What about the addition of adenine protects molecules? Can other bases provide the same protection or is it adenine specific?
I am reading Richard Dawkins's book, "The Selfish Gene."
In chapter 2 he talks about chemists putting simple substances into flasks and providing a source of energy. After a few weeks, something interesting occurs . . .
...amino acids have been found—the building blocks of proteins, one of the two great classes of biological molecules.
I have two questions:
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What is the great class of biological molecule to which he refers: amino acids or proteins?
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What is the other great class of biological molecules?
One of the question for my homework for testing biological molecule is:
"If a solution containing both reducing sugar and non-reducing sugar, suggest how this might be possible to repeat Benedict's solution test to confirm the presence of both type of sugar"
How do I find out the non-reducing sugar within the solution? If I use HCL to hydrolyze then add Benedict's, it wouldn't make any difference since the reducing sugar would be the one that shows the evidence anyway. How do I prove this?
Proteins are responsible for the occurrence and treatment of many diseases, and therefore protein sequencing will revolutionize proteomics and clinical diagnostics. Biological nanopore approach has proved successful for single‐molecule DNA sequencing, which resolves the identities of 4 natural deoxyribonucleotides based on the current blockages and duration times of their translocations across the nanopore confinement. However, open challenges still remain for biological nanopores to sequentially identify each amino acid (AA) of single proteins due to the inherent complexity of 20 proteinogenic AAs in charges, volumes, hydrophobicity and structures. Herein, we focus on recent exciting advances in biological nanopores for single‐molecule protein sequencing (SMPS) from native protein unfolding, control of peptide translocation, AA identification to applications in disease detection.
https://ift.tt/33uAHxt
Proteins are responsible for the occurrence and treatment of many diseases, and therefore protein sequencing will revolutionize proteomics and clinical diagnostics. Biological nanopore approach has proved successful for single‐molecule DNA sequencing, which resolves the identities of 4 natural deoxyribonucleotides based on the current blockages and duration times of their translocations across the nanopore confinement. However, open challenges still remain for biological nanopores to sequentially identify each amino acid (AA) of single proteins due to the inherent complexity of 20 proteinogenic AAs in charges, volumes, hydrophobicity and structures. Herein, we focus on recent exciting advances in biological nanopores for single‐molecule protein sequencing (SMPS) from native protein unfolding, control of peptide translocation, AA identification to applications in disease detection.
https://ift.tt/33uAHxt
