Question

A stretch of 20 amino acids is sufficient to form an \(\alpha\) helix long enough to span the lipid bilayer of a membrane. How could this piece of information be used to search for membrane proteins in a data bank of primary sequences of proteins?

Short answer

Search for stretches of 20 hydrophobic amino acids in sequences to find membrane proteins.

Step-by-step solution

Understand the Lipid Bilayer Structure

The lipid bilayer typically found in cell membranes is approximately 3 to 4 nanometers thick. Proteins that span this bilayer are known as transmembrane proteins.

Link \\(\alpha\\) Helix with Span Length

An \(\alpha\) helix consists of 3.6 amino acids per turn, with a rise of about 0.15 nm per amino acid. Thus, a stretch of 20 amino acids forms an \(\alpha\) helix approximately 3.0 nm long, which is adequate to span the lipid bilayer.

Analyze Primary Protein Sequences

In a data bank of primary protein sequences, identify sequences with stretches of 20 hydrophobic amino acids. These stretches are potential candidates for forming the \(\alpha\) helices that span lipid bilayers.

Check Hydrophobicity

Since membrane-spanning \(\alpha\) helices are typically composed of hydrophobic amino acids, it is important to verify that identified sequences have a high hydrophobicity index.

Search and Validation in Databank

Use software tools to scan protein sequences for stretches of 20 or more consecutive hydrophobic amino acids. Further validate these candidates by examining the context of the sequence and checking for other known domains.

Key concepts

Alpha Helix

An alpha helix is a common structural motif in proteins. This structure is crucial in understanding the functionality of many proteins, including those that span lipid bilayers.

The alpha helix is characterized by a spiral shape, stabilized by hydrogen bonds between the carbonyl oxygen of one amino acid and the amide hydrogen of another, four residues away.

• This configuration results in 3.6 amino acids per turn of the helix.
• Each amino acid contributes approximately 0.15 nanometers to the length of the helix.

When considering membrane proteins, an alpha helix formed by a stretch of 20 amino acids spans a length of about 3.0 nanometers. This is particularly long enough to cross a typical lipid bilayer, providing a bridge from one side of a cell membrane to the other.

Recognizing stretches of amino acids in their alpha-helical form can indicate their role as transmembrane regions in proteins, critical for cellular processes and signaling.

Lipid Bilayer

The lipid bilayer forms the fundamental structure of cellular membranes. It establishes a barrier that separates the inner cellular environment from the external one.

The bilayer is composed of two layers of phospholipid molecules, with hydrophilic (water-attracting) "heads" facing outward and hydrophobic (water-repelling) "tails" facing inward.

• This arrangement excludes water and water-soluble substances, maintaining the essential conditions for cellular activity.
• The thickness of the lipid bilayer is typically between 3 to 4 nanometers, which corresponds well with the length of a typical transmembrane alpha helix.

Membrane proteins that integrate into this lipid bilayer can either pass through completely or associate on one side. Transmembrane proteins, in particular, possess regions long enough to fully span the lipid bilayer, often adopting structures like the alpha helix to facilitate this function.

Thus, identifying and understanding the lipid bilayer is vital to comprehending how proteins can embed themselves into membranes, and how they contribute to the cell's functionality.

Hydrophobic Amino Acids

Hydrophobic amino acids play a significant role in the structural and functional aspects of membrane proteins. These amino acids prefer to avoid water, aligning perfectly with the environment found within the lipid bilayer.

Inside the bilayer, the environment is non-polar, favoring interactions with hydrophobic amino acids.

• Examples of hydrophobic amino acids include alanine, valine, leucine, isoleucine, and phenylalanine.
• Membrane-spanning regions of proteins are typically rich in these amino acids.

When searching for potential membrane proteins within databases, sequences with stretches of 20 or more consecutive hydrophobic amino acids are often flagged as likely candidates for forming transmembrane helices.

The identification and analysis of these hydrophobic regions can provide insights not only into potential protein function but also in understanding how proteins are structured to interact within the lipid-rich environment of cellular membranes. Understanding the nature of hydrophobic amino acids, therefore, is key to unlocking the secrets behind many integral membrane proteins.