Which of the following statements accurately represents characteristics of nmr and x‑ray crystallography? x‑ray crystallography can be used only for larger proteins or complexes. the limitations of x‑ray crystallography and nmr are the same with respect to all proteins. nmr is preferable to x‑ray crystallography because it can be used with proteins in a wider range of molecular weights. x‑ray crystallography generally gives a more detailed (higher resolution) view than does nmr.

X‑ray crystallography generally gives a more detailed (higher resolution) view than does NMR.

Explanation:

X-ray crystallography and nuclear magnetic resonance (NMR) are two major techniques for the examination of protein structure. Both of them have their advantage in use, and each of them is appropriate for a certain type of examination.

X‑ray crystallography has high resolution and it is not that much  limited by the protein molecular weight. Disadvantage is that the protein that is being examined must be in the crystal structure. Another disadvantage is that this method gives the static structure of the protein (motions are not available).

NMR advantage is that the structure of the protein is in its native state (it includes dynamics and intermolecular interactions) andd it doesm't have to be crystallized. Disadvantage of NMR is it cannot be used for large molecules (64kDa is the largest molecular mass).

vodka and hennesy

explanation:

hydroxyl -oh

alcohols, always polar, can form hydrogen bonds with h2o molecules

carboxyl -cooh  

cargoxylic acids, has acidic properties which is a source of hydrogen ions, found in cells in ionized for with a charge of oh-1

carbonyl > co

ketone if within skeleton, aldehyde if group is at the end of skeleton, k & a may be structural isomers, it determines 2 sugars (ketose & aldose)

amino -nh2

amines, acts as a base, it can pick up h+ ions from surrounding solution, ionized with charge of 1+

methyl ch2

addition to rna/dna affects and gene expression

phosphate -opo3 ²⁻

organic phosphates, contributes to negative charge to, molecule that it is a part of, and potential to react with h20

sulfhydryl -sh

thiols, cross-linking stabilize the protein, and it is structure