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What does the prefix " \(\alpha\) " mean when referring to an \(\alpha\) -amino acid?

Short Answer

Expert verified
The prefix \(\alpha\) refers to the amino group attached to the alpha carbon.

Step by step solution

01

Identify the Amino Acid Structure

Amino acids are organic molecules that contain both an amino group (\(-NH_2\)) and a carboxyl group (\(-COOH\)). The specific structure of an amino acid consists of a central carbon atom, known as the alpha (\(\alpha\)) carbon, to which the amino group, carboxyl group, hydrogen atom, and an R group (side chain) are attached.
02

Define the Alpha Carbon

The alpha carbon is the first carbon atom that attaches to a functional group, in this case, the carboxyl group (\(-COOH\)). It is the central carbon to which the amino group (\(-NH_2\)), the carboxyl group, and the R group are bonded. This makes it an integral part of the amino acid structure.
03

Explain the Meaning of the Prefix "Alpha"

The prefix "alpha" (\(\alpha\)) in \(\alpha\)-amino acid refers to the position of the amino group attached to the alpha carbon. This implies the amino group is attached to the first carbon next to the carboxyl group, distinguishing \(\alpha\)-amino acids from other amino acids that may have the amino group in different positions.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Amino acid structure
Amino acids are crucial organic compounds that play a significant role in forming proteins, which are essential for numerous biological functions. Each amino acid consists of a basic structure with a central carbon atom called the alpha carbon. This central atom is bound to four different groups, creating a unique structure vital for biological activity.

Here's the basic structure of an amino acid:
  • An amino group (\(-NH_2\)) - this part of the molecule makes it an 'amino' acid.
  • A carboxyl group (\(-COOH\)) - this provides the 'acid' part of the name.
  • A hydrogen atom.
  • An R group or side chain, which varies among different amino acids and determines their specific properties.
Understanding how these components are arranged around the alpha carbon is key to understanding amino acids' chemical behavior and their biological functions.

The diversity in the R group leads to over 20 types of amino acids, each with unique characteristics. Despite their differences, they share this fundamental structure.
Alpha carbon
The term "alpha carbon" might seem complex, but it's quite straightforward once broken down. In the world of chemistry, carbons are often labeled in a chain relative to a functional group. The alpha carbon is the first carbon atom connected to the carboxyl group, which is quite central in amino acids' unique structure.

Imagine the alpha carbon as the heart of the amino acid structure. It holds together the amino group, the carboxyl group, and the R group, acting as the main axis around which the molecule revolves.

The geometry around the alpha carbon is typically tetrahedral, allowing for multiple bonding arrangements. This flexibility is crucial as it enables proteins to form their distinct three-dimensional structures and perform their unique functions within biological systems.

Thanks to the position and bonds formed by the alpha carbon, each amino acid gains its specific spatial structure and functional capacity, contributing greatly to the diversity of proteins.
Functional groups in organic chemistry
Functional groups play an essential role in organic chemistry, as they largely determine the properties and reactivity of molecules. These groups are specific atoms or clusters of atoms within molecules that exhibit predictable chemical behavior.

In amino acids, the key functional groups are the amino group (\(-NH_2\)) and the carboxyl group (\(-COOH\)). These groups influence the molecule's ability to form bonds and participate in chemical reactions.
  • The amino group acts as a base, capable of accepting protons.
  • The carboxyl group acts as an acid, able to donate protons.
These characteristics allow amino acids to link together through peptide bonds, forming proteins.

The role of the R group, another critical component, should also be highlighted. It introduces unique functional attributes to the molecule, from making it polar or nonpolar to charged or uncharged. These properties significantly impact the amino acid's role in proteins, affecting protein folding, stability, and interactions. Understanding functional groups helps us make sense of the vast array of molecular behaviors and activities within cells and all living organisms.

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Most popular questions from this chapter

Write full structures for the following peptides: (a) C-H-E-M (b) E-A-S-Y (c) P-E-P-T-I-D-E

Proteins can be cleaved specifically at the amide bond on the carboxyl side of methionine residues by reaction with cyanogen bromide, \(\mathrm{BrC} \equiv \mathrm{N}:\) The reaction occurs in several steps: (a) The first step is a nucleophilic substitution reaction of the sulfur on the methionine side chain with BrCN to give a cyanosulfonium ion, \(\mathrm{R}_{2} \mathrm{SCN}^{+}\). Show the structure of the product, and propose a mechanism for the reaction. (b) The second step is an internal \(\mathrm{S}_{\mathrm{N}} 2\) reaction, with the carbonyl oxygen of the methionine residue displacing the positively charged sulfur leaving group and forming a five-membered ring product. Show the structure of the product and the mechanism of its formation. (c) The third step is a hydrolysis reaction to split the peptide chain. The carboxyl group of the former methionine residue is now part of a lactone (cyclic ester) ring. Show the structure of the lactone product and the mechanism of its formation. (d) The final step is a hydrolysis of the lactone to give the product shown. Write the mechanism of the reaction.

Show the mechanism for formation of a Boc derivative by reaction of an aming acid with di-tert-butyl dicarbonate.

There are six isomeric tripeptides containing valine, tyrosine, and glycine. Name them using both three- and one-letter abbreviations.

Of the 19 L amino acids, 18 have the \(S\) configuration at the \(\alpha\) carbon. Cysteine is the only \(\mathrm{L}\) amino acid that has an \(R\) configuration. Explain.

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