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Alles über Proteine: Von Primärstruktur bis Quartärstruktur und Aminosäuren

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Alles über Proteine: Von Primärstruktur bis Quartärstruktur und Aminosäuren
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Laura

@lauraxsn

·

134 Follower

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Proteins and amino acids are fundamental building blocks of life. This document explores their structure, properties, and functions in detail. Proteinogenic amino acids form the basis of protein molecules, with each having unique characteristics based on their side chains. The document covers amino acid structure, isoelectric points, and peptide bond formation.

3.5.2021

12115

Aminosäure
Strukturformel:
COOH
I
H₂N-C-H
I
R
L-Aminosäure
COOH
I
H-C-NH2
T
R
D-Aminosäure/
kommt in der Natur vor / Aminogruppe ist in der

Amino Acid Structure and Properties

Amino acids are the building blocks of proteins. They have a central carbon atom (α-carbon) bonded to an amino group, a carboxyl group, a hydrogen atom, and a variable side chain (R group).

Key points about amino acid structure:

  • Amino acids exist in L- and D-forms, with L-forms predominating in nature.
  • They can act as acids or bases (ampholytes) depending on pH.
  • At their isoelectric point, amino acids exist as zwitterions with a neutral net charge.

Definition: The isoelectric point is the pH at which an amino acid has no net electrical charge.

Highlight: Amino acids exhibit chirality due to their asymmetric α-carbon, resulting in optical activity.

The document explains how amino acids change their ionic form based on pH, which is crucial for understanding their behavior in biological systems and laboratory techniques like electrophoresis.

Vocabulary: Zwitterion - A molecule with both positive and negative charges, but a net neutral charge overall.

Calculation of the isoelectric point is briefly mentioned, which is essential for predicting amino acid behavior in different pH environments.

Aminosäure
Strukturformel:
COOH
I
H₂N-C-H
I
R
L-Aminosäure
COOH
I
H-C-NH2
T
R
D-Aminosäure/
kommt in der Natur vor / Aminogruppe ist in der

Öffnen

Peptide Bond Formation

The final section explains the formation of peptide bonds, which is the fundamental process in protein synthesis.

Key points about peptide bond formation:

  • Two amino acids react through a condensation reaction, releasing a water molecule.
  • The peptide bond forms between the carboxyl group of one amino acid and the amino group of another.
  • The resulting molecule is called a dipeptide.

Vocabulary: Condensation reaction - A reaction in which two molecules combine to form a larger molecule, typically with the loss of a small molecule such as water.

The document describes the structure of a peptide, including:

  • N-terminal end
  • C-terminal end
  • Peptide bond

Highlight: The peptide bond is very stable, while the terminal ends can react further to form longer chains.

Classification of peptide chains:

  • Oligopeptides: 2 to 9 amino acid residues
  • Polypeptides: 10 to 100 amino acid residues
  • Proteins: more than 100 amino acid residues

This information is crucial for understanding how individual amino acids come together to form the complex structures of proteins, which are essential for numerous biological functions.

Example: The dipeptide formed by alanine and glycine is shown, illustrating the peptide bond formation process.

The document also mentions mesomeric boundary formulas, which help explain the planar nature and partial double bond character of the peptide bond. This structural feature is critical for understanding higher-order protein structures.

Aminosäure
Strukturformel:
COOH
I
H₂N-C-H
I
R
L-Aminosäure
COOH
I
H-C-NH2
T
R
D-Aminosäure/
kommt in der Natur vor / Aminogruppe ist in der

Öffnen

Amino Acid Titration Curve

The document presents a titration curve for glycine, illustrating how the ionic state of an amino acid changes with pH.

Key points of the titration curve:

  1. At low pH, glycine exists predominantly as a cation (positively charged ion).
  2. As pH increases, there's a point where cations and zwitterions are present in equal amounts, exhibiting strong buffering capacity.
  3. At the isoelectric point (pI), glycine exists entirely as zwitterions.
  4. Further increase in pH leads to a mixture of zwitterions and anions, again with strong buffering capacity.
  5. At high pH, glycine exists predominantly as an anion (negatively charged ion).

Definition: Buffering capacity refers to the ability of a solution to resist changes in pH when acids or bases are added.

This titration curve is essential for understanding how amino acids behave in different pH environments, which is crucial for various biochemical processes and laboratory techniques.

Highlight: The isoelectric point (pI) for glycine is shown to be around pH 6, which is characteristic for this amino acid.

Understanding titration curves is vital for predicting amino acid behavior in different physiological conditions and for designing experiments involving proteins.

