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» Authors » Oyvind Halskau Jr

Oyvind Halskau Jr

Explore the profile of Oyvind Halskau Jr including associated specialties, affiliations and a list of published articles. Areas
Snapshot
Articles 7
Citations 94
Followers 0
Related Specialties
Biochemistry
Science
Chemistry
Top 10 Co-Authors
Aurora Martinez
Sondre Volden
Inge Jonassen
Jarl Underhaug
Gisle Saelensminde
Wilhelm R Glomm
Ronny Helland
Jose M Sanchez-Ruiz
David Rodriguez-Larrea
Masahiro Yasuda
Published In
Extremophiles
J Biol Chem
J Phys Chem B
Nanoscale
Proc Natl Acad Sci U S A
Affiliations
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Recent Articles
1.
The binding of 14-3-3γ to membranes studied by intrinsic fluorescence spectroscopy
Bustad H, Underhaug J, Halskau Jr O, Martinez A
FEBS Lett . 2011 Mar; 585(8):1163-8. PMID: 21420405
Human 14-3-3 proteins contain two conserved tryptophan residues in each monomer, Trp60 and Trp233 in isoform γ. 14-3-3γ binds to negatively charged membranes and here we show that membrane binding...
2.
Emergent membrane-affecting properties of BSA-gold nanoparticle constructs
Lystvet S, Volden S, Yasuda M, Halskau Jr O, Glomm W
Nanoscale . 2011 Mar; 3(4):1788-97. PMID: 21359387
By adsorbing bovine serum albumin (BSA) on gold nanoparticles (Aunps) with diameters 30 nm and 80 nm, different degrees of protein unfolding were obtained. Adsorption and adlayer conformation were characterized...
3.
Three-way interaction between 14-3-3 proteins, the N-terminal region of tyrosine hydroxylase, and negatively charged membranes
Halskau Jr O, Ying M, Baumann A, Kleppe R, Rodriguez-Larrea D, Almas B, et al.
J Biol Chem . 2009 Oct; 284(47):32758-69. PMID: 19801645
Tyrosine hydroxylase (TH), the rate-limiting enzyme in the synthesis of catecholamines, is activated by phosphorylation-dependent binding to 14-3-3 proteins. The N-terminal domain of TH is also involved in interaction with...
4.
Amino acid contacts in proteins adapted to different temperatures: hydrophobic interactions and surface charges play a key role
Saelensminde G, Halskau Jr O, Jonassen I
Extremophiles . 2008 Oct; 13(1):11-20. PMID: 18825305
Thermophiles, mesophiles, and psychrophiles have different amino acid frequencies in their proteins, probably because of the way the species adapt to very different temperatures in their environment. In this paper,...
5.
Large-scale modulation of thermodynamic protein folding barriers linked to electrostatics
Halskau Jr O, Perez-Jimenez R, Ibarra-Molero B, Underhaug J, Munoz V, Martinez A, et al.
Proc Natl Acad Sci U S A . 2008 Jun; 105(25):8625-30. PMID: 18550823
Protein folding barriers, which range from zero to the tens of RT that result in classical two-state kinetics, are primarily determined by protein size and structural topology [Plaxco KW, Simons...
6.
Adsorption behavior of acidic and basic proteins onto citrate-coated Au surfaces correlated to their native fold, stability, and pI
Glomm W, Halskau Jr O, Hanneseth A, Volden S
J Phys Chem B . 2007 Dec; 111(51):14329-45. PMID: 18052360
The adsorption of eight different proteins (alpha-lactalbumin (types I and III), bovine serum albumin, hemoglobin, myoglobin, cytochrome c, alpha-casein, and lysozyme) onto a model anionic surface was performed at equivalent...
7.
Structure-dependent relationships between growth temperature of prokaryotes and the amino acid frequency in their proteins
Saelensminde G, Halskau Jr O, Helland R, Willassen N, Jonassen I
Extremophiles . 2007 Apr; 11(4):585-96. PMID: 17429573
We studied the amino acid frequency and substitution patterns between homologues of prokaryotic species adapted to temperatures in the range 0-102 degrees C, and found a significant temperature-dependent difference in...