About: The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State Financial support from the Schweizerischer Nationalfonds (Project no. 21-50929.97) is gratefully acknowledged

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About: The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State Financial support from the Schweizerischer Nationalfonds (Project no. 21-50929.97) is gratefully acknowledged Goto Sponge NotDistinct Permalink

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scientific article published on 01 January 2001

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в січні 2001 (uk) articolo scientifico (pubblicato il 2001) (it) im Jahr 2001 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en xineru de 2001 (ast) artikull shkencor i botuar më 01 janar 2001 (sq) scientific article published on 01 January 2001 (en)
publication date	wds:Q73444388-E2ADC78A-CFCA-41BA-8B5C-B8485AE97007
publication date	2001-01-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q73444388-DC90C038-521A-4272-AA2C-FBB7454A6412
language of work or name	English
author name string	wds:Q73444388-B9600B5F-7DBC-4900-8859-67D134A27852 wds:Q73444388-CB08A7C2-2278-4734-90E2-3E9B7BBE4C75
author name string	Christine Peter Roland Bürgi
rdfs:label	The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State Financial support from the Schweizerischer Nationalfonds (nl) The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State Financial support from the Schweizerischer Nationalfonds (Project no. 21-50929.97) is gratefully acknowledged (en) The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State Financial support from the Schweizerischer Nationalfonds (Project no. 21-50929.97) is gratefully acknowledged (sq)
skos:prefLabel	The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State Financial support from the Schweizerischer Nationalfonds (nl) The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State Financial support from the Schweizerischer Nationalfonds (Project no. 21-50929.97) is gratefully acknowledged (en) The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State Financial support from the Schweizerischer Nationalfonds (Project no. 21-50929.97) is gratefully acknowledged (sq)
name	The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State Financial support from the Schweizerischer Nationalfonds (nl) The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State Financial support from the Schweizerischer Nationalfonds (Project no. 21-50929.97) is gratefully acknowledged (en) The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State Financial support from the Schweizerischer Nationalfonds (Project no. 21-50929.97) is gratefully acknowledged (sq)
author	wds:Q73444388-0ACCAAEB-5B3F-45F9-943A-7D5D7F014EBA wds:Q73444388-B5BFD5A6-7B98-477F-8E82-96EC8578CBD5
author	Wilfred F van Gunsteren Xavier Daura
title	wds:Q73444388-A50AB6C0-B81D-4A24-9565-1632F2CAB2A9
title	The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State Financial support from the Schweizerischer Nationalfonds (Project no. 21-50929.97) is gratefully acknowledged (en)
page(s)	wds:Q73444388-7B7DCE55-E247-4E30-8427-3BCE592CFF6D
page(s)	351-355
instance of	wds:Q73444388-8D3E762F-4164-4652-9A36-96F6382EE8D5
instance of	scholarly article
PubMed ID	wds:Q73444388-D7A546F1-97F0-4723-B777-C5D950981AA8 wds:Q73444388-bf68730d-59c3-4c5f-babf-89e6e4880e24
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11180322
PubMed ID	11180322
published in	wds:Q73444388-76F0A7C4-A65D-4608-A630-52647557D699
published in	Angewandte Chemie International Edition
issue	wds:Q73444388-0B3BBD83-5DD1-481D-92A5-D28E5C0D1DCE
volume	wds:Q73444388-3092A2DA-4961-4AE7-A739-4FE54C35F632
issue	2
volume	40
DOI	wds:Q73444388-83B8AAF9-20DF-43E4-8223-92B8DF67CE0E
DOI	http://dx.doi.org/10.1002/1521-3773(20010119)40:2%3C351::AID-ANIE351%3E3.0.CO;2-6
DOI	10.1002/1521-3773(20010119)40:2<351::AID-ANIE351>3.0.CO;2-6
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q73444388
is cites work of	Toward an accurate theoretical framework for describing ensembles for proteins under strongly denaturing conditions Random-coil behavior and the dimensions of chemically unfolded proteins Exploring Flory's isolated-pair hypothesis: statistical mechanics of helix-coil transitions in polyalanine and the C-peptide from RNase A. Fast protein folding on downhill energy landscape Validation of the 53A6 GROMOS force field Deciphering the folding transition state structure and denatured state properties of nucleophosmin C-terminal domain Temperature and urea induced denaturation of the TRP-cage mini protein TC5b: A simulation study consistent with experimental observations A simple model for polyproline II structure in unfolded states of alanine-based peptides Uncovering specific electrostatic interactions in the denatured states of proteins Validation of the GROMOS force-field parameter set 45Alpha3 against nuclear magnetic resonance data of hen egg lysozyme. Local structural preferences and dynamics restrictions in the urea-denatured state of SUMO-1: NMR characterization Native and nonnative conformational preferences in the urea-unfolded state of barstar Kinetics and thermodynamics of type VIII beta-turn formation: a CD, NMR, and microsecond explicit molecular dynamics study of the GDNP tetrapeptide Comment on the Communication "The Key to Solving the Protein-Folding Problem Lies in an Accurate Description of the Denatured State" by van Gunsteren et al. We thank Eugene Shakhnovich (Harvard University) for pointing out the references on lattice NMR characterization of the near native and unfolded states of the PTB domain of Dok1: alternate conformations and residual clusters Folding and misfolding of the papillomavirus E6 interacting peptide E6ap Modulating native-like residual structure in the fully denatured state of photoactive yellow protein affects its refolding Stochastic simulation of structural properties of natively unfolded and denatured proteins. Could Microwave Irradiation Cause Misfolding of Peptides?
is cites work of	wds:Q31030952-A9343253-4F75-4CE2-92C0-3D8C15BA8BFB wds:Q34452373-76D93B1F-5325-4388-9F2A-F32CCC210CAB wds:Q33777703-6DF0C09E-DA08-42EC-90E9-9B8D42926505 wds:Q38270402-F37261F2-2B0C-40D0-B8B6-068C4049CE74 wds:Q36527257-32F14C5C-F4AD-49B3-A863-2AF5F0695ACB wds:Q42625856-06771455-6F12-494E-8105-7FC17CEB1C70 wds:Q95391509-E53C411D-35AD-469D-BE62-619DE6539878 wds:Q33713782-AC53C92F-0B99-4D77-87AA-3F7615080013 wds:Q28540276-817A9191-C160-4664-87E0-912BAA274C85 wds:Q35163087-23466398-9373-4A85-9D65-843F1F5C8BBA wds:Q37493905-5C8B8C55-DD15-4CFC-8AA8-733702107E44 wds:Q36572197-689BCB5B-19D3-4D0B-A7D2-7DF73AD8DBB8 wds:Q41933651-AACDC1C2-FD15-4B4A-A28D-B90CBDF37591 wds:Q34984722-703D53DE-7AF2-4433-97F2-EEFB6D35D75D wds:Q30986204-508E4B45-8587-42E7-853E-F9C6DE5B77B6 wds:Q51362509-A6D933E0-96AB-4206-844F-E7C46975A751 wds:Q30979733-6121C4F8-E0A3-4973-8A99-F73CE9AD6A43 wds:Q90265628-A7A19E6C-07C9-4BC2-BADE-D815C8F02B61 wds:Q33800083-661E3D4D-B735-434D-923D-E487F9979DC1

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