ArticleBiophysical journal2012
Structure, stability, and aggregation of β-2 microglobulin mutants: insights from a Fourier transform infrared study in solution and in the crystalline state.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed.
- Affibodies as valuable tool to prevent βBiology direct · 2025Article
- A self-assembled protein β-helix as a self-contained biofunctional motif.Nature communications · 2025Article
- The residues 4 to 6 at the N-terminus in particular modulate fibril propagation of β-microglobulin.Acta biochimica et biophysica Sinica · 2022Article
- Conformational Stability and Dynamics in Crystals Recapitulate Protein Behavior in Solution.Biophysical journal · 2020Article
- Two novel fish paralogs provide insights into the Rid family of imine deaminases active in pre-empting enamine/imine metabolic damage.Scientific reports · 2020Article
- Methionine oxidation in α-synuclein inhibits its propensity for ordered secondary structure.The Journal of biological chemistry · 2019Article
- Investigating the Molecular Basis of the Aggregation Propensity of the Pathological D76N Mutant of Beta-2 Microglobulin: Role of the Denatured State.International journal of molecular sciences · 2019Article
- Insights into Insulin Fibril Assembly at Physiological and Acidic pH and Related Amyloid Intrinsic Fluorescence.International journal of molecular sciences · 2017Article
- Biochemical and Electrophysiological Modification of Amyloid Transthyretin on Cardiomyocytes.Biophysical journal · 2016Article
- Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability.Scientific reports · 2016Article
- Co-fibrillogenesis of Wild-type and D76N β2-Microglobulin: THE CRUCIAL ROLE OF FIBRILLAR SEEDS.The Journal of biological chemistry · 2016Article
- Wild type beta-2 microglobulin and DE loop mutants display a common fibrillar architecture.PloS one · 2015Article
- Decoding the Structural Bases of D76N ß2-Microglobulin High Amyloidogenicity through Crystallography and Asn-Scan Mutagenesis.PloS one · 2015Article
- Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.Journal of the American Chemical Society · 2014Article
- Role of water in chromosome spreading and swelling induced by acetic acid treatment: a FTIR spectroscopy study.European journal of histochemistry : EJH · 2014Article
- Biophysical characterization of Met-G-CSF: effects of different site-specific mono-pegylations on protein stability and aggregation.PloS one · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
β-2 microglobulin (β2m) is an amyloidogenic protein involved in dialysis-related amyloidosis. We report here the study of the structural properties of the protein in solution and in the form of single crystals by Fourier transform infrared (FTIR) spectroscopy and microspectroscopy. The investigation has been extended to four β2m mutants previously characterized by x-ray crystallography: Asp(53)Pro, Asp(59)Pro, Trp(60)Gly, and Trp(60)Val. These variants displayed very similar three-dimensional structures but different thermal stability and aggregation propensity, investigated here by FTIR spectroscopy. For each variant, appreciable spectral differences were found between the protein in solution and in single crystals, consisting in a downshift of the main β-sheet band and in better resolved turn and loop bands, indicative of reduced protein secondary structure dynamics in the crystalline state. Notably, the well-resolved spectra of the β2m crystalline variants enabled us to identify structural differences induced by the single amino acid mutations. Such differences encompass turn and loop structures that might affect the stability and aggregation propensity of the investigated β2m variants. This study highlights the potential of FTIR microspectroscopy to acquire useful structural information on protein crystals, complementary to the crystallographic analyses.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.