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21 Carboxylic Acid Derivatives -- Part 23
The structure of a molecule is made up of the sequence of acids and disulfide bridges.
amyloid plaques and destruction of nerve tissue are thought to be caused by an infectious agent that promotes misfolding and polymerization.
Prosthetic groups include sugars, lipids, nucleic acids, and metal complexes.
The weights of the polypeptides are higher than 5000 amu.
A type of structure in which the chain is not curled into a helix or lined up in a sheet.
There are segments of random coil that fold the molecule into its shape.
A method for determining the N-terminal amino acid.
The peptide is treated with 2,4-dinitrofluorobenzene.
The rest of the peptide is destroyed in the process of derivatizing.
The secondary structure is usually a helix or random coil.
The order in which amino acids are linked together is a word.
To determine the sequence of a peptide.
There are only two types of Proteins, composed of only amino acids.
The peptide is cleaved from the solid support when it is complete.
The 20 a@amino acids are found in almost all naturally occurring proteins.
A@amino acids can be synthesised by reaction of an aldehyde with ammonia and cyanide ion.
It is possible to remove and identify the residue at the N and C end points.
Transamination is a common method for the synthesis of amino acids.
A structure with an overall charge of zero but two negatively charged substituent.
The majority of the amino acids are in zwitterionic forms.
Each skill is followed by problem numbers.
Draw the structures from the names of the two acids.
Information from terminal and partial hydrolysis can be used to determine the structure of a peptide.
The isoelectric point of phenylalanine is 5.
The major form of phenylalanine has pH values of 1, 5.5, and 11.
Take the complete structure of the peptide and draw it.
How would you make any of the standard amino acids?
You can use any necessary reagents.
Suggestions for a method for the synthesis of the natural l enantiomer of alanine from the readily available l enantiomer of lactic acid.
The Strecker synthesis can be used to make isoleucine.
The structures for the following peptides should be written.
Tell us if the peptide is acidic, basic, or neutral.
The structure is drawn in a different way.
You need to identify and label each acid.
The full name and abbreviated name should be given.
phenyl alanine, aspartic acid, and methanol are given by complete hydrolysis of aspartame.
There is no effect on aspartame.
The phenylthiohydantoin of aspartic acid is given after treatment with phenyl isothiocyanate.
There is a proposal for a structure for aspartame.
One Gly, two Ala, one Met, and one Phe are found in an unknown peptide that has been shown to be a pentapeptide.
The first free amino acid released after treatment of the original pentapeptide is alanine.
The structure for the unknown pentapeptide should be proposed.
The steps and intermediates are shown in the picture.
There are functional groups other than carboxyl groups at the C terminus.
The hydrolysate is found to contain Ala, Phe, Val, and Glu.
There is an unknown pentapeptide that gives leucine, valine, and isoleucine.
When the hydrolysate is neutralized, there is no smell of ammonia.
A long, flexible amide linkage is usually used to bind the peptide to the active sites of the enzymes.
It can be drawn in both of its forms.
Show how a disulfide bridge can be formed with two Cys residues.
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