Cargando…

Assessing the Effect of Loop Mutations in the Folding Space of β(2)-Microglobulin with Molecular Dynamics Simulations

We use molecular dynamics simulations of a full atomistic Gō model to explore the impact of selected DE-loop mutations (D59P and W60C) on the folding space of protein human β(2)-microglobulin (Hβ(2)m), the causing agent of dialysis-related amyloidosis, a conformational disorder characterized by the...

Descripción completa

Detalles Bibliográficos
Autores principales:	Estácio, Sílvia G., Shakhnovich, Eugene I., Faísca, Patrícia F. N.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	MDPI 2013
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3794727/ https://www.ncbi.nlm.nih.gov/pubmed/23975166 http://dx.doi.org/10.3390/ijms140917256

Ejemplares similares

A Simulated Intermediate State for Folding and Aggregation Provides Insights into ΔN6 β(2)-Microglobulin Amyloidogenic Behavior
por: Estácio, Sílvia G., et al.
Publicado: (2014)

The Early Phase of β2-Microglobulin Aggregation: Perspectives From Molecular Simulations
por: Loureiro, Rui J. S., et al.
Publicado: (2020)

Interfacial Dynamics and Growth Modes of β(2)-Microglobulin Dimers
por: Oliveira, Nuno F. B., et al.
Publicado: (2023)

Catalysis of Protein Folding by Chaperones Accelerates Evolutionary Dynamics in Adapting Cell Populations
por: Çetinbaş, Murat, et al.
Publicado: (2013)

Disease-relevant β(2)-microglobulin variants share a common amyloid fold
por: Wilkinson, Martin, et al.
Publicado: (2023)

Loosening of Side-Chain Packing Associated with Perturbations in Peripheral Dynamics Induced by the D76N Mutation of β(2)-Microglobulin Revealed by Pressure-NMR and Molecular Dynamic Simulations
por: Sakurai, Kazumasa, et al.
Publicado: (2019)

Evidence of evolutionary selection for cotranslational folding
por: Jacobs, William M., et al.
Publicado: (2017)

Structure, Folding Dynamics, and Amyloidogenesis of D76N β(2)-Microglobulin: ROLES OF SHEAR FLOW, HYDROPHOBIC SURFACES, AND α-CRYSTALLIN
por: Mangione, P. Patrizia, et al.
Publicado: (2013)

Structure-Based Prediction of Protein-Folding Transition Paths
por: Jacobs, William M., et al.
Publicado: (2016)

Predicting stable binding modes from simulated dimers of the D76N mutant of [Formula: see text] 2-microglobulin
por: Oliveira, Nuno F.B., et al.
Publicado: (2021)

A First-Principles Model of Early Evolution: Emergence of Gene Families, Species, and Preferred Protein Folds
por: Zeldovich, Konstantin B, et al.
Publicado: (2007)

Validation of DBFOLD: An efficient algorithm for computing folding pathways of complex proteins
por: Bitran, Amir, et al.
Publicado: (2020)

The Early Phase of β2m Aggregation: An Integrative Computational Study Framed on the D76N Mutant and the ΔN6 Variant
por: J. S. Loureiro, Rui, et al.
Publicado: (2019)

Contribution of Selection for Protein Folding Stability in Shaping the Patterns of Polymorphisms in Coding Regions
por: Serohijos, Adrian W.R., et al.
Publicado: (2014)

Assessing the effect of dynamics on the closed-loop protein-folding hypothesis
por: Chintapalli, Sree V., et al.
Publicado: (2014)

Clinical Images: β(2)‐Microglobulin amyloidosis
por: Ștefan, Gabriel, et al.
Publicado: (2021)

Molecular Dynamics Simulations of Matrix Metalloproteinase 13 and the Analysis of the Specificity Loop and the S1′−Site
por: Choi, Jun Yong, et al.
Publicado: (2023)

Mechanism of collagen folding propagation studied by Molecular Dynamics simulations
por: Hartmann, Julian, et al.
Publicado: (2021)

Low-Resolution Models for the Interaction Dynamics of Coated Gold Nanoparticles with β2-microglobulin
por: Brancolini, Giorgia, et al.
Publicado: (2019)

Insights into the Folding and Unfolding Processes of Wild-Type and Mutated SH3 Domain by Molecular Dynamics and Replica Exchange Molecular Dynamics Simulations
por: Chu, Wen-Ting, et al.
Publicado: (2013)

The two tryptophans of β2-microglobulin have distinct roles in function and folding and might represent two independent responses to evolutionary pressure
por: Raimondi, Sara, et al.
Publicado: (2011)

Influence of heparin molecular size on the induction of C- terminal unfolding in β2-microglobulin
por: Fukasawa, Kanon, et al.
Publicado: (2016)

Wild Type Beta-2 Microglobulin and DE Loop Mutants Display a Common Fibrillar Architecture
por: Natalello, Antonino, et al.
Publicado: (2015)

Intermolecular Alignment in β(2)-Microglobulin Amyloid Fibrils
por: Debelouchina, Galia T., et al.
Publicado: (2010)

Systemic Amyloidosis: Lessons from β(2)-Microglobulin
por: Stoppini, Monica, et al.
Publicado: (2015)

Tiling Nussinov’s RNA folding loop nest with a space-time approach
por: Palkowski, Marek, et al.
Publicado: (2019)

How Difficult Is It to Fold a Knotted Protein? In Silico Insights from Surface-Tethered Folding Experiments
por: Soler, Miguel A., et al.
Publicado: (2012)

Effects of Knots on Protein Folding Properties
por: Soler, Miguel A., et al.
Publicado: (2013)

Accelerated Molecular Dynamics Simulation for Helical Proteins Folding in Explicit Water
por: Duan, Lili, et al.
Publicado: (2019)

Molecular insights into cell toxicity of a novel familial amyloidogenic variant of β2‐microglobulin
por: Leri, Manuela, et al.
Publicado: (2016)

β(2)-microglobulin–deficient Mice Are Resistant to Bullous Pemphigoid
por: Liu, Zhi, et al.
Publicado: (1997)

THE SMALL SUBUNIT OF HL-A ANTIGENS IS β2-MICROGLOBULIN
por: Grey, Howard M., et al.
Publicado: (1973)

Ochratoxin A and β2-Microglobulin in BEN Patients and Controls
por: Yordanova, Pavlina, et al.
Publicado: (2010)

Understanding the complex mechanisms of β(2)-microglobulin amyloid assembly
por: Eichner, Timo, et al.
Publicado: (2011)

Structural and Thermodynamic Characteristics of Amyloidogenic Intermediates of β-2-Microglobulin
por: Chong, Song-Ho, et al.
Publicado: (2015)

Impacts of Mutations in the P-Loop on Conformational Alterations of KRAS Investigated with Gaussian Accelerated Molecular Dynamics Simulations
por: Shi, Shuhua, et al.
Publicado: (2023)

Characterization of RNA polymerase II trigger loop mutations using molecular dynamics simulations and machine learning
por: Dutagaci, Bercem, et al.
Publicado: (2023)

Capturing RNA Folding Free Energy with Coarse-Grained Molecular Dynamics Simulations
por: Bell, David R., et al.
Publicado: (2017)

Molecular Dynamics Simulation as a Tool to Identify Mutual Synergistic Folding Proteins
por: Magyar, Csaba, et al.
Publicado: (2023)

Optimality of Mutation and Selection in Germinal Centers
por: Zhang, Jingshan, et al.
Publicado: (2010)

Cannot write session to /tmp/vufind_sessions/sess_muvesh91q3dj6rpaevk276n2t8