009 nî lūn-bûn
@nan
2009 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models
@ast
Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models
@en
type
label
Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models
@ast
Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models
@en
prefLabel
Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models
@ast
Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models
@en
P2860
P921
P1476
Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models
@en
P2093
Tural Aksel
P2860
P304
P356
10.1016/S0076-6879(08)04204-3
P407
P50
P577
2009-01-01T00:00:00Z