Proteins: Functions, Structure and Synthesis Flashcards
What are the main functions of proteins?
-Carry out enzymatic functions
-Generating movements of cells
-Carrying signals from cell to cell and within individual cells
-Providing support to cells and tissues
What are the main features of proteins?
- Proteins are linear chains of amino acids arranged in a 3D structural hierarchy
- Diversity of structures, resulting in a wide range of functions. Functions depend on the 3D protein structure. Its 3D structure is determined by a proteins amino acid sequence.
Without its normal conformation (native folding), the protein loses its biological activity.
What are IDSs? Intrinsically disordered Proteins?
Are proteins that have lost their native, functional folding, resulting in an insoluble aggregation in many organs (causing many diseases)
What can the accumulation lead to?
the neurotoxic effects in neurodegeneration diseases: Beta amyloid protein is one of the IDPs associated with neurodegenerative diseases like Parkinsons, prion disease and Alzheimers diseases.
What are amino acid monomers?
- Proteins are assembled essentially from a set of 20 different amino acids
- Amino acids have in common: Carbon a(alpha), amino (-NH2) and carboxyl (-COOH) functional groups
- R group or side chain is specific for each amino acid
What makes up an amino acid?
-Alpha carbon, amino and carboxyl
What are peptide bonds between amino acids called?
Polypeptides
What do the peptide bonds between amino acids do? diagram
- In a protein, amino acids are linked together by covalent peptide bonds formed between carboxylic acid and amino groups of two consecutive amino acids.
- The continuous peptide bonds between amino acids form linear, unbranched polypeptides and the backbone of the protein.
- The R groups are protruding the outside
- Every proteing has a unique sequence of amino acids with a carboxyl end (C-term) and an amino end (N-term)
What is the four level protein structure?
he architecture of proteins has four levels of organisation: Primary, Secondary, Tertiary and Quaternary
What is the Primary structure of proteins?
- The unique sequence of amino acids in a polypeptide chain, with no folding
Based on the length of the sequence:
- Peptide=short chain(<50 amino acids)
- Protein=longer chain (>50 amino acids)
Also referred to polypeptides. Both are composed of repetition of amino acids.
What is the Secondary Structure of proteins?
- Secondary structure consists of stable spatial coils and folds of segments within a polypeptide chain. They are formed by H-bonds between the backbone amino and carbonyl groups and often involving repeating structural patterns (helices and sheets)
- Typical secondary structures are:
-Coil called (alpha a) helix
-Folded structure called B (beta) pleated sheet related to its amino acid sequence
What is the Tertiary Structure of Proteins ?
- Tertiary structure is the three-dimensional folding pattern determine by interactions among various side chains. It determines the overall folding/conformation of a polypeptide chain subunit.
- It is stabilised primarily by:
-Hydrophobic interactions (weak and reversible) between non-polar side chains
-Ionic bonds and strong covalent bonds called disulfide bridges (of cysteines) between non-polar side chains.
-Hydrogen bonds involving polar side chains and backbone amino/carboxyl groups
What is the Quaternary Structure of Proteins?
- Quaternary structure is the result of the association of two or more polypeptide chain subunits into a closely packed arrangement. For example:
1) Haemoglobin, to transport oxygen in red blood cells, consisting of four polypeptide chains: two a (alpha) and two (B beta)
2) Tubulin, the component of microtubules, consisting of 2 polypeptide chains: a (alpha) and B(beta)
How do you recognise DNA structure?
deoxyribose lacking OH-at 2’, nucleotide sugar (Pentose)
-double stranded
How do you recognise RNA structure?
RNA-Ribose having OH- at 2’’, nucleotide sugar (Pentose)
-single stranded
What is protein synthesis in Eukaryotic cells?
Protein synthesis (or gene expression) consists in two phases-transcription and translation (separated by the RNA maturation in the eukaryotic cells)
Where does Transcription take place?
Where does Translation take place?
What is Transcription?
The process of converting DNA (double stranded) to mRNA(single stranded)
-It occurs in the nucleus
Why does Transcription take place inside the nucleus?
DNA is too large to leave the nucleus (RNA can pass through the nuclear pores)
What is the process of Transcription?
RNA polymerase uses one of DNA strands as a template to produce pre-messenger RNA (pre-mRNA-codes for proteins) with a complementary sequence to DNA.
- It adds nucelotides (complementary base pairing -U INSTEAD OF T) in the 5’-3’ direction.
- Only 1 strand of the 2 strands of DNA is transcribed.
- DNA transcription consists of 3 stages
What are the 3 stages of Transcription?
-Initiation
-Elongation
-Termination
DNA Transcription -Initiation
Initiation step - RNA polymerase, with the help of transcription factors, binds to a specific sequence of DNA (promoter-just before the start site of a gene). Each gene has its own promoter. This ensures that the genetic region will be transcribed into RNA.
- RNA polymerase separates the double strands and use a single strand as a template
- 2 initial RNA nucleotides are joined together to begin the complementary RNA strand synthesis