Protein Structure-sensitive Analysis by Normal Pulse Voltammetry
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F16%3A00471946" target="_blank" >RIV/68081707:_____/16:00471946 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1002/elan.201600202" target="_blank" >http://dx.doi.org/10.1002/elan.201600202</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/elan.201600202" target="_blank" >10.1002/elan.201600202</a>
Alternative languages
Result language
angličtina
Original language name
Protein Structure-sensitive Analysis by Normal Pulse Voltammetry
Original language description
Earlier we showed that constant current chronopotentiometric stripping (CPS) at mercury-containing electrodes reflects changes in proteins, such as denaturation, single amino acid exchange or protein damage by physical and chemical agents. Here we attempted to compare performance of the galvanostatic CPS with the potentiostatic normal pulse voltammetry (NPV). We have found that repeated 50ms or longer NPV pulses denature the surface-attached protein. Using shorter pulses and adapting other NPV settings we have been able to obtain a good resolution of native (folded) and denatured (unfolded) bovine serum albumin. On the other hand, partial denaturation of the surface-attached native bovine serum albumin during the potential scanning may prevent detection of small conformational changes in the protein.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
BO - Biophysics
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GA15-15479S" target="_blank" >GA15-15479S: New tools for research and diagnostics of diseases. Microfluidic reactors and electrochemistry for analysis of proteins and their glycosylation.</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Electroanalysis
ISSN
1040-0397
e-ISSN
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Volume of the periodical
28
Issue of the periodical within the volume
11
Country of publishing house
DE - GERMANY
Number of pages
6
Pages from-to
2884-2889
UT code for WoS article
000387891400034
EID of the result in the Scopus database
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