About: Protein stability: electrostatics and compact denatured states

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scientific article published on May 1991

Attributes	Values
rdf:type	Item
description	videnskabelig artikel (da) article científic (ca) articolo scientifico (it) artigo científico (pt) bilimsel makale (tr) vedecký článok (sk) vetenskaplig artikel (sv) vědecký článek (cs) wetenschappelijk artikel (nl) wissenschaftlicher Artikel (de) научни чланак (sr) article scientifique (fr) artículu científicu espublizáu en 1991 (ast) наукова стаття, опублікована в травні 1991 (uk) 1991年學術文章 (zh) مقالة علمية نشرت في مايو 1991 (ar) scientific article published on May 1991 (en)
publication date	wds:Q37510917-A10D0618-4058-43D0-A175-83AA19E57E80
publication date	1991-05-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q37510917-30F7E653-B205-4EA9-92D7-3CF21B00B391
language of work or name	English
cites work	wds:Q37510917-0FD2276D-26BB-4EE5-A7C6-BA5BD5AE54C9 wds:Q37510917-2B3234F7-7033-406A-9D93-C50D46FAD8B5 wds:Q37510917-2D1728AC-E38B-4B23-BC50-1C977D4E0E06 wds:Q37510917-405995CA-ADBE-4661-A38D-5938E59612A7 wds:Q37510917-7A3487E0-1B37-44A0-9775-CE96BA3C08B3 wds:Q37510917-7CC42306-7EE3-44CC-B4C0-2884AFADB74F wds:Q37510917-8EB6382B-9125-4914-8E89-3F1B7FA25E23 wds:Q37510917-9DCFB118-DF4F-4A72-8EE0-4D8AAD6135A7 wds:Q37510917-A072A0DF-6BBA-4B08-AE6F-5822F1DA991D wds:Q37510917-A0A23FFB-3C69-4223-85B4-6452F6C6F3A7 wds:Q37510917-BD7259B2-DDF2-4B9C-97DB-CFC52B424F32 wds:Q37510917-C6D56E5C-301E-4A99-9AC1-A6E64608EF2A wds:Q37510917-CE04D341-17B9-4E1B-AA1E-6537490AD961 wds:Q37510917-D43922ED-0B68-4A25-A1F8-329987DE736A wds:Q37510917-DCA2C4E6-9CBE-45CE-B00B-8DC76C90959F wds:Q37510917-E73D11DD-BFAE-45BE-A7A9-A39222EB7B8F
cites work	Origins of structure in globular proteins The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Calculation of the total electrostatic energy of a macromolecular system: solvation energies, binding energies, and conformational analysis Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin Some factors in the interpretation of protein denaturation Theory for the folding and stability of globular proteins Conformational states of beta-lactamase: molten-globule states at acidic and alkaline pH with high salt. Cold denaturation of myoglobin Calculation of electrostatic interactions in proteins Thermal stabilities of globular proteins Reactivity of sperm whale metmyoglobin towards hydrogen ions and p-nitrophenyl acetate Thermodynamic study of the apomyoglobin structure Phase diagram for acidic conformational states of apomyoglobin Electrostatic stabilization in myoglobin. pH dependence of summed electrostatic contributions On the "heat-coagulation" of proteins: Part II. The action of hot water upon egg-albumen and the influence of acid and salts upon reaction velocity. Charge effects on folded and unfolded proteins
author name string	wds:Q37510917-AB1307B4-7980-403D-B3D9-1C2A5A715B6F wds:Q37510917-C57498F2-5987-4B4E-AA52-26CC409CBD71
author name string	Alonso DO Stigter D
rdfs:label	Protein stability: electrostatics and compact denatured states (en) Protein stability: electrostatics and compact denatured states (nl) Protein stability: electrostatics and compact denatured states (ast)
skos:prefLabel	Protein stability: electrostatics and compact denatured states (en) Protein stability: electrostatics and compact denatured states (nl) Protein stability: electrostatics and compact denatured states (ast)
name	Protein stability: electrostatics and compact denatured states (en) Protein stability: electrostatics and compact denatured states (nl) Protein stability: electrostatics and compact denatured states (ast)
author	wds:Q37510917-180D47FC-9174-43CB-9A33-6DBDCD9216DD
author	Ken A. Dill
title	wds:Q37510917-BB8BFCFB-C5EA-4786-A88F-48B7E89FAC30
title	Protein stability: electrostatics and compact denatured states (en)
page(s)	wds:Q37510917-43D1E7D3-6FD4-4CCA-8834-2347D8DC68FF
page(s)	4176-4180
instance of	wds:Q37510917-2994837A-9C5F-43E5-9593-69080D292E2F
instance of	scholarly article
PubMed ID	wds:Q37510917-BB584575-621D-4D2C-8B04-B0F83C2A8403
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2034662
PubMed ID	2034662
published in	wds:Q37510917-C367CF5D-487F-4F61-AC44-440A7A899058
published in	Proceedings of the National Academy of Sciences of the United States of America
issue	wds:Q37510917-ED9932D2-E6DD-4943-BF8E-EB5B05B0AFE1
volume	wds:Q37510917-A22DEB36-3B42-476B-B838-811C15D2D3FE
issue	10
volume	88
DOI	wds:Q37510917-BD21C9FA-1DE1-4309-9D14-76CDD1F4C159
DOI	http://dx.doi.org/10.1073/PNAS.88.10.4176
DOI	10.1073/PNAS.88.10.4176
ResearchGate publication ID	wds:Q37510917-9B62A6CD-1AF9-4EF6-A08C-2FA2152953E4
ResearchGate publication ID	21120673
ADS bibcode	wds:Q37510917-0D5DE86F-8558-47EA-B5FA-79E78895FF3C
ADS bibcode	1991PNAS...88.4176S
PMCID	wds:Q37510917-D2A82B3C-F1D5-4D9C-A1FA-1CA572E49BA4
PMCID	51621
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q37510917
is cites work of	Principles of protein folding--a perspective from simple exact models. Carboxyl pK(a) values, ion pairs, hydrogen bonding, and the pH-dependence of folding the hyperthermophile proteins Sac7d and Sso7d Electrostatic effects on funneled landscapes and structural diversity in denatured protein ensembles Backbone dipoles generate positive potentials in all proteins: origins and implications of the effect Membrane association of functional vesicular stomatitis virus matrix protein in vivo Nitrile Bonds as Infrared Probes of Electrostatics in Ribonuclease S

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