47 questions · 29 sources · 0 syntheses
Protein Structure
The three-dimensional architecture of proteins.
Source-derived questions
Questions extracted from the papers in this topic, excluding the curated questions above.
- How accurate was AlphaFold 2 compared to experimental structures at the CASP competition?
- How are defects in ubiquitin pathways connected to diseases like Parkinson's and cancer?
- How are haemoglobin and chlorophyll molecular cousins, and what actually differs between them?
- How did Günter Blobel demonstrate that proteins carry built-in address labels?
- How did Kurt Wüthrich use nuclear magnetic resonance to determine protein structure in solution?
- How did X-ray crystallography go on to reveal the structure of DNA and haemoglobin?
- How did the CASP competition measure progress on the protein-folding problem for over two decades?
- How does AlphaFold2 predict a protein's structure directly from its sequence, and how accurate is it compared to experimental methods?
- How does X-ray crystallography reveal the atomic structure of something as large and irregular as a protein?
- How does a vortex fluidic device use shear force to refold proteins?
- How does an ultracentrifuge use spinning force to reveal the mass of a single protein molecule?
- How does moving-boundary electrophoresis separate proteins that look identical in solution?
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- How does ubiquitin mark a protein for destruction inside a cell?
- How does ubiquitin tag proteins for destruction inside a cell?
- How is chlorophyll's porphyrin ring structurally related to haemoglobin?
- How is hemoglobin's structure related to myoglobin's, given that hemoglobin carries oxygen in blood rather than muscle?
- What are disordered protein regions, and why were they long dismissed as structural filler?
- What are signal sequences, and how do they direct a newly made protein to its correct cellular compartment?
- What did Nishizuka discover about how the lipid diacylglycerol activates protein kinase C?
- What did Sumner crystallize in 1926, and what did it prove about the chemical nature of enzymes?
- What did two-dimensional NMR make possible for studying protein structure?
- What does it mean for David Baker to design proteins that 'do not exist in nature', and what are these novel proteins used for?
- What does the ribosome actually do inside a living cell?
- What happens to egg-white proteins during denaturation?
- What is haemin and why does it sit at the core of the haemoglobin molecule?
- What later fields of science and industry grew out of Tiselius's separation method?
- What resolution did Hodgkin's 1969 insulin structure achieve, and why did that matter?
- What role does the proteasome play in breaking down tagged proteins?
- What role does the proteasome play once a protein has been tagged with ubiquitin?
- What role does transfer RNA play in translating a codon into the correct amino acid, and how did Holley reveal it?
- What shape did myoglobin turn out to have, and how does that shape let it hold and release oxygen?
- What technique did Sanger use to label the terminal ends of protein fragments during sequencing?
- What was the 'phase problem' in X-ray crystallography, and how did attaching heavy atoms like mercury solve it?
- Where does coordination chemistry show up in biology and medicine today?
- Which diseases are linked to disruption of the ubiquitin-proteasome pathway?
- Why did Kendrew's myoglobin structure get solved before Perutz's haemoglobin, despite being the same underlying method?
- Why did Sanger's decade-long sequencing of insulin overturn the assumption that proteins had irregular, variable composition?
- Why did chemists before Svedberg struggle to determine whether proteins were discrete molecules or fuzzy colloidal clouds?
- Why did many proteins, especially membrane proteins, resist the older method of crystallisation for imaging?
- Why did membrane proteins resist crystallization for so long, and how did Michel's detergents solve the problem?
- Why did most biochemists in the 1940s assume protein, not DNA, carried genetic information?
- Why did rational protein design keep failing before Frances Arnold's approach?
- Why did scientists originally assume proteins were simple, repetitive structures before Kendrew and Perutz's work?
- Why did traditional mass spectrometry destroy proteins before they could be measured?
- Why do plants use magnesium to capture light while animals use iron to carry oxygen?
- Why is reversing protein denaturation relevant to diseases like Alzheimer's?
- Why is ubiquitin's near-universal presence in eukaryotic cells significant?
Sources
- AlphaFold solves the protein-folding problem
- DNA identified as genetic material
- Ig Nobel Prize in Chemistry
- Lasker Award (Basic Medical Research)
- Lasker Award (Basic Medical Research)
- Lasker Award (Basic Medical Research)
- Lasker Award (Basic Medical Research)
- Nobel Prize in Chemistry
- Nobel Prize in Chemistry
- Nobel Prize in Chemistry
- Nobel Prize in Chemistry
- Nobel Prize in Chemistry
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- Nobel Prize in Chemistry
- Nobel Prize in Chemistry
- Nobel Prize in Chemistry
- Nobel Prize in Chemistry
- Nobel Prize in Chemistry
- Nobel Prize in Chemistry
- Nobel Prize in Chemistry
- Nobel Prize in Chemistry
- Nobel Prize in Chemistry
- Nobel Prize in Chemistry
- Nobel Prize in Chemistry
- Nobel Prize in Physiology or Medicine
- Nobel Prize in Physiology or Medicine
- Three-dimensional structure of insulin determined
- Three-dimensional structure of myoglobin and hemoglobin resolved
- Willstätter determines chlorophyll structure
- von Laue discovers X-ray diffraction by crystals