<p>(A) Raw NIR spectra data set. Two regions over 1300–1600 nm and 2050–2350 nm were focused on to evaluate changes with water and protein structures, respectively. (B) A magnified view at 1300–1600 nm. The direction of absorbance increment is indicated by an arrow. (C) Time-dependency of absorbance. Absorbance increment obtained by averaging absorbance over 1300–1600 nm (closed circles) or 2050–2350 nm (open circles) was plotted against time. The three phases, i.e., phases I (nucleation), II (elongation), and III (equilibrium), are represented.</p
Insulin has a largely alpha-helical structure and exists as amixture of hexameric, dimeric, and mono...
This work presents near-infrared spectroscopy (NIRS) as an in-line process analyzer for monitoring p...
The monomer–dimer transition of insulin has been probed with two-dimensional infrared spectroscopy a...
The formation of amyloid fibrils proceeds via a nucleation-dependent mechanism in which nucleation p...
<p>Time dependent FT-IR spectra of insulin (2.0 mg/ml in D<sub>2</sub>O) in absence (A) and presence...
<p>(A) FTIR absorption spectrum at around the amide I region (solid line). The dashed line represent...
<p>(A) Absorbance spectra obtained before and after 276 nm light continuous exc. (0.25 h, 0.5 h, 0.7...
Tyrosine fluorescence emission spectra of the natively folded and standard insulin. The insulin samp...
© 2018, European Biophysical Societies' Association. The protein hormone insulin exists in several f...
During protein folding or unfolding, population of intermediates or partially unfolded conformations...
A non-toxic, nine residue peptide, NIVNVSLVK is shown to interfere with insulin fibrillation by vari...
<p>Absorbance profiles at 220 nm from size exclusion chromatography experiments with insulin (350 μM...
The monomer–dimer equilibrium for insulin is one of the essential steps in forming the receptor-bind...
© 2022 The Royal Society of ChemistryAmyloid proteins that undergo self-assembly to form insoluble f...
Two-dimensional NMR spectra have been recorded for bovine insulin at low pH in acetonitrile/water mi...
Insulin has a largely alpha-helical structure and exists as amixture of hexameric, dimeric, and mono...
This work presents near-infrared spectroscopy (NIRS) as an in-line process analyzer for monitoring p...
The monomer–dimer transition of insulin has been probed with two-dimensional infrared spectroscopy a...
The formation of amyloid fibrils proceeds via a nucleation-dependent mechanism in which nucleation p...
<p>Time dependent FT-IR spectra of insulin (2.0 mg/ml in D<sub>2</sub>O) in absence (A) and presence...
<p>(A) FTIR absorption spectrum at around the amide I region (solid line). The dashed line represent...
<p>(A) Absorbance spectra obtained before and after 276 nm light continuous exc. (0.25 h, 0.5 h, 0.7...
Tyrosine fluorescence emission spectra of the natively folded and standard insulin. The insulin samp...
© 2018, European Biophysical Societies' Association. The protein hormone insulin exists in several f...
During protein folding or unfolding, population of intermediates or partially unfolded conformations...
A non-toxic, nine residue peptide, NIVNVSLVK is shown to interfere with insulin fibrillation by vari...
<p>Absorbance profiles at 220 nm from size exclusion chromatography experiments with insulin (350 μM...
The monomer–dimer equilibrium for insulin is one of the essential steps in forming the receptor-bind...
© 2022 The Royal Society of ChemistryAmyloid proteins that undergo self-assembly to form insoluble f...
Two-dimensional NMR spectra have been recorded for bovine insulin at low pH in acetonitrile/water mi...
Insulin has a largely alpha-helical structure and exists as amixture of hexameric, dimeric, and mono...
This work presents near-infrared spectroscopy (NIRS) as an in-line process analyzer for monitoring p...
The monomer–dimer transition of insulin has been probed with two-dimensional infrared spectroscopy a...