About: Microscopic Mechanism for Cold Denaturation

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scientific article published in Physical Review Letters

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rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) наукова стаття, опублікована в березні 2008 (uk) im März 2008 veröffentlichter wissenschaftlicher Artikel (de) article publié dans la revue scientifique Physical Review Letters (fr) scientific article published in Physical Review Letters (en)
publication date	wds:Q58454505-17BF8A04-82C7-4DDD-AF57-49BB0AAABE2B
publication date	2008-03-18 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q58454505-CF62412F-B88B-4D79-AD8B-65AA67F7CB87
language of work or name	English
cites work	wds:Q58454505-005EC2A6-7061-4DB3-A068-F108C353C8F8 wds:Q58454505-0D53AEDE-8610-4A25-9EF2-29301FAC4D77 wds:Q58454505-1C002C69-2C15-4A51-B7D2-22382F1CF2BB wds:Q58454505-2DB893E5-4461-44E8-9ABE-5C8C1DD9C366 wds:Q58454505-353E27DF-C25D-4149-A7E3-95E826D5251E wds:Q58454505-474061D7-1C08-4C12-9151-AE8CE581D549 wds:Q58454505-4FB26524-B892-4B52-A144-9065C00C921F wds:Q58454505-5C48D48C-C584-462E-9374-4E231ADB5C44 wds:Q58454505-69639B24-42B7-4089-B11F-136691DCBC4C wds:Q58454505-B29790F7-F1CE-4661-B64E-25CD519CC06E wds:Q58454505-B6C9BFAD-BCE3-4A67-9B97-2853CBED25CF wds:Q58454505-B98E72FB-B396-4F27-8B3B-118335DFBCB7 wds:Q58454505-CE364605-50BF-47AB-B425-06EC69BF589A
cites work	Protein unfolding, amyloid fibril formation and configurational energy landscapes under high pressure conditions Principles that govern the folding of protein chains Molecular dynamics simulations at constant pressure and/or temperature Dominant forces in protein folding Modeling water, the hydrophobic effect, and ion solvation Some factors in the interpretation of protein denaturation Finite-size scaling and Monte Carlo simulations of first-order phase transitions. The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins. Cold denaturation of myoglobin Possible Mechanism for Cold Denaturation of Proteins at High Pressure On the temperature--pressure free-energy landscape of proteins. A Simple Model of Water and the Hydrophobic Effect Potential of mean force between two hydrophobic solutes in water
author name string	wds:Q58454505-964BC672-6F42-4782-BCDB-305C44C916D3 wds:Q58454505-B0838CC4-0086-4EDC-8C2A-C9267EBFE351
author name string	Cristiano L Dias Martin Grant
rdfs:label	Microscopic Mechanism for Cold Denaturation (en) Microscopic Mechanism for Cold Denaturation (nl)
skos:prefLabel	Microscopic Mechanism for Cold Denaturation (en) Microscopic Mechanism for Cold Denaturation (nl)
name	Microscopic Mechanism for Cold Denaturation (en) Microscopic Mechanism for Cold Denaturation (nl)
author	wds:Q58454505-64C15A4E-006E-4398-BA2A-C2451783B994 wds:Q58454505-C7DF35BB-6454-4EF3-A0F5-66ED58566F30 wds:Q58454505-FABD9DB7-8519-4824-B013-CB7237AC5FB6
author	Mikko Karttunen Ilpo Vattulainen Tapio Ala-Nissila
title	wds:Q58454505-A9FDF4B7-CE1B-4A4A-98AF-8A2519E0F3F6
title	Microscopic mechanism for cold denaturation (en)
page(s)	wds:Q58454505-0764602A-F1D5-42C0-9D34-D1A70D70D1BB
page(s)	118101
instance of	wds:Q58454505-A46E432B-476D-4D6B-9917-A577E3F1525C
instance of	scholarly article
PubMed ID	wds:Q58454505-FBA8BDDA-E223-4DCB-A469-E6C2736E1863
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/18517830
PubMed ID	18517830
published in	wds:Q58454505-9EBA529C-5355-4198-A65C-F2594496ECE7
published in	Physical Review Letters
issue	wds:Q58454505-D7DEB617-789C-451E-8066-77C7BBFDAC5E
volume	wds:Q58454505-71E9A94E-291A-4DDB-A8A5-95367D293FAA
issue	11
volume	100
DOI	wds:Q58454505-A23D300D-F7F7-49DB-951B-61A44900C10B
DOI	http://dx.doi.org/10.1103/PHYSREVLETT.100.118101
DOI	10.1103/PHYSREVLETT.100.118101
arXiv ID	wds:Q58454505-9D7F2C71-87C0-4C93-B6B4-93A24AFF4728
arXiv ID	0704.2787
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q58454505
is cites work of	Cold adaptation, ca2+ dependency and autolytic stability are related features in a highly active cold-adapted trypsin resistant to autoproteolysis engineered for biotechnological applications Beta-peptide bundles with fluorous cores Cutting Ice: Nanowire Regelation Understanding the role of hydrogen bonds in water dynamics and protein stability. Effects of sugars on the thermal stability of a protein. Temperature-dependent solvation modulates the dimensions of disordered proteins Spectroscopic studies of the Salmonella enterica adenosyltransferase enzyme SeCobA: molecular-level insight into the mechanism of substrate Cob(II)alamin activation Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: a review Contribution of Water to Pressure and Cold Denaturation of Proteins. On the mechanism of cold denaturation Physical origin of hydrophobicity studied in terms of cold denaturation of proteins: comparison between water and simple fluids. The hydrophobic temperature dependence of amino acids directly calculated from protein structures Three-dimensional "Mercedes-Benz" model for water. Hydrophobicity within the three-dimensional Mercedes-Benz model: Potential of mean force Essential roles of protein-solvent many-body correlation in solvent-entropy effect on protein folding and denaturation: comparison between hard-sphere solvent and water. Hydrophobicity at low temperatures and cold denaturation of a protein. Computational investigation of cold denaturation in the Trp-cage miniprotein The Unfolded State of the C-Terminal Domain of L9 Expands at Low but Not at Elevated Temperatures. Consistent Treatment of Hydrophobicity in Protein Lattice Models Accounts for Cold Denaturation In Silico Evidence That Protein Unfolding is a Precursor of Protein Aggregation A theoretical analysis on characteristics of protein structures induced by cold denaturation. The non-uniform early structural response of globular proteins to cold denaturing conditions: a case study with Yfh1. A fully atomistic computer simulation study of cold denaturation of a β-hairpin. Modeling simple amphiphilic solutes in a Jagla solvent. NMR studies on the monomer-tetramer transition of melittin in an aqueous solution at high and low temperatures Observation of solvent penetration during cold denaturation of E. coli phosphofructokinase-2.

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