FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts.
FTIR spectroscopy
aggregates
neutral salts
protein denaturation
second derivative method
secondary structure
Journal
Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414
Informations de publication
Date de publication:
14 04 2020
14 04 2020
Historique:
received:
12
02
2020
revised:
27
03
2020
accepted:
30
03
2020
entrez:
17
4
2020
pubmed:
17
4
2020
medline:
7
4
2021
Statut:
epublish
Résumé
The effect of neutral salts on protein conformation was first analyzed by Hofmeister in 1888, however, even today this phenomenon is not completely understood. To clarify this effect, we studied changes in the secondary structure of two proteins: human serum albumin with predominantly α-helical structure and porcine pancreas β-trypsin with the typical β-structural arrangement in aqueous solutions of neutral salts (KSCN, KCl, (NH
Identifiants
pubmed: 32295172
pii: biom10040606
doi: 10.3390/biom10040606
pmc: PMC7226448
pii:
doi:
Substances chimiques
Salts
0
Thiocyanates
0
Potassium Chloride
660YQ98I10
Trypsin
EC 3.4.21.4
potassium thiocyanate
TM7213864A
Serum Albumin, Human
ZIF514RVZR
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Government of Russian Federation
ID : Grant 08-08
Pays : International
Déclaration de conflit d'intérêts
The authors declare no conflict of interest.
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