About: Contribution of hydrophobic interactions to protein stability

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Contribution of hydrophobic interactions to protein stability Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

scientific article published in Nature

Attributes	Values
rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) article publié dans la revue scientifique Nature (fr) scientific article published in Nature (en) im Juni 1988 veröffentlichter wissenschaftlicher Artikel (de) наукова стаття, опублікована в Nature в червні 1988 (uk)
publication date	wds:Q59082159-5AC5EA4B-B19A-4804-8D39-C6B662974049
publication date	1988-06-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q59082159-348DFCA0-6C7B-4A6E-9765-082A95ABA54D
language of work or name	English
exact match	wds:Q59082159-3FC99B8E-50CA-4B63-9D38-93847D605C5B
exact match	https://scigraph.springernature.com/pub.10.1038/333784a0
cites work	wds:Q59082159-109CB048-5CDA-42F8-8359-C76F51770415 wds:Q59082159-42A7B34B-3F76-43D8-82DE-373BA23D2C5A wds:Q59082159-444C51B3-783B-4488-B7E5-70C9EEFDC36D wds:Q59082159-45C90A9B-E44C-4FD8-8CBC-84B3F7CD35E9 wds:Q59082159-47842688-67B2-46AD-80D4-D843ECD08EAC wds:Q59082159-64FD8E04-5CD3-4037-8206-3BA7148A0FD0 wds:Q59082159-6BA45A47-0FBE-44BD-84CC-F72E6A925BBE wds:Q59082159-7BD60CCC-4C48-485E-B03A-2893AE184061 wds:Q59082159-8FD01C75-165F-4170-BD67-4E20D055816E wds:Q59082159-9086BDBC-D63D-47CA-856C-B4D23EE891B1 wds:Q59082159-96E8F1D7-DEDC-49C2-BA0A-910F1507F82D wds:Q59082159-A529E8EE-7845-41DC-8F3F-233726174D92 wds:Q59082159-AB1B87B6-99E3-48A3-873B-4717E377AC92 wds:Q59082159-B4877386-5F04-4375-99AE-346B217BACFF wds:Q59082159-BED90B2F-B8AE-4B6C-BB0E-699BC6827AB9 wds:Q59082159-C0B94A24-CE29-41D9-9B63-0A8053954F96 wds:Q59082159-C6A12904-587D-47F9-95AD-0C4D85E391E4 wds:Q59082159-CF7CEF93-0460-4885-BCFC-14DAE984B1C7 wds:Q59082159-DCE595C9-B4EE-449E-B996-AB7CDAA08D60 wds:Q59082159-DDBC9740-0A92-44CC-99F9-94D0C7E9C5D7 wds:Q59082159-DF9BC636-5BB0-4B41-A7F9-91AFA471D56F wds:Q59082159-E6AB7AA4-B64C-4389-BCE6-70A79C8F5A27 wds:Q59082159-FF27F5C7-3003-4B77-906E-F417260A29FD
cites work	Principles that determine the structure of proteins Free energy calculations by computer simulation Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme Oligonucleotide-Directed Mutagenesis: A Simple Method Using Two Oligonucleotide Primers and a Single-Stranded DNA Template Affinities of amino acid side chains for solvent water Structural patterns in globular proteins Different base/base mismatches are corrected with different efficiencies by the methyl-directed DNA mismatch-repair system of E. coli Determination and analysis of urea and guanidine hydrochloride denaturation curves Folding and association of proteins The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus) Molecular structure of a new family of ribonucleases Kinetic and magnetic resonance studies of effects of genetic substitution of a Ca2+-liganding amino acid in staphylococcal nuclease A reversible thermal transition of the extracellular ribonuclease of Bacillus amyloliquefaciens Structure-activity relationships in engineered proteins: analysis of use of binding energy by linear free energy relationships Expression of Bacillus amyloliquefaciens extracellular ribonuclease (barnase) in Escherichia coli following an inactivating mutation. Interactions between an alpha-helix and a beta-sheet. Energetics of alpha/beta packing in proteins. Ribonuclease of Bacillus subtilis Helix to helix packing in proteins Mutant forms of staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturation Conformational stability of mixed disulfide derivatives of beta-lactoglobulin B Packing of alpha-helices onto beta-pleated sheets and the anatomy of alpha/beta proteins Environmental effects on the thermal transition of Bacillus amyloliquefaciens ribonuclease (barnase)
author name string	wds:Q59082159-09FD3FEE-C4FE-40B5-8934-18B863209B04 wds:Q59082159-8287811F-DA91-4DE6-85B4-3CE91ADD1AC1 wds:Q59082159-D30C9425-038E-4400-9C42-D7997AD90EDE wds:Q59082159-F98017C9-BBE1-459E-8347-2AEB5CA83BF7
author name string	D Sali A R Fersht K Nyberg J T Kellis
rdfs:label	Contribution of hydrophobic interactions to protein stability (en) Contribution of hydrophobic interactions to protein stability (nl)
skos:prefLabel	Contribution of hydrophobic interactions to protein stability (en) Contribution of hydrophobic interactions to protein stability (nl)
name	Contribution of hydrophobic interactions to protein stability (en) Contribution of hydrophobic interactions to protein stability (nl)
author	wds:Q59082159-7986C343-CDA8-4E71-8954-09E07698C03C
author	Alan Fersht
title	wds:Q59082159-2F031903-EC24-4EF7-B338-D30BBB4C964A
title	Contribution of hydrophobic interactions to protein stability (en)
page(s)	wds:Q59082159-BACD5737-74DA-452D-A9FF-317803FE59B9
page(s)	784-786
instance of	wds:Q59082159-8D064891-A9B9-4329-BECF-3981EB0B3F62
instance of	scholarly article
main subject	wds:Q59082159-81FE4772-5987-4457-B1E3-3541199F7D96
main subject	hydrophobicity
PubMed ID	wds:Q59082159-4A0784FA-A569-46AF-8276-651A0551990C
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3386721
PubMed ID	3386721
published in	wds:Q59082159-8896F5BC-57D8-4CC5-A4E6-D1F236302DEB
published in	Nature
issue	wds:Q59082159-A0AA43EF-8E4D-4174-A9FB-7234DED5A5BB
volume	wds:Q59082159-457BE140-78E9-4B1C-A2F9-AC06EC822A4A
issue	6175
volume	333
DOI	wds:Q59082159-9C4E4116-B931-4750-83F8-759A15D3ACE4
DOI	http://dx.doi.org/10.1038/333784A0
DOI	10.1038/333784A0
Dimensions Publication ID	wds:Q59082159-5E79A437-C7C0-4576-B6F2-104171EE28AF
Dimensions Publication ID	1044335885
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q59082159
is cites work of	Protein compressibility, dynamics, and pressure Hydrophobic effect in protein folding and other noncovalent processes involving proteins

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 190 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software