protein structure
Secondary
Primary
Tertiary
This is how it further coils and fold into a specific 3D shape depending on its R groups
This is the way that the amino acids fold or coil into an a-helix or a b-pleated sheet, due to hydrogen bonds fromed between the oxygen and hydregens in the amoino acid
This is the sequence of the amino acids
+ info
+ info
+ info
Bonds & forces
Hydrophobic
What bonds form the secondary, tertiary and quaternary structures?
Van Der Waal
Hydrogen Bond
- Ionic Bonds: form between oppositly charged groups
- Disulfide Bonds: form between two suphur atoms
- Hydrogen Bonds: form between perminently polar groups
- Hydrophobic: these groups repel water and therfore often draw together
- Van Der Waal Forces: attraction between polar groups
Disulfide Bond
Ionic Bond
Quarternary Structure
This is the bonding between 2 or more different polypeptide chains that interact creating a 3D arreangment.Not every protein has quarterary. Some polypeptide chains attach to a non-protein substance known as a prosthetic group. The interaction between these two things makes a conjugated protein.
Globular Proteins
Fibourous Proteins
Protein types
Globular proteins and fibourous proteins
Haemoglobin
The Globular Protein
Haemoglobin is a pigment found in Red Blood Cells that enabel them to carry oxyben round the body for resperation. Haemolgobin proteins contains 2 dofferent types of polyertide chains: the aplpha chain (141 amino acids) and the beta chain (146 amino acids), It also a compound protein meaning it contains a prosthetic group called heme which allows the oxygen to attach to the protein due to the iron in the group (it has 4 heme groups), this makes it a conjugated protein. The protein is soluable which is important as oxygen isnt soluable and this allows it to be transported easily.
A disease linked to heamoglobin is called sickle cell anaemia which is when one amino acid is replaced on the surface of teh beta chain for a non polar amino acid which makes this much less soluable, This causes massive problembs.
Collagen
The Fibrous Protein
Collagen, an insoluble fibrous protein, is the most common protein found in animals. It is made of three polypeptide chains which are wound together to for a helix shape and because almost every third amino acid is glycine (the smallest amino acid) it allows the strands to be tightly wound as they can lie close together. The collagen strands then interact and run parallel to each other and form covalent bonds between the R groups of different stands. These cross-links hold the collagens together which forms fibril, with the ends of parallel molecules being staggered to avoid weak spots. The fibrils then create fibres by lying next to each other. Collagen fibres are then lined up in different directions depending on the forces they must withstand.
Collegen is necessary in the human body as it gives our skin strength and elasticity that protects the soft tissues underneath it, there are 30 different types of collagen that are found inthe body and they are all slightly different as they all are found in differnt parts and thererfore need to do slightly different things. The tesile strenth that it gives to the skin and other parts of the body comes from the stagered covalent bonds that are formed between the collegens. Also the many hydrogen bonds give it a greater strength. This is especially important for its role in the artery wall where it needs to be very strong as it must wothstand the high pressures exerted onto the artery wall and it must prevent them from bursting.
VS
Haemoglobin
Collagen
- Fibrous structure
- Insoluable
- Not conjugated
- Has not tertiary structure
- Has 3 polypeptide chains
- All polypeptide chains are identical
- Has a structural role
- Has a repeadted amino acid sequence
- Globuar structure
- Soluable
- Has a prothetic group (conjugated)
- Has a tertiary structure
- Has 4 polypeptide chains
- Has 2 diferent types of polypeptide chains (alpha & beta)
- Has a functional role of carrying oxygen
- Not a repeating amino acid sequence
Collagen and Haemoglobin
Rose Dixon
Created on October 12, 2021
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Transcript
protein structure
Secondary
Primary
Tertiary
This is how it further coils and fold into a specific 3D shape depending on its R groups
This is the way that the amino acids fold or coil into an a-helix or a b-pleated sheet, due to hydrogen bonds fromed between the oxygen and hydregens in the amoino acid
This is the sequence of the amino acids
+ info
+ info
+ info
Bonds & forces
Hydrophobic
What bonds form the secondary, tertiary and quaternary structures?
Van Der Waal
Hydrogen Bond
Disulfide Bond
Ionic Bond
Quarternary Structure
This is the bonding between 2 or more different polypeptide chains that interact creating a 3D arreangment.Not every protein has quarterary. Some polypeptide chains attach to a non-protein substance known as a prosthetic group. The interaction between these two things makes a conjugated protein.
Globular Proteins
Fibourous Proteins
Protein types
Globular proteins and fibourous proteins
Haemoglobin
The Globular Protein
Haemoglobin is a pigment found in Red Blood Cells that enabel them to carry oxyben round the body for resperation. Haemolgobin proteins contains 2 dofferent types of polyertide chains: the aplpha chain (141 amino acids) and the beta chain (146 amino acids), It also a compound protein meaning it contains a prosthetic group called heme which allows the oxygen to attach to the protein due to the iron in the group (it has 4 heme groups), this makes it a conjugated protein. The protein is soluable which is important as oxygen isnt soluable and this allows it to be transported easily.
A disease linked to heamoglobin is called sickle cell anaemia which is when one amino acid is replaced on the surface of teh beta chain for a non polar amino acid which makes this much less soluable, This causes massive problembs.
Collagen
The Fibrous Protein
Collagen, an insoluble fibrous protein, is the most common protein found in animals. It is made of three polypeptide chains which are wound together to for a helix shape and because almost every third amino acid is glycine (the smallest amino acid) it allows the strands to be tightly wound as they can lie close together. The collagen strands then interact and run parallel to each other and form covalent bonds between the R groups of different stands. These cross-links hold the collagens together which forms fibril, with the ends of parallel molecules being staggered to avoid weak spots. The fibrils then create fibres by lying next to each other. Collagen fibres are then lined up in different directions depending on the forces they must withstand.
Collegen is necessary in the human body as it gives our skin strength and elasticity that protects the soft tissues underneath it, there are 30 different types of collagen that are found inthe body and they are all slightly different as they all are found in differnt parts and thererfore need to do slightly different things. The tesile strenth that it gives to the skin and other parts of the body comes from the stagered covalent bonds that are formed between the collegens. Also the many hydrogen bonds give it a greater strength. This is especially important for its role in the artery wall where it needs to be very strong as it must wothstand the high pressures exerted onto the artery wall and it must prevent them from bursting.
VS
Haemoglobin
Collagen