Aminosäure
Strukturformel:
COOH
I
H₂N-C-H
I
R
L-Aminosäure
COOH
I
H-C-NH2
T
R
D-Aminosäure/
kommt in der Natur vor / Aminogruppe ist in der

Öffnen

Proteinogenic Amino Acids

This section provides a comprehensive overview of the 22 proteinogenic amino acids that serve as the building blocks for proteins in living organisms.

The amino acids are categorized into four main groups based on their side chain properties:

  1. Neutral amino acids with nonpolar side chains
  2. Neutral amino acids with polar side chains
  3. Acidic amino acids
  4. Basic amino acids

Example: Glycine (Gly) is the simplest amino acid with just a hydrogen atom as its side chain.

The document presents a detailed table of all proteinogenic amino acids, including their full names, three-letter codes, and structural formulas. This information is crucial for understanding protein structure and function.

Highlight: Some amino acids are classified as essential amino acids, meaning they cannot be synthesized by the human body and must be obtained through diet.

Special attention is given to amino acids with unique properties:

  • Proline, which has a cyclic structure
  • Selenocysteine and pyrrolysine, which are less common but still considered proteinogenic

This comprehensive list of amino acids is vital for students and researchers studying protein structure and function.

Aminosäure
Strukturformel:
COOH
I
H₂N-C-H
I
R
L-Aminosäure
COOH
I
H-C-NH2
T
R
D-Aminosäure/
kommt in der Natur vor / Aminogruppe ist in der

Öffnen

Aminosäure
Strukturformel:
COOH
I
H₂N-C-H
I
R
L-Aminosäure
COOH
I
H-C-NH2
T
R
D-Aminosäure/
kommt in der Natur vor / Aminogruppe ist in der

Öffnen

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Alles über Proteine: Von Primärstruktur bis Quartärstruktur und Aminosäuren

user profile picture

Laura

@lauraxsn

·

134 Follower

Follow

Proteins and amino acids are fundamental building blocks of life. This document explores their structure, properties, and functions in detail. Proteinogenic amino acids form the basis of protein molecules, with each having unique characteristics based on their side chains. The document covers amino acid structure, isoelectric points, and peptide bond formation.

3.5.2021

12115

 

11/12

 

Chemie

462

Aminosäure
Strukturformel:
COOH
I
H₂N-C-H
I
R
L-Aminosäure
COOH
I
H-C-NH2
T
R
D-Aminosäure/
kommt in der Natur vor / Aminogruppe ist in der

Amino Acid Structure and Properties

Amino acids are the building blocks of proteins. They have a central carbon atom (α-carbon) bonded to an amino group, a carboxyl group, a hydrogen atom, and a variable side chain (R group).

Key points about amino acid structure:

  • Amino acids exist in L- and D-forms, with L-forms predominating in nature.
  • They can act as acids or bases (ampholytes) depending on pH.
  • At their isoelectric point, amino acids exist as zwitterions with a neutral net charge.

Definition: The isoelectric point is the pH at which an amino acid has no net electrical charge.

Highlight: Amino acids exhibit chirality due to their asymmetric α-carbon, resulting in optical activity.

The document explains how amino acids change their ionic form based on pH, which is crucial for understanding their behavior in biological systems and laboratory techniques like electrophoresis.

Vocabulary: Zwitterion - A molecule with both positive and negative charges, but a net neutral charge overall.

Calculation of the isoelectric point is briefly mentioned, which is essential for predicting amino acid behavior in different pH environments.

Aminosäure
Strukturformel:
COOH
I
H₂N-C-H
I
R
L-Aminosäure
COOH
I
H-C-NH2
T
R
D-Aminosäure/
kommt in der Natur vor / Aminogruppe ist in der

Peptide Bond Formation

The final section explains the formation of peptide bonds, which is the fundamental process in protein synthesis.

Key points about peptide bond formation:

  • Two amino acids react through a condensation reaction, releasing a water molecule.
  • The peptide bond forms between the carboxyl group of one amino acid and the amino group of another.
  • The resulting molecule is called a dipeptide.

Vocabulary: Condensation reaction - A reaction in which two molecules combine to form a larger molecule, typically with the loss of a small molecule such as water.

The document describes the structure of a peptide, including:

  • N-terminal end
  • C-terminal end
  • Peptide bond

Highlight: The peptide bond is very stable, while the terminal ends can react further to form longer chains.

Classification of peptide chains:

  • Oligopeptides: 2 to 9 amino acid residues
  • Polypeptides: 10 to 100 amino acid residues
  • Proteins: more than 100 amino acid residues

This information is crucial for understanding how individual amino acids come together to form the complex structures of proteins, which are essential for numerous biological functions.

Example: The dipeptide formed by alanine and glycine is shown, illustrating the peptide bond formation process.

