Proteins And Mutations

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Products of transcription and translation of nucleic acids. It is where the information stored and delivered by the nucleic acid is manifested

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Proteins

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Building blocks of proteins that provides energy through generation of ATP

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Amino acids

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Structural composition of amino acids Funct

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Amino group (NH3) and Carboxyl group (-COOH)

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Functions of amino acids

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- Cellular structure and support

- Biosynthesis of enzymes and hormones

- Production of antibodies

- Exhibit a number of chemical messaging patterns

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How many amino acids are needed to make every type of protein?

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20

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Types of protein

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- Essential

- Conditionally Essential

- Non-Essential

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Amino acid we only get from the food we eat

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Essential

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Amino acids where healthy bodies can make under normal circumstances

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Conditionally Essential

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Amino acid that we can get from food but our body can also make

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Non-Essential

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What are the essential amino acids?

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HILLMPTTV (HILLs ang MaPa na Tinravel sa TV)

- Histidine

- Isoleucine

- Leucine

- Lysine

- Methionine

- Phenylalanine

- Threonine

- Tryptophan

- Valine

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What are the conditionally essential amino acids?

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ACGPGT (Ang Classmate kong si Gerald ay sumali ng Pilipinas Got Talent)

- Arginine

- Cystine

- Glutamine

- Glycine

- Proline

- Tyrosine

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What are the non-essential proteins?

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GAAAS

- Glutamate

- Alanine

- Asparagine

- Aspartate

- Serine

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Amino acids with aliphatic side chains; Hydrophobic

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Non-polar amino acids

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Examples of non-polar amino acids

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Alanine, Leucine, Isoleucine, Proline, Valine, Tryptophan, Methionine, Phenylalanine

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Amino acids that are uncharged and hydrophilic

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Polar amino acids

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Examples of Polar amino acids

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Glycine, Serine, Threonine, Cysteine, Tyrosine, Asparagine, Glutamine

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Amino acids that are negatively charged and hydrophilice

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Acidic amino acids

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Examples of Acidic amino acids

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Aspartic acid and Glutamic acid

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Amino acids that are positively charged and hydrophilic

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Basic amino acids

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Examples of basic amino acids

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Arginine, Lysine, Histidine

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Amino acids that can either be hydrophobic or Hydrophilic

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Phenylalanine, Tryptophan, Tyrosine

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Protein structure where the sequence of amino acids are linear; Linked with peptide bonds and its polypeptide chains are unbranched

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Primary structure

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Protein structure where interactions between amino acid side chains fold a protein into predictable configurations; Linked with Hydrogen bond and has alpha-helix and beta sheet as its major structure

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Secondary structure

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Protein structure that has a 3D shape; Folding of polypeptide chain, driven by hydrophobic amino acids; Van der Waals forces can also contribute to its structure

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Tertiary structure

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A protein structure where protein or polypeptide has two or more polypeptide chains or subunits that can interact withor each other

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Quaternary Structure

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Ordered sequence of nucleotides on a chromosome that encodes a specific functional group; Fundamental unit of inheritance

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Gene

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The process by which a gene’s information is converted into the structures and functions of a cell process of producing a biologically functional molecule (Protein or RNA)

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Gene Expression

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Sequence of three DNA or RNA nucleotides that corresponds with a specific amino acid or stop signal during protein synthesis

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Codon

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How many sense codons does a human have?

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61

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How many stop codon?

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Three (3)

(UAA, UGA, UAG)

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Start codon

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Methionine (AUG)

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Which codon are specific?

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Methionine (AUG) and Tryptophan (UGG)

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Characteristics of the genetic code

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- Specificity

- Universality

- Degeneracy

- Non-overlapping and comma less

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Characteristic: A particular codon always codes for the same amino acid

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Specificity

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Characteristic: Its specificity has been conserved from very early stages of evolution, with only slight differences in the manner in which the code is translated

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Universality

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Characteristic: Redundant; A given amino acid may have more then one triplet coding for it

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Degeneracy

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Characteristic: The code is read from a fixed starting point as a continuous sequence of bases, taken three at a time without any punctuation between codons

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Non-overlapping and comma less

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Process of copying one strand of DNA into RNA thru a process similar to that of DNA replication

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Transcription

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RNA polymerase binds to a region of a gene called promoter

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Initiation

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Addition of nucleotide to the mRNA strand

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Elongation

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mRNA strand is complete and detaches from DNA

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Termination

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A process in which genetic code in the mRNA is read to make a protein

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Translation

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Process of Translation

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MR CAT APP

Messenger RNA goes to

Ribosomes which read the sequence in three’s called

Codons are recognized by

Anticodons found in the

Transfer RNA which carries

Amino acids which is join via

Peptide bonds to form

Polypeptide chain/Protein

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Change in the DNA sequence due to; Altering of the nucleotide sequence; Changes in the nucleotide sequence of a DNA that escape proof reading and repair

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Mutations

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Classifications of Mutations

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Spontaneous mutation and Induced mutation

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Mutation that occurs during normal cells processes

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Spontaneous mutations

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Mutation wherein the rate of mutation can be increased by chemical/radiation

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Induced mutation

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Mutation: codon with a changed base codes for the same amino acid

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Silent mutation

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Mutation: codon with the changed base codes for a different amino acid

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Missense mutation

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Mutation: codon with changed bass becomes a termination codon

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Nonsense mutation

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Mutation: A sequence of three bases that is repeated in tandem will become amplified in number so that too many copies of the triplet occur

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Trinucleotide repeat expansion

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Mutation: One base is incorrectly added during replication and replaces the pair in corresponding position on the complementary strand

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Substitution

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Mutation: Mutations at mut can alter the way introns are removed from pre-mRNA molecules producing aberrant proteins

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Splice mutations

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Mutation: One or two nucleotides are either deleted or added to the coding region of an mRNA, altering the reading frame

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Frameshift mutations

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Mutation: Insertion or deletion that takes place in a multiple of 3 nucleotides and does not lead to any shift in the reading frame

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Non-frameshift mutation

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Disease having a missense in the hemoglobin beta

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Sickle cell anemia

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Missense in the fribrillin

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Marfan Syndrome

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Deletion of Dystrophin,DMD

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Muscular Dustrophy

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Missense in p53 tumorsupressor gene, TP53

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Li-Fraumeni syndrome

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Missense frameshift and splice site mutations in homogentisic acid oxidase

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Alkaptonuria (ochronosis)

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Deletion of CFTR gene

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Cystic fibrosis

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Deletion of 5p

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Cri-du-chat syndrome

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Splice site, missense or deletion of phenylalanine hydroxylass, PAH or PKU1

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Phenylketonuria

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Expanding trinucleotide repeat of Fragile X mental retardation 2

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Fragile XE

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Expanding trinucleotide repeat on HTT gene

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Huntington’s Disease