Based on their chemical structures, explain why some amino acids do not travel as far up...

Based on their chemical structures, explain why some amino acids do not travel as far up the paper as others in paper chromatography .

Solutions

Expert Solution

Paper chromatography is a analytical technique (one of the chromatographic technique) which is used to seperate coloured components on a specialised filter paper composed of celluloe which act as stationary phase. And the solvent used is mobile phase.

Amino acid structure is like: H₂N-CH(R)-COOH.

Different amino acids travel with different rates on the paper due to difference in their R group.

Amino acid which has higher affinity towards mobile phase will go up the with the mobile phase while amino acid which has higher affinity towards stationary phase, it will stick to the paper and move more slowly with the solvent (mobile phase). Usually smaller amino acid molecules will move farther than larger amino acid molecules.

The affinity of amino acid with mobile phase depend on solublity of amino acid in mobile phase.

Other factors that affect migration are molecular weight of amino acid, size, shape, polarity,etc.

The rate of movement of amino acid wrt to solvent front is given by the term R_f (Retention or Retardation Factor). It is defined as the ratio of distance travelled by the amino acid to the distance travelled by the solvent (mobile phase).

queen_honey_blossom answered 1 year ago

Next > < Previous

Related Solutions

Can the exact same sequence of amino acids fold into different tertiary structures?

Explain the importance of essential amino acids to animals

Perhaps the most central concept in amino acid degradation is that some amino acids are glucogenic,...

Perhaps the most central concept in amino acid degradation is that some amino acids are glucogenic, some are ketogenic and some are both glucogenic and ketogenic. Which of the following amino acids is both glucogenic and ketogenic? A. Arg B. Ile C. Leu D. Asn E. Cys

1) Name and classify the common amino acids according to the chemical structure of their R...

1) Name and classify the common amino acids according to the chemical structure of their R groups. (Note: Please this is my Medicicinal biochemistry class question just that medicinal biochemistry is not listed among the subject then i marked this question under chemistry. Please i need an answer to this question.) show all work

Explain why nitrogen is shuttled from peripheral tissues to liver in the form of amino acids...

Explain why nitrogen is shuttled from peripheral tissues to liver in the form of amino acids instead of being released into the blood as free ammonium ions for the liver to scavenge?

Draw three-dimensional representations of the following amino acids. Explain their structures. (a) L-phenylalanine (b) L-histidine (c)...

Draw three-dimensional representations of the following amino acids. Explain their structures. (a) L-phenylalanine (b) L-histidine (c) D-serine (d) L-tryptophan

1.How do D -amino acids differ from L-amino acids? What biological roles are played by peptides...

1.How do D -amino acids differ from L-amino acids? What biological roles are played by peptides that contain D -amino acids? 2.Which amino acid is technically not an amino acid? Which amino acid contains no chiral carbon atoms? 3.For each of the following, name an amino acid in which the R group contains it: a hydroxyl group, a sulfur atom, a second chiral carbon atom, an amino group, an amide group, an acid group, an aromatic ring, and a branched...

Explain why all protein sources are not the same. (Hint: think about limiting amino acids and...

Explain why all protein sources are not the same. (Hint: think about limiting amino acids and complementary proteins)

3) Proteins are made up of amino acids as the building blocks. a) The structural integrity...

3) Proteins are made up of amino acids as the building blocks. a) The structural integrity of a protein is critical for its functions. Using no more than 300 words, describe TWO (2) examples of mutations or alterations to the native protein sequence which have led to an enhancement or reduction in the biological activity of the mutant proteins. For example, enzyme kinetics, antimicrobial activity, anticancer, drug interaction, and others. (Note: Must only be based on recent (<5 years) research...

protein molecules are polypetide chains are made up of amino acids in their phisologically functoning or...

protein molecules are polypetide chains are made up of amino acids in their phisologically functoning or native state these chains fold in a unique manner such that the nonpolar groups of the amino acids are usually burired in the interior region of the proteins where there is little or no contact with water. when a protein denatures the chain unfolds so that these non polar groups are exposed to water. a useful estimate of the changes of the thermodynamic quantities...

Subjects