2.4- PROTEINS
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- Created on: 12-02-15 12:51
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- 2.4- PROTEINS
- THE FOUR LEVELS OF PROTEIN ORGANISATION STRUCTURE
- Primary
- The order in which the specific amino acids are combined.
- The alpha-carbon is bonded to:
- A hydrogen atom
- A carboxyl group
- An amino group
- A variable group
- The alpha-carbon is bonded to:
- The order in which the specific amino acids are combined.
- Secondary
- Refers to the coiling or the folding of a polypeptide chain.
- The alpha helix structure resembles a coiled spring, and is secured by H-bonding in a peptide chain.
- The beta helix structure appears to be folded, and is held with H-bonding between peptide units of adjacent chains.
- Refers to the coiling or the folding of a polypeptide chain.
- Tertiary
- Refers to the 3D structure of the polypeptide chain.
- Hydrophobic interactions contribute to the folding and shaping of the protein.
- Hydrogen bonding helps to stabilise the protein structure
- Ionic bonding can occur between positive and negative R groups.
- Disulfide bridges are caused by covalent bonding between R groups of cysteine amino acids
- Refers to the 3D structure of the polypeptide chain.
- Quaternary
- Refers to the structure of a protein maromolecule formed by interactions between multiple peptide chains.
- Primary
- WHAT IS A PROTEOME?
- The entire complement of proteins that is, or can be, expressed by a cell, tissue or organism.
- TYPES OF PROTEIN
- Rubisco
- The enzyme (ribulose bisphosphate) that catalyses the first reaction of the Calvin Cycle.
- Insulin
- A hormone, produced by the pancreas, that causes a decrease in blood sugar levels and an increase of sugar inside the body’s cells.
- Immunoglobulin
- Another name for an antibody that recognises antigens, as part of the immune system’s response.
- Rhodopsin
- A pigment, found in the retina of the eye, which is particularly useful in conditions of low light.
- Collagen
- The main protein component of connective tissue, which is mostly found in skin, tendons and ligaments.
- Spider silk
- A fibrous protein spun by spiders, for making webs and drop lines, and building nests
- Rubisco
- FIBROUS AND GLOBULAR PROTEINS
- Fibrous Proteins
- Shape: Long and narrow.
- Role: Structural, for strength and support.
- Solubility: (Generally) insoluble in water.
- Sequence: Repetitive amino acid sequence.
- Stability: Less sensitive to changes in temperature, pH, etc.
- Examples: Collagen, fibrin, keratin, elastin.
- Globular Proteins
- Shape: Spherical.
- Function: Functional, for transport, catalysing reactions.
- Solubility: (Generally) soluble in water.
- Sequence: Irregular amino acid sequence.
- Stability: More sensitive to changes in temperature, pH, etc.
- Examples: Catalase, haemoglobin, insulin.
- Fibrous Proteins
- POLAR AND NON-POLAR AMINO ACIDS
- Polar Amino Acids
- Hydrophilic R groups.
- For water-soluble proteins, they are found on the surface.
- For membrane-bound proteins, they line the interior pores.
- Non-Polar Amino Acids
- Hydrophobic R groups.
- For water-soluble proteins, they are found in the centre.
- For membrane-bound proteins, they line the interior pores.
- Polar Amino Acids
- http://www.ib.bio ninja.com.au/ higher-level/topic-7-nucleic-acids-and/75-proteins.html
- THE FOUR LEVELS OF PROTEIN ORGANISATION STRUCTURE
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