liu.seSearch for publications in DiVA
Endre søk
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Method Development for Determining the Stability of Heat Stable Proteins Combined with Biophysical Characterization of Human Calmodulin and the Disease Associated Variant D130G
Linköpings universitet, Institutionen för fysik, kemi och biologi.
Linköpings universitet, Institutionen för fysik, kemi och biologi.
Linköpings universitet, Institutionen för fysik, kemi och biologi.
Linköpings universitet, Institutionen för fysik, kemi och biologi.
Vise andre og tillknytning
2016 (engelsk)Independent thesis Basic level (degree of Bachelor), 10,5 poäng / 16 hpOppgave
Abstract [en]

Calmodulin is a highly conserved calcium ion binding protein expressed in all eukaryotic species. The 149 amino acid residues in the primary structure are organized in seven α helices with the highly flexible central α helix connecting the two non-cooperative domains of calmodulin. Each domain contains two EF-hand motifs to which calcium ions bind in a cooperative manner, hence the binding of four calcium ions saturate one calmodulin molecule. In the cardiovascular area calmodulin is involved in the activation of cardiac muscle contraction, and mutations that arise in the genetic sequence of the protein often have severe consequences. One such consequential mutation that can arise brings about the replacement of the highly conserved aspartic acid with glycine at position 130 in the amino acid sequence. In this research, the thermal and chemical stability within the C domain of the D130G variant of human calmodulin was investigated using a new method only requiring circular dichroism spectroscopic measurements. Affinity studies within the C domain of the D130G variant of human calmodulin were performed using fluorescence spectroscopy, and the ligands chosen for this purpose were trifluoperazine and p- HTMI. All analytical experiments were performed with the C domain of wild type human calmodulin as a reference. From the new method, it was concluded that the C domain of the D130G variant of human calmodulin has a slightly decreased stability in terms of Tm and Cm values compared to the C domain of wild type human calmodulin. The affinity analyses indicated that neither trifluoperazine nor p-HTMI discriminates between the C domain of the D130G variant of human calmodulin and the C domain of wild type human calmodulin in terms of dissociation constants. The pivotal outcome from this research is that the new method is applicable for determination of the stability parameters Tm and Cm of heat stable proteins. 

sted, utgiver, år, opplag, sider
2016. , s. 47
Emneord [en]
Calmodulin, wild type, D130G variant, method, affinity, trifluoperazine, p-HTMI.
HSV kategori
Identifikatorer
URN: urn:nbn:se:liu:diva-138022ISRN: LITH-IFM-G-EX--16/3178--SEOAI: oai:DiVA.org:liu-138022DiVA, id: diva2:1106033
Fag / kurs
Chemical Biology
Presentation
2016-05-27, ACAS, Linköpings Universitet (campus valla), A-huset, Linköping, 08:15 (svensk)
Veileder
Examiner
Tilgjengelig fra: 2017-06-09 Laget: 2017-06-06 Sist oppdatert: 2017-06-09bibliografisk kontrollert

Open Access i DiVA

fulltext(3606 kB)188 nedlastinger
Filinformasjon
Fil FULLTEXT01.pdfFilstørrelse 3606 kBChecksum SHA-512
cfa4d603fce78d2bc48eed6a32f907d20ac695d0bd8e046b63a20576322a543cf213f89f15ac107bf1d9d7f05569f0ea81ad6f72314c8c7a2db71cc166772c3d
Type fulltextMimetype application/pdf

Andre lenker

http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-138022

Søk i DiVA

Av forfatter/redaktør
Aleckovic, EhlimanaChamoun, SherleyEinarsson, Ellen
Av organisasjonen

Søk utenfor DiVA

GoogleGoogle Scholar
Totalt: 188 nedlastinger
Antall nedlastinger er summen av alle nedlastinger av alle fulltekster. Det kan for eksempel være tidligere versjoner som er ikke lenger tilgjengelige

urn-nbn

Altmetric

urn-nbn
Totalt: 1025 treff
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf