Why are high resolution structures better than low resolution structures? They allow you to analyze larger proteins They are experimentally easier to generate You can detect hydrogen atoms The positions of the atoms in the structure are more accurate
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Why are high resolution structures better than low resolution structures?
They allow you to analyze larger proteins
They are experimentally easier to generate
You can detect hydrogen atoms
The positions of the atoms in the structure are more accurate
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- Which of these is an advantage of NMR over X-ray crystallography when it comes to determining the structure of proteins? It has higher resolution It can analyze larger proteins It can analyze the structure of proteins in solution It can analyze negatively charged proteinsKeratin and fibroin are examples of ……… proteins. These proteins have ……….. structure repeating a single type of ……….. structure element. can you fill in the blanks……….. proteins do not have a defined secondary structure composition. They can have both helices and sheets. When primary sequence is studied, it does not look like there is any order in the sequence, but there is order in 3D structure. ……… amino acids are clustered in the core of the protein, away from the solvent (water molecules) and …….. amino acids are on the surface of the protein.
- In your own words discuss the different structures (primary, secondary, tertiary, and Quaternary structures) of protein. What are the five factors that promote protein folding and stability. (Hint: One factor is the Hydrogen bond). Extra Hint: Another factor is the Hydrophobic effect. Do not just copy and paste from other sources/websites/books/articles/etc.A peptide bond... is a version of an ester bond is a version of an amide bond is the basis of protein secondary structure is formed by addition of waterChoose the FALSE statement about protein electrophoresis. The proteins in the gel can be visualized by staining them with silver. The distance and speed that a protein moves depend on its shape. Small proteins move rapidly through the gel. It is performed in a thin, horizontal slab of polyacrylamide. The gel serves as a molecular sieve that enhances separation.
- Which of the following statements about electron microscopy are true? a) Most existing protein structures have been resolved using electron microscopy b) Electron microscopy is not used in structural biology as it can not give as high a resolution as X-ray crystallography and NMR c) The smaller a protein, the easier it is to solve its structure with electron microscopy d) By taking pictures of the same protein frozen in ice thousands of times and then adding them together, you get a high-resolution image of the protein e) The first protein structure with true atomic resolution was solved using electron microscopy last yearPeptide bond is /has ……………. This structural feature prevents protein to sample all possible conformations available can you fill in the blanksWhat physical method is most frequently use to determine three dimensional structures of protein? Fluorescence spectroscopy Electron microscopy X ray crystallography Nuclear magnetic resonance spectroscopy Mass spectrometry
- Amino acids have the generic structure, where R represents different carbon-based side chains. Describe how the structure of amino acids allows them to be linked into long peptide chains to form proteins. Make an imaginary peptide chain or protein molecule.One advantage of the protein structures solved by NMR comparing to the x-ray structures is: a. It can determine the absolute, unique structure. b. It can solve protein structures in solution, which might be more physiological relevant. c. It is much easier to solve the structure. d. It has higher resolution. e. It can solve proteins with higher molecular weight.A _____ is an example of protein secondary structure. Select one: a. polypeptide b. domain c. barrel