Search Results - "Ham, Sihyun"

Distinct Role of Hydration Water in Protein Misfolding and Aggregation Revealed by Fluctuating Thermodynamics Analysis by Chong, Song-Ho, Ham, Sihyun

“…Protein aggregation in aqueous cellular environments is linked to diverse human diseases. Protein aggregation proceeds through a multistep process initiated by…”
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Effect of linker on the binding free energy of stapled p53/HDM2 complex by Im, Haeri, Ham, Sihyun

“…Inactivation of the tumor suppressor p53 resulting from the binding with a negative regulator HDM2 is among the predominant defects in human cancers…”
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Folding Free Energy Landscape of Ordered and Intrinsically Disordered Proteins by Chong, Song-Ho, Ham, Sihyun

“…Folding funnel is the essential concept of the free energy landscape for ordered proteins. How does this concept apply to intrinsically disordered proteins…”
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Dynamics of Hydration Water Plays a Key Role in Determining the Binding Thermodynamics of Protein Complexes by Chong, Song-Ho, Ham, Sihyun

“…Interfacial waters are considered to play a crucial role in protein–protein interactions, but in what sense and why are they important? Here, using molecular…”
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Impact of chemical heterogeneity on protein self-assembly in water by Chong, Song-Ho, Ham, Sihyun

“…Hydrophobicity is thought to underlie self-assembly in biological systems. However, the protein surface comprises hydrophobic and hydrophilic patches, and…”
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Anomalous Dynamics of Water Confined in Protein–Protein and Protein–DNA Interfaces by Chong, Song-Ho, Ham, Sihyun

“…Confined water often exhibits anomalous properties not observable in the bulk phase. Although water in hydrophobic confinement has been the focus of intense…”
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Structure of Full-Length SMC and Rearrangements Required for Chromosome Organization by Diebold-Durand, Marie-Laure, Lee, Hansol, Ruiz Avila, Laura B., Noh, Haemin, Shin, Ho-Chul, Im, Haeri, Bock, Florian P., Bürmann, Frank, Durand, Alexandre, Basfeld, Alrun, Ham, Sihyun, Basquin, Jérôme, Oh, Byung-Ha, Gruber, Stephan

“…Multi-subunit SMC complexes control chromosome superstructure and promote chromosome disjunction, conceivably by actively translocating along DNA double…”
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Local environment effects on charged mutations for developing aggregation-resistant monoclonal antibodies by Lee, Jihyeon, Chong, Song-Ho, Ham, Sihyun

“…Protein aggregation is a major concern in biotherapeutic applications of monoclonal antibodies. Introducing charged mutations is among the promising strategies…”
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Examining a Thermodynamic Order Parameter of Protein Folding by Chong, Song-Ho, Ham, Sihyun

“…Dimensionality reduction with a suitable choice of order parameters or reaction coordinates is commonly used for analyzing high-dimensional time-series data…”
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New Computational Approach for External Entropy in Protein–Protein Binding by Chong, Song-Ho, Ham, Sihyun

“…Molecular recognition through the noncovalent association of biomolecules is of central importance in biology and pharmacology. Developing reliable…”
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Site-directed analysis on protein hydrophobicity by Chong, Song-Ho, Ham, Sihyun

“…Hydrophobicity of a protein is considered to be one of the major intrinsic factors dictating the protein aggregation propensity. Understanding how protein…”
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Conformational Entropy of Intrinsically Disordered Protein by Chong, Song-Ho, Ham, Sihyun

“…Intrinsically disordered proteins (IDPs), though lacking stable tertiary structures, are known to possess a certain amount of residual structure…”
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Protein Folding Thermodynamics: A New Computational Approach by Chong, Song-Ho, Ham, Sihyun

“…Folding free energy is the fundamental thermo­dynamic quantity characterizing the stability of a protein. Yet, its accurate determination based on…”
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Atomic decomposition of the protein solvation free energy and its application to amyloid-beta protein in water by Chong, Song-Ho, Ham, Sihyun

“…We report the development of an atomic decomposition method of the protein solvation free energy in water, which ascribes global change in the solvation free…”
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A Cyclized Helix-Loop-Helix Peptide as a Molecular Scaffold for the Design of Inhibitors of Intracellular Protein-Protein Interactions by Epitope and Arginine Grafting by Fujiwara, Daisuke, Kitada, Hidekazu, Oguri, Masahiro, Nishihara, Toshio, Michigami, Masataka, Shiraishi, Kazunori, Yuba, Eiji, Nakase, Ikuhiko, Im, Haeri, Cho, Sunhee, Joung, Jong Young, Kodama, Seiji, Kono, Kenji, Ham, Sihyun, Fujii, Ikuo

“…The design of inhibitors of intracellular protein–protein interactions (PPIs) remains a challenge in chemical biology and drug discovery. We propose a cyclized…”
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Atomic Level Investigations of Early Aggregation of Tau43 in Water II. Tau43‐Aβ42 vs. Tau43‐Tau43 Dimerizations by Chatterjee, Prathit, Cho, Myung Keun, Bui, Huong T. D., Ham, Sihyun

“…Amyloid β (Aβ) senile plaques and Tau neurofibrillary tangles (NFTs) are major hallmarks of Alzheimer's disease (AD). However, early stages of Tau aggregation…”
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Explicit Characterization of the Free Energy Landscape of pKID–KIX Coupled Folding and Binding by Chong, Song-Ho, Im, Haeri, Ham, Sihyun

“…The most fundamental aspect of the free energy landscape of proteins is that it is globally funneled such that protein folding is energetically biased. Then,…”
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Configurational entropy of protein: A combined approach based on molecular simulation and integral-equation theory of liquids by Chong, Song-Ho, Ham, Sihyun

“…[Display omitted] ► A novel theoretical method is developed to calculate protein configurational entropy. ► Our method does not assume Gaussian distribution of…”
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Role of electrostatic interactions in determining the G-quadruplex structures by Lee, Jinkeong, Im, Haeri, Chong, Song-Ho, Ham, Sihyun

“…[Display omitted] •We investigate the energetics of three representative G-quadruplex structures.•Conformational energy and solvation free energy correlate…”
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Structural heterogeneity in familial Alzheimer's disease mutants of amyloid-beta peptides by Chong, Song-Ho, Yim, Janghyun, Ham, Sihyun

“…Alzheimer's disease is a neurodegenerative disorder characterized by progressive deposition of amyloid-beta (Aβ) peptides in brain parenchyma and cerebral…”
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