MBB 222 Lecture Notes - Lecture 15: Adenine, Transfer Rna, Crystallography
3 Mar 2016
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Document Summary
Protein structural analysis: nuclear magnetic resonance, x-ray crystallography, transmission electron microscopy. Provides the finest visualization of protein structures currently available. Pros: can obtain structures even better that 1 resolution (0. 1 nm). Structures as large as viruses have been determined by x-ray crystallography. Cons: must be able to crystallize the protein. Proteins are not fully hydrated so not in their native environment. The energy absorbed to flip the nuclei is recorded as a peak on an nmr spectrum: the energy required for the nuclei to flip depends on the surroundings of the nuclei. Cons: limited to smaller proteins ~40 kda (300 - 400 amino acids). Secondary: any regular, stable structure taken by some or all of the nucleotides. Nucleotide = base + sugar + phosphate [e. g. adenosine monophosphate (amp)] Carbons in the ribose or deoxyribose are numbered with primes (") to distinguish them from atoms in the bases.
