IPS1- Classification of Amino acid Based on Structure

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40 Terms

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300 amino acids

Over _____ amino acids exist in nature

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20

Over 300 amino acids exist in nature, but proteins are made mainly from ____special ones called L-α-amino acids

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L-α-amino acids

Over 300 amino acids exist in nature, but proteins are made mainly from 20 special ones called_____

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True

[Amino Acid]

[T/F] 

Out of these 20 amino acids ,

  • 10 are essential (we must get them from food)

  • 10 are nonessential (our bodies can make them).

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7 types

Amino acids are grouped into ____ types based on their structure

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3-letter code and a 1-letter code

These amino acids are grouped into 7 types based on their structure. Each one has a _____ and ____ to represent it. 

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Selenocysteine

The 21st protein L-α-amino acid

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Selenocysteine

____- is a special amino acid found in many living things

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Selenocysteine

It’s like cysteine, but it has selenium instead of sulfur

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Selenocysteine

_____-

  • Is added directly to proteins during translation (when RNA is turned into protein), not after the protein is made.

  • Is only in translation not in transcription

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Selenocysteine

Unlike the other 20 amino acids, it doesn't use a regular 3-letter codon in the genetic code.

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Amino acids with nonpolar side chains

[CLASSIFICATION OF AMINO ACID ACCORDING TO SIDE CHAIN]

These amino acids don’t give or take protons and don’t form hydrogen or ionic bonds

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hydrophobic (don’t mix with water).

[CLASSIFICATION OF AMINO ACID ACCORDING TO SIDE CHAIN]

Amino acids with nonpolar side chains  are like oil or fat, so they are____ [hydrophillic /hydrophobic]

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  • Glycine

  • Alanine

  • Valine

  • Leucine

  • Isoleucine

  • Methionine

  • Phenylalanine

  • Tryptophan

  • Proline 

Examples of Amino acids with nonpolar side chains [9]

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  • Phenylalanine

  • Tryptophan

  • Proline 

[CLASSIFICATION OF AMINO ACID ACCORDING TO SIDE CHAIN]

Most Amino acids with nonpolar side chains  are ALIPATHIC HYDROCARBON  except ___ [3] which are CLOSED RING HC STRUCTURE 

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Amino acids with uncharged POLAR side groups

[CLASSIFICATION OF AMINO ACID ACCORDING TO SIDE CHAIN]

These amino acids are having zero net charge at neutral pH.

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  • Serine

  • Threonine

  • Cysteine

  • Aspargine

  • Glutamine

Example of Amino acids with uncharged POLAR side groups [5]

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True

[CLASSIFICATION OF AMINO ACID ACCORDING TO SIDE CHAIN]

[T/F]

Amino acids with uncharged POLAR side groups

  • In the case of Cysteine and Tyrosine , they can lose proton at alkaline pH.

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Amino acids with acidic side chains

[CLASSIFICATION OF AMINO ACID ACCORDING TO SIDE CHAIN]

____-

  • These amino acids are proton donors

  • They are fully ionized in neutral pH forming a negatively charged carboxylate group (-COO- )

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  • Aspartic acid

  • Glutamic acid 

Example of Amino acids with acidic side chains [2] 

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UNDERSTAND

Ionization of aspartic and glutamic acid

  • The acid group (shown in the green box) loses a proton, which is typical acid behavior. 

<p><strong>Ionization of aspartic and glutamic acid</strong></p><ul><li><p>The acid group (shown in the green box) loses a proton, which is typical acid behavior.&nbsp;</p></li></ul><p></p>
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UNDERSTAND

This turns it into a carboxylate group (COO⁻), 

<p>This turns it into a carboxylate group (COO⁻),&nbsp;</p>
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Amino acids with basic side chains

[CLASSIFICATION OF AMINO ACID ACCORDING TO SIDE CHAIN]

These amino acids accept protons, based on the Bronsted-Lowry theory.

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  • Lysine

  • Arginine

  • Histidine

Example of Amino acids with basic side chains [3]

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True 

[T/F]

Lysine (Lys) and Arginine (Arg) are fully charged and positive. 

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Histidine (His)

_____- is a weak base. By itself, it’s not charged, but in proteins, its side chain can be positive or neutral.

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  • Arginine

  • Asparagine

  • Aspartic acid

  • Cysteine

  • Glutamic acid

  • Glutamine

  • Glycine

  • Histidine

  • Lysine

  • Serine

  • Threonine

🧬 Hydrophilic Amino Acids [11]

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  • Alanine

  • Isoleucine

  • Leucine

  • Methionine

  • Phenylalanine

  • Proline

  • Tryptophan

  • Tyrosine

  • Valine

💧 Hydrophobic Amino Acids [9]

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R-groups (side chains)

The _____of amino acids help enzymes do their jobs.

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imidazole ring

The______ ring in histidine can give or take protons at normal body pH. This makes it important for enzyme reactions and for balancing H⁺ ions in red blood cells.

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  • alcohol groups

  • nucleophiles

The ____groups in serine and threonine, and the -SH group in cysteine, let these amino acids act as____ during enzyme reactions

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nucleophiles

____- attack other molecules during enzyme reactions

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  • –SH group

  • disulfide bonds

The______ groups in cysteine can form _____ with another cysteine, helping shape and stabilize proteins

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–OH groups

The ___ groups in serine, tyrosine, and threonine help control enzyme activity.

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  • 300 natural amino acids

  • 20

There are over _____ natural amino acids, but only____make up proteins.

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True

[T/F]

  • Humans and animals can’t make 10 of these 20 amino acids in enough amounts for growth and health.

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  • essential

  • non-essential 

Amino acids are called : 

  • [essential / non-essential] ______- if we must get them from food

  • [essential / non-essential] _____ - if our body can make them 

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True

[T/F]

  • We can’t make essential amino acids because our DNA doesn’t have the instructions for them.

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Aspartic acid

Amide of Asparagine (Asn)

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Glutamic acid

Amide of Glutamine