Amino Acids Side Chains Quiz

Questions and Answers

Which of the following applies to the structure of the isoleucine side chain? (Select all that apply)

Contains the sulfhydryl group

Contains a branched hydrocarbon chain (correct)

Contains a positively charged side chain

Contains an aromatic ring

Which of the following applies to the structure of the phenylalanine side chain? (Select all that apply)

Contains an aromatic ring (correct)

Contains the sulfhydryl group

Contains a branched hydrocarbon chain

Contains a positively charged side chain

Which of the following applies to the structure of the methionine side chain? (Select all that apply)

Contains an aromatic ring

Contains a branched hydrocarbon chain

Contains the sulfhydryl group

Contains a sulfomethyl group (correct)

Which of amino acids has the basic properties? (Select all that apply)

Histidine Signup and view all the answers

Stereoisomers exist for all amino acids, except:

Glycine Signup and view all the answers

Lysine, arginine and __________ have no charge in the weakly alkaline medium:

Histidine Signup and view all the answers

All of these amino acids are hydrophobic (nonpolar), except:

Lysine Signup and view all the answers

The primary structure of the protein is:

The linear sequence of amino acids joined by peptide bonds in a protein Signup and view all the answers

The primary structure of a protein:

Is stabilized by peptide bonds that are formed between the α-amino and α-carboxyl groups of amino acids Signup and view all the answers

The basis of the protein primary structure is:

Polypeptide chain Signup and view all the answers

What types of relationships or interactions are characteristic of the protein primary structure?

The relationship between α-amino and α-carboxyl groups of amino acids Signup and view all the answers

Peptide bond in a protein:

Has a partial double character Signup and view all the answers

Salting-out is one of the methods used for protein isolation. Which protein properties most depend on the concentration of salts?

The degree of hydration of protein Signup and view all the answers

To obtain a native protein one can use the following method:

Sedimentation by salts of alkaline-earth metals Signup and view all the answers

Which of these methods results in a reversible precipitation of the protein?

Precipitation in the presence of ammonium sulfate – (NH4)2SO4 Signup and view all the answers

Choose a salt for reversible protein precipitation:

Ammonium sulfate Signup and view all the answers

Choose a salt for irreversible protein precipitation:

Silver nitrate Signup and view all the answers

What happens to the protein at high temperature in the presence of hydrochloric acid?

Hydrolysis Signup and view all the answers

One of the steps in studying the protein amino acid composition is its splitting into smaller peptides. For this purpose, it is possible to use:

Chymotrypsin Signup and view all the answers

The interaction __________ is the basis of Western blot:

Antigen-antibody Signup and view all the answers

An antibody labeled with an enzyme or isotope is called:

Molecular probe Signup and view all the answers

AIDS diagnosis by Western blot analysis includes all of the steps, except:

Salting-out of proteins Signup and view all the answers

The mixture of proteins was treated with sodium dodecyl sulfate and subjected to polyacrylamide gel electrophoresis (PAGE). The protein mobility in this electrophoresis depends on:

The molecular weight Signup and view all the answers

The mixture of proteins was treated with sodium dodecyl sulfate, applied to the polyacrylamide gel and separated by electrophoresis (PAGE). The proteins:

Moved to the anode Signup and view all the answers

What does 'the protein tertiary structure' imply?

The arrangement of entire polypeptide chain in space Signup and view all the answers

Study Notes

Isoleucine and Phenylalanine Side Chains

Isoleucine features a branched hydrocarbon chain, important for its hydrophobic properties.
Phenylalanine contains an aromatic ring, contributing to its unique biochemical behavior.

Methionine Side Chain Structure

Methionine includes a sulfomethyl group, distinguishing it from other amino acids with different functional groups.

Basic Properties of Amino Acids

Histidine is recognized for its basic properties, impacting its role in protein structures and functions.

Stereoisomers in Amino Acids

Glycine is the only amino acid without stereoisomers due to its non-chiral structure.

Charge in Weakly Alkaline Medium

Histidine, along with lysine and arginine, exhibits no charge in mildly alkaline conditions, affecting its reactivity.

Hydrophobic Amino Acids

Among listed amino acids, lysine is not hydrophobic (nonpolar), contrasting with the others like tryptophan and phenylalanine.

Primary Structure of Proteins

Defined as the linear sequence of amino acids connected by peptide bonds, crucial for understanding protein function.
Stabilized by peptide bonds formed between the α-amino and α-carboxyl groups of amino acids.

Basis of Protein Primary Structure

Composed primarily of polypeptide chains, which determine protein identity and function.

Characteristic Interactions in Primary Structure

Involves relationships between the α-amino and α-carboxyl groups, reflecting the covalent nature of peptide bonds.