The document also mentions mesomeric boundary formulas, which help explain the planar nature and partial double bond character of the peptide bond. This structural feature is critical for understanding higher-order protein structures.

Aminosäure
Strukturformel:
COOH
I
H₂N-C-H
I
R
L-Aminosäure
COOH
I
H-C-NH2
T
R
D-Aminosäure/
kommt in der Natur vor / Aminogruppe ist in der

Amino Acid Titration Curve

The document presents a titration curve for glycine, illustrating how the ionic state of an amino acid changes with pH.

Key points of the titration curve:

  1. At low pH, glycine exists predominantly as a cation (positively charged ion).
  2. As pH increases, there's a point where cations and zwitterions are present in equal amounts, exhibiting strong buffering capacity.
  3. At the isoelectric point (pI), glycine exists entirely as zwitterions.
  4. Further increase in pH leads to a mixture of zwitterions and anions, again with strong buffering capacity.
  5. At high pH, glycine exists predominantly as an anion (negatively charged ion).

Definition: Buffering capacity refers to the ability of a solution to resist changes in pH when acids or bases are added.

This titration curve is essential for understanding how amino acids behave in different pH environments, which is crucial for various biochemical processes and laboratory techniques.

Highlight: The isoelectric point (pI) for glycine is shown to be around pH 6, which is characteristic for this amino acid.

Understanding titration curves is vital for predicting amino acid behavior in different physiological conditions and for designing experiments involving proteins.

Aminosäure
Strukturformel:
COOH
I
H₂N-C-H
I
R
L-Aminosäure
COOH
I
H-C-NH2
T
R
D-Aminosäure/
kommt in der Natur vor / Aminogruppe ist in der

Proteinogenic Amino Acids

This section provides a comprehensive overview of the 22 proteinogenic amino acids that serve as the building blocks for proteins in living organisms.

The amino acids are categorized into four main groups based on their side chain properties:

  1. Neutral amino acids with nonpolar side chains
  2. Neutral amino acids with polar side chains
  3. Acidic amino acids
  4. Basic amino acids

Example: Glycine (Gly) is the simplest amino acid with just a hydrogen atom as its side chain.

The document presents a detailed table of all proteinogenic amino acids, including their full names, three-letter codes, and structural formulas. This information is crucial for understanding protein structure and function.

Highlight: Some amino acids are classified as essential amino acids, meaning they cannot be synthesized by the human body and must be obtained through diet.

Special attention is given to amino acids with unique properties:

  • Proline, which has a cyclic structure
  • Selenocysteine and pyrrolysine, which are less common but still considered proteinogenic

This comprehensive list of amino acids is vital for students and researchers studying protein structure and function.

Aminosäure
Strukturformel:
COOH
I
H₂N-C-H
I
R
L-Aminosäure
COOH
I
H-C-NH2
T
R
D-Aminosäure/
kommt in der Natur vor / Aminogruppe ist in der
Aminosäure
Strukturformel:
COOH
I
H₂N-C-H
I
R
L-Aminosäure
COOH
I
H-C-NH2
T
R
D-Aminosäure/
kommt in der Natur vor / Aminogruppe ist in der

Nichts passendes dabei? Erkunde andere Fachbereiche.

Knowunity ist die #1 unter den Bildungs-Apps in fünf europäischen Ländern

Knowunity wurde bei Apple als "Featured Story" ausgezeichnet und hat die App-Store-Charts in der Kategorie Bildung in Deutschland, Italien, Polen, der Schweiz und dem Vereinigten Königreich regelmäßig angeführt. Werde noch heute Mitglied bei Knowunity und hilf Millionen von Schüler:innen auf der ganzen Welt.

Ranked #1 Education App

Laden im

Google Play

Laden im

App Store

Knowunity ist die #1 unter den Bildungs-Apps in fünf europäischen Ländern

4.9+

Durchschnittliche App-Bewertung

13 M

Schüler:innen lieben Knowunity

#1

In Bildungs-App-Charts in 12 Ländern

950 K+

Schüler:innen haben Lernzettel hochgeladen

Immer noch nicht überzeugt? Schau dir an, was andere Schüler:innen sagen...

iOS User

Ich liebe diese App so sehr, ich benutze sie auch täglich. Ich empfehle Knowunity jedem!! Ich bin damit von einer 4 auf eine 1 gekommen :D

Philipp, iOS User

Die App ist sehr einfach und gut gestaltet. Bis jetzt habe ich immer alles gefunden, was ich gesucht habe :D

Lena, iOS Userin

Ich liebe diese App ❤️, ich benutze sie eigentlich immer, wenn ich lerne.