(Q67921533)

English

Protein interactions with surface-immobilized metal ions: Structure-dependent variations in affinity and binding capacity with temperature and urea concentration

scientific article published on 01 May 1991

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scholarly article

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:1856719%20AND%20SRC:MED&resulttype=core&format=json

19 September 2019

Protein interactions with surface-immobilized metal ions: structure-dependent variations in affinity and binding capacity with temperature and urea concentration (English)

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Europe PubMed Central

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19 September 2019

Protein interactions with surface-immobilized metal ions: Structure-dependent variations in affinity and binding capacity with temperature and urea concentration (English)

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10.1016/0162-0134(91)80037-I

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11 December 2022

inorganic chemistry

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10.1016/0162-0134(91)80037-I

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11 December 2022

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10.1016/0162-0134(91)80037-I

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11 December 2022

author name string

T. W. Hutchens

1

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1856719

11 December 2022

T. T. Yip

2

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11 December 2022

language of work or name

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National Center for Biotechnology Information

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11 December 2022

publication date

1 May 1991

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19 September 2019

number of pages

14

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full work available at URL

https://api.elsevier.com/content/article/PII:016201349180037I?httpAccept=text/xml

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10.1016/0162-0134(91)80037-I

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11 December 2022

https://api.elsevier.com/content/article/PII:016201349180037I?httpAccept=text/plain

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10.1016/0162-0134(91)80037-I

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11 December 2022

Journal of Inorganic Biochemistry

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19 September 2019

42

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19 September 2019

2

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Europe PubMed Central

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19 September 2019

105-118

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:1856719%20AND%20SRC:MED&resulttype=core&format=json

19 September 2019

Metal chelate affinity chromatography, a new approach to protein fractionation

1

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Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes

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Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains

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Differential interaction of peptides and protein surface structures with free metal ions and surface-immobilized metal ions

8

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Complex formation between metallic cations and proteins, peptides and amino acids

9

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Surface topography of histidine residues: a facile probe by immobilized metal ion affinity chromatography

11

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Protein interactions with immobilized transition metal ions: quantitative evaluations of variations in affinity and binding capacity

12

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11 December 2022

Journal of Cell Biology

13

107

846a

author name string

Yip

publication date

1988

1 reference

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THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONS

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Protein interaction with immobilized ligands: quantitative analyses of equilibrium partition data and comparison with analytical chromatographic approaches using immobilized metal affinity adsorbents

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Real-space refinement of the structure of hen egg-white lysozyme

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The Protein Data Bank: a computer-based archival file for macromolecular structures

18

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The interpretation of protein structures: Estimation of static accessibility

21

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Immobilized metal ion affinity adsorption and immobilized metal ion affinity chromatography of biomaterials. Serum protein affinities for gel-immobilized iron and nickel ions

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Evaluation of the interaction of peptides with Cu(II), Ni(II), and Zn(II) by high-performance immobilized metal ion affinity chromatography

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Buried surface area, conformational entropy, and protein stability

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Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. I. Reinvestigation of the histidine peak assignments

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Proton nuclear magnetic resonance studies of histidine residues in rat and other rodent pancreatic ribonucleases. Effects of ph and inhibitors

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Assignment of the histidine peaks in the nuclear magnetic resonance spectrum of ribonuclease

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Nuclear magnetic resonance studies of the structure and binding sites of enzymes. I. Histidine residues

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Ultrasonic absorption studies of protein-buffer interactions. Determination of equilibrium parameters of titratable groups.

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Reassignment of the active site histidines in ribonuclease A by selective deuteration studies

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Salting-out in amphiphilic gels as a new approach to hydrophobic adsorption

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Salting-out adsorption techniques for protein purification

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41 Modification of histidyl residues in proteins by diethylpyrocarbonate

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Identifiers

10.1016/0162-0134(91)80037-I

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:1856719%20AND%20SRC:MED&resulttype=core&format=json

19 September 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:1856719%20AND%20SRC:MED&resulttype=core&format=json

19 September 2019

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