Peptide Bond Properties

Peptide bonds possess partial double bond characteristics, leading to rigidity in protein structures and limiting rotation.

Salting-Out Method in Protein Isolation

Degree of hydration of proteins is influenced by salt concentration, which is critical for successful protein isolation.

Obtaining Native Proteins

Sedimentation by salts of alkaline-earth metals is an effective method to achieve native protein structures.

Reversible Protein Precipitation

Ammonium sulfate precipitation is a reversible process, enabling the recovery of proteins without permanent denaturation.

Irreversible Protein Precipitation

Silver nitrate is used for irreversible protein precipitation, often leading to protein denaturation.

Effects of High Temperature with Hydrochloric Acid

High temperatures in the presence of hydrochloric acid result in hydrolysis of proteins, damaging their structure.

Peptide Bond Cleavage

Chymotrypsin is utilized to split proteins into smaller peptides, aiding in the analysis of amino acid composition.

Western Blot Interactions

The antigen-antibody interaction forms the basis of the Western blot technique, crucial for protein detection.

Molecular Probes in Diagnostics

Enzyme or isotope-labeled antibodies are referred to as molecular probes, enhancing sensitivity in detection assays.

Steps in AIDS Diagnosis via Western Blot

Steps include applying molecular probes, separating proteins by molecular weight, and autoradiography; salting-out is not typically included.

Protein Mobility in PAGE

Protein mobility during polyacrylamide gel electrophoresis (PAGE) is primarily influenced by molecular weight, determining the separation efficacy.

Electrophoresis Movement

Proteins treated with sodium dodecyl sulfate (SDS) migrate towards the anode during electrophoresis, as they acquire a negative charge.

Tertiary Structure of Proteins

The tertiary structure refers to the three-dimensional arrangement of the entire polypeptide chain, crucial for protein functionality.

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Description

Test your knowledge on the structures of amino acids, specifically isoleucine and phenylalanine. This quiz will challenge you to identify key features of their side chains, including functional groups and structural characteristics. See how well you understand the building blocks of proteins!

Amino Acids Side Chains Quiz

Questions and Answers

Which of the following applies to the structure of the isoleucine side chain? (Select all that apply)

Which of the following applies to the structure of the phenylalanine side chain? (Select all that apply)

Which of the following applies to the structure of the methionine side chain? (Select all that apply)

Which of amino acids has the basic properties? (Select all that apply)

Stereoisomers exist for all amino acids, except:

Lysine, arginine and __________ have no charge in the weakly alkaline medium:

All of these amino acids are hydrophobic (nonpolar), except:

The primary structure of the protein is:

The primary structure of a protein:

The basis of the protein primary structure is:

What types of relationships or interactions are characteristic of the protein primary structure?

Peptide bond in a protein:

Salting-out is one of the methods used for protein isolation. Which protein properties most depend on the concentration of salts?

To obtain a native protein one can use the following method:

Which of these methods results in a reversible precipitation of the protein?

Choose a salt for reversible protein precipitation:

Choose a salt for irreversible protein precipitation:

What happens to the protein at high temperature in the presence of hydrochloric acid?

One of the steps in studying the protein amino acid composition is its splitting into smaller peptides. For this purpose, it is possible to use:

The interaction __________ is the basis of Western blot:

An antibody labeled with an enzyme or isotope is called:

AIDS diagnosis by Western blot analysis includes all of the steps, except:

The mixture of proteins was treated with sodium dodecyl sulfate and subjected to polyacrylamide gel electrophoresis (PAGE). The protein mobility in this electrophoresis depends on:

The mixture of proteins was treated with sodium dodecyl sulfate, applied to the polyacrylamide gel and separated by electrophoresis (PAGE). The proteins:

What does 'the protein tertiary structure' imply?

Study Notes

Isoleucine and Phenylalanine Side Chains

Methionine Side Chain Structure

Basic Properties of Amino Acids

Stereoisomers in Amino Acids

Charge in Weakly Alkaline Medium

Hydrophobic Amino Acids

Primary Structure of Proteins

Basis of Protein Primary Structure

Characteristic Interactions in Primary Structure

Peptide Bond Properties

Salting-Out Method in Protein Isolation

Obtaining Native Proteins

Reversible Protein Precipitation

Irreversible Protein Precipitation

Effects of High Temperature with Hydrochloric Acid

Peptide Bond Cleavage

Western Blot Interactions

Molecular Probes in Diagnostics

Steps in AIDS Diagnosis via Western Blot

Protein Mobility in PAGE

Electrophoresis Movement

Tertiary Structure of Proteins

Studying That Suits You

Description

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