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Michael Bloemendal

Researcher at University of Amsterdam

Publications -  32
Citations -  1166

Michael Bloemendal is an academic researcher from University of Amsterdam. The author has contributed to research in topics: Circular dichroism & Protein secondary structure. The author has an hindex of 13, co-authored 32 publications receiving 1117 citations. Previous affiliations of Michael Bloemendal include VU University Amsterdam & Royal Free Hospital.

Papers
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Journal ArticleDOI

Estimation of protein secondary structure and error analysis from circular dichroism spectra.

Ivo H. M. van Stokkum, +4 more
- 15 Nov 1990 - 
TL;DR: The adequacy of thelinear model is investigated, paying special attention to the estimation of the error in the secondary structure estimates, and it is shown that the linear model is only adequate for the alpha-helix class.
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Temperature-induced changes in protein structures studied by Fourier transform infrared spectroscopy and global analysis.

I.H.M. van Stokkum, +5 more
- 22 Aug 1995 - 
TL;DR: In all the proteins investigated, except for ribonuclease S, an intermolecular beta-sheet band indicative of aggregation appeared concomitant with the denaturation of the secondary structure, and this was interpreted as a change in tertiary structure leading to enhanced solvent accessibility.
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Protein Secondary Structure from Fourier Transform Infrared and/or Circular Dichroism Spectra

R. Pribic, +4 more
- 01 Nov 1993 - 
TL;DR: A multivariate linear model (Gauss-Markoff model) with noise is used to analyze the estimation of protein secondary structure from spectra of 21 reference proteins whose structures are known from X-ray studies and it is concluded that the linear model is more adequate for the protein FTIR spectra than for the CD spectra.
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Fourier transform infrared spectroscopy and differential scanning calorimetry of transferrins: human serum transferrin, rabbit serum transferrin and human lactoferrin

Jonathan M. Hadden, +4 more
- 16 Mar 1994 - 
TL;DR: FTIR spectroscopy shows that a distinct loss of protein secondary structure occurs at the transition temperatures shown by DSC, indicating that significant structural changes do occur upon iron binding/release.
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Non-random conformation of a mouse IgG2a monoclonal antibody at low pH.

Wim Jiskoot, +6 more
- 01 Oct 1991 - 
TL;DR: The combined results suggest an acid-induced expansion and enhanced flexibility of MN12, which eventually leads to irreversible aggregation.