MindMap Gallery Protein structure and function mind map
This is a mind map about the structure and function of proteins, including amino acid structure and function, protein structure, special proteins, protein physical and chemical properties, etc. Hope this helps!
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This is a mind map about bacteria, and its main contents include: overview, morphology, types, structure, reproduction, distribution, application, and expansion. The summary is comprehensive and meticulous, suitable as review materials.
This is a mind map about plant asexual reproduction, and its main contents include: concept, spore reproduction, vegetative reproduction, tissue culture, and buds. The summary is comprehensive and meticulous, suitable as review materials.
This is a mind map about the reproductive development of animals, and its main contents include: insects, frogs, birds, sexual reproduction, and asexual reproduction. The summary is comprehensive and meticulous, suitable as review materials.
protein structure and function
Amino acid structure and function
Amino acids are the basic building blocks of protein
L-a-amino acid
Except glycine because it is symmetrical
Amino acid composition
Amino
carboxyl
Start with the amino group
left to right
connected by peptide bonds
Main chain skeleton: CONHCONHCONH
Amino acid classification
due to side chain properties
acidic amino acids
All non-essential amino acids
Aspartic acidAsp
Glutamic acidGlu
Tiandong Valley
Since the side chain is a carboxyl group, so ask: Amino acids containing two carboxyl groups Answer: Tiandonggu of acidic amino acids
basic amino acids
ArginineArg
LysineLys
HistidineHis
Seiyagumi
Nonpolar aliphatic amino acids, polar aliphatic amino acids, aromatic amino acids
imino acid
proline
Synthetic polypeptide chain processing and production
Hydroxyproline
The strongest polarity
Cysteine
Sulfhydryl-containing -SH sulfur-containing amino acid
disulfide bond to form cystine
So the reason why many proteins have i-sulfhydryl groups is that they are composed of cysteine
essential amino acids
formula
non-essential amino acids
Can be synthesized in the body
Physical and chemical properties
Two-phase ionization
There are both amino and carboxyl groups
There is an isoelectric point
At this pH, acidic ionization and alkaline ionization tend to be the same
Separating proteins using different isoelectric points
Does not swim at the isoelectric point
Contains conjugated double bonds and can absorb ultraviolet A280nm
Ninhydrin can react to form a blue-violet compound
active peptide
GlutathioneGSH
Contains sulfhydryl groups and has reducing properties
Plays an important reducing role in the body
Dehydrogenase produces reduced form
gamma peptide bond
If there is less glucose-6-phosphate dehydrogenase in red blood cells, less reduced glutathione will result in anemia.
neonatal hemolytic jaundice
peptide hormone
protein structure
The order of amino acids is the primary structure
peptide bond link
Protein spatial conformation mainly depends on primary conformation
The primary structure determines the high-level structure
The primary structure is the same and the functions are relatively the same.
secondary structure
Primary structural fold: a helix
Clockwise right hand spiral around center
If the helical acceptor group interaction is weakened, helix formation is more likely
Each amino group forms a hydrogen bond with the fourth carboxyl group
beta sheet
lamellar structure
origami zigzag
Carboxyl oxygen and imino hydrogen form hydrogen bonds
within globular protein
β corner,
180 fold
The second residue is often proline
Omega Ring
Used for molecular recognition on protein surfaces
Can form a motif
Hydrogen bond maintenance
The local spatial structure of