About: Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: synergism among multiple depletions

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About: Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: synergism among multiple depletions Goto Sponge NotDistinct Permalink

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scientific article published on 01 June 2003

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в червні 2003 (uk) im Juni 2003 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en xunu de 2003 (ast) scientific article published on 01 June 2003 (en)
publication date	wds:Q57851835-4A7FE787-F845-4CFE-AFBE-F7149E870F0F
publication date	2003-06-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57851835-3ECCB397-1924-4492-9FB4-EF1A37E455C3
language of work or name	English
cites work	wds:Q57851835-13186CE7-141B-4DC4-8AEC-5FFEBF7F32D7 wds:Q57851835-16A41E7E-65CB-4DF1-8E94-D971E40A0D5A wds:Q57851835-192AB7CA-C01B-4F63-AB8B-6416AD6EB6D6 wds:Q57851835-22CA1C68-F38A-45B9-B16F-A6551B349F75 wds:Q57851835-33DE1383-97E5-4036-AFBF-60E2DBFDB744 wds:Q57851835-3E75D185-A19D-47F5-9FAF-643B19BE18E1 wds:Q57851835-43246C12-6F9A-4EEC-A581-CBD0F66DFD29 wds:Q57851835-439ED940-C174-4357-BFD0-164096E0AF44 wds:Q57851835-47BFDEBF-BB95-4AF0-8DCF-BE5A6F6EE8D5 wds:Q57851835-56837F4B-7706-4439-84C7-9DB981744BCB wds:Q57851835-57B95AE9-51C6-4A31-8F82-511E5966E96A wds:Q57851835-62B0CE1E-014B-4560-9228-C40667337AC3 wds:Q57851835-663900AE-16E2-4E54-A939-891F6CFA85AB wds:Q57851835-7155F0D5-B23F-4961-9D22-C80224A59016 wds:Q57851835-719D440F-E1E0-48E2-89C7-65C11BF9D76F wds:Q57851835-72212658-437E-4783-A286-17F362DE2CDE wds:Q57851835-726E9E0D-49FE-4A92-8E83-6149FE941AD0 wds:Q57851835-776B9E3D-1080-450F-B0F7-3F46D78A2457 wds:Q57851835-7DD4F612-459F-44D9-8856-A4F4969C4034 wds:Q57851835-81EAA1A6-E89B-4D43-BA16-B6FC3BA639A5 wds:Q57851835-8219D7E0-F98E-4153-B179-0E15A7D3190B wds:Q57851835-8262F57E-7EFC-42E1-87FB-64C573BA4EF9 wds:Q57851835-8D73F762-5E18-4EBF-9607-518391B473A4 wds:Q57851835-9AFC71C6-B93F-4D4B-88BC-C452138FD568 wds:Q57851835-A17F7A0C-633B-4D16-A204-D391D69586FB wds:Q57851835-A2BE7301-129D-474F-B9D2-104A50650C7A wds:Q57851835-A7F69C15-E2C1-40AF-A1C0-4DB90276B98F wds:Q57851835-B8D2C7C8-D69A-49B5-B3D5-F4F2A3A09B29 wds:Q57851835-BE696EE8-5808-474B-8E93-86ADCDD7C63E wds:Q57851835-C258BB39-86E5-40EA-812D-56840D9E5258 wds:Q57851835-EF14FC35-9FC7-44F5-AF82-84ED5D803A08 wds:Q57851835-FC20D1EB-9AAE-4D0A-AA28-BE889C555D65
cites work	Substantial increase of protein stability by multiple disulphide bonds Mutational effects on protein stability Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme Phage lambda repressor revertants. Amino acid substitutions that restore activity to mutant proteins Stability of proteins: small globular proteins Energetics of ribonuclease T1 structure. Thermodynamics of ribonuclease T1 denaturation Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles Temperature dependence of the hydrophobic interaction in protein folding Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles Dominant forces in protein folding The crystal structure of nickel(II)-azurin A rapid and efficient one-tube PCR-based mutagenesis technique using Pfu DNA polymerase Effects of site-specific amino acid modification on protein interactions and biological function Additivity of mutational effects in proteins The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus) A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme Mutant forms of staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturation The azurin gene from Pseudomonas aeruginosa codes for a pre-protein with a signal peptide. Cloning and sequencing of the azurin gene X-ray crystal structure of the two site-specific mutants His35Gln and His35Leu of azurin from Pseudomonas aeruginosa A spectroscopic and calorimetric investigation on the thermal stability of the Cys3Ala/Cys26Ala azurin mutant Extended theoretical analysis of irreversible protein thermal unfolding. Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli Cumulative effect of intragenic amino-acid replacements on the thermostability of a protein Long-range electrostatic interactions can influence the folding, stability, and cooperativity of dihydrofolate reductase. Synergism in folding of a double mutant of the alpha subunit of tryptophan synthase Thermodynamics and kinetics of the thermal unfolding of plastocyanin Effects of metal ligation and oxygen on the reversibility of the thermal denaturation of Pseudomonas aeruginosa azurin
author name string	wds:Q57851835-2BB6BCFD-B017-4258-B242-A5C3FD009EFA wds:Q57851835-42784A3A-791D-4B0C-96D2-96408C62A752 wds:Q57851835-CEE65BB0-1172-4BD7-A1AB-399DBAAFA87A
author name string	Gerard W Canters Domenico M Grasso Martin Ph Verbeet
rdfs:label	Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: synergism among multiple depletions (en) Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: synergism among multiple depletions (nl)
skos:prefLabel	Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: synergism among multiple depletions (en) Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: synergism among multiple depletions (nl)
name	Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: synergism among multiple depletions (en) Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: synergism among multiple depletions (nl)
author	wds:Q57851835-D51A22BD-DCDE-4E08-8454-7B74DCC7FA0E wds:Q57851835-F3F86BD7-A9F2-4C24-A8A8-DF86EF595820
author	Danilo Milardi Carmelo La Rosa
title	wds:Q57851835-C502DC99-2B2E-445D-B10D-FE3C4E6236B3
title	Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: synergism among multiple depletions (en)
page(s)	wds:Q57851835-C043BB06-500A-480D-9F9D-A49E2921F29D
page(s)	121-127
instance of	wds:Q57851835-9E1F16F8-48A8-4CA9-A415-FAD970A898FB
instance of	scholarly article
PubMed ID	wds:Q57851835-2CF4CD25-CE8A-499E-8773-A2E98438AA4F
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/12745263
PubMed ID	12745263
published in	wds:Q57851835-2AE37FA0-83C8-4CD2-9633-C529BC0B0D19

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