We focus on the dynamical aspects of wetting phenomena on the nanoscale for which bulk hydrodynamic equations become invalid. At the nanoscale, phenomena that are irrelevant on the micrometer scale and larger, or that can be summarily incorporated in terms of boundary conditions, become important. Among these features are long-ranged molecular interactions such as dispersion forces, thermal fluctuations, hydrodynamic slip, segregation of mixtures and solutions at walls, and electrical double layers.

Wetting Phenomena in Nanofluidics

Late embryogenesis-abundant (LEA) proteins are one of the components involved in desiccation tolerance (DT) by maintaining cellular structures in the dry state. Among them, MtPM25, a member of the group 5 is specifically associated with DT in Medicago truncatula seeds. Its function is unknown and its classification as a LEA protein remains elusive. Here, evidence is provided that MtPM25 is a hydrophobic, intrinsically disordered protein that shares the characteristics of canonical LEA proteins. Screening protective activities by testing various substrates against freezing, heating and drying indicates that MtPM25 is unable to protect membranes but able to prevent aggregation of proteins during stress. Prevention of aggregation was also found for the water soluble proteome of desiccation-sensitive radicles. This inhibition was significantly higher than that of MtEM6, one of the most hydrophilic LEA protein associated with DT. Moreover, when added after the stress treatment, MtPM25 is able to rapidly dissolve aggregates in a non-specific manner. Sorption isotherms show that when it is unstructured, MtPM25 absorbs up to threefold more water than MtEM6. MtPM25 is likely to act as a protective molecule during drying and plays an additional role as a repair mechanism compared with other LEA proteins.

https://www.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1365-3040.2009.02093.x

MtPM25 is an atypical hydrophobic late embryogenesis-abundant protein that dissociates cold and desiccation-aggregated proteins.

The molecular origin of the hydrophobic effect is investigated using the angle-dependent integral equation theory combined with the multipolar water model. The thermodynamic quantities of solvation (excess quantities) of a nonpolar solute are decomposed into the translational and orientational contributions. The translational contributions are substantially larger with the result that the temperature dependence of the solute solubility, for example, can well be reproduced by a model simple fluid where the particles interact through strongly attractive potential such as water and the particle size is as small as that of water. The thermodynamic quantities of solvation for carbon tetrachloride, whose molecular size is ∼1.9 times larger than that of water, are roughly an order of magnitude smaller than those for water and extremely insensitive to the strength of solvent-solvent attractive interaction and the temperature. The orientational contributions to the solvation energy and entropy are further decompos...

Molecular origin of the hydrophobic effect: analysis using the angle-dependent integral equation theory.

It has been experimentally shown that the folding of apoplastocyanin (apoPC) accompanies a very large enthalpic loss [N. Baden et al., J. Chem. Phys. 127, 175103 (2007)]. This implies that an even larger entropic gain occurs in stabilizing the folded structure to overcome the enthalpic loss. Here, we calculate the water-entropy gain upon the folding of apoPC using the angle-dependent integral equation theory combined with the multipolar water model and the recently developed morphometric approach. It is demonstrated that the calculated value is in quantitatively good accord with the value estimated from the experimental data by accounting for the conformational-entropy loss. According to a prevailing view, the water adjacent to a hydrophobic group is unstable especially in terms of the rotational entropy and the folding is driven primarily by the release of such unfavorable water to the bulk through the burial of nonpolar side chains. We show, however, that the resultant entropic gain is too small to elucidate the experimental result. The great entropic gain observed is ascribed to the reduction in the restriction for the translational motion of water molecules in the whole system.

Thermodynamics of apoplastocyanin folding: comparison between experimental and theoretical results.

By reviewing the results of our analyses based on statistical-mechanical theories, we point out that the entropic effect arising from the translational motion of water molecules is a principal driving force in a variety of self-assembling and ordering processes in biological systems such as protein folding, molecular recognition, and ordered aggregation of protein molecules. The great entropic loss for the biomolecules accompanying these processes is largely compensated by a great entropic gain of the water that is present in the system. The microscopic mechanisms of protein folding and denaturation, receptor-ligand binding, and amyloid-fibril formation are discussed in detail. We describe an effort to develop a unique method for predicting the native structure of a protein. The roles of NaCl and cosolute molecules are also briefly discussed.

Roles of translational motion of water molecules in sustaining life.

On the energetics of protein folding in aqueous solution

Handle everyday research tasks with reliable, citation-backed results

Your personal Research Agent to handle research tasks with citation-backed results

Popular Tasks used by Researchers

How can I help with your research?

Meet SciSpace

Get more enhanced response by uploading the PDFs you want me to reference.

No relevant PDFs in your library

SciSpace is the AI research assistant for academics. Run systematic literature reviews on 280M+ papers, and write papers with cited sources. Trusted by 1M+ students, PhDs & researchers.

SciSpace | AI for Research

Analyze PDFs

Code & Manuscripts

Funding & Grants

Literature & Patents

Medical & Clinical Data

Systematic Review

Visualize & Present

Web & Data

Build a Google Scholar-like website for your research.

Build a website

Create charts and images for your research

Create a Chart

Write a paper for submission to a journal

Draft a manuscript

Patent Search

Design eye-catching scientific posters in minutes.

Scientific Poster Generation

Systematic Literature Review

One task is running at the moment. Your messages will be shown right after.

Drag and drop or click here to browse

Loved by <highlight>1 million+</highlight> researchers

Extract a list of specific topics and their sources from unstructured text

Topics

Compare and analyze relevant papers that matches with your search

Papers

Get insights from PDFs and bookmarked papers from your library

My library

Recent searches

Try searching for:

Catch AI-generated content in scholarly and non-scholarly content

{ai} Detector

Ai Writer

Get PDF Summaries, highlighted text explanations 

Chat with PDF

Effortlessly create in-text citations and bibliographies in APA and 2,500 other formats

Citation generator

Get explanations, summaries, and answers on academic papers

Ease up your research workflow with {scispace}'s cohort of exciting AI tools

Elevate your academic writing skills and convey your ideas the way you want

Paraphraser

Explore our range of reading and writing tools

Your file is being prepared and should be ready in a few minutes. If it's a large file, it might take a bit longer. You can close this window, and we'll email you the file when it's done.

You have reached a maximum limit of <strong>{limit}</strong> columns in the table. Remove at least <strong>1</strong> column to add or create another one.

Yuichi Harano

Author Tools

Chat about Author

Papers

On the energetics of protein folding in aqueous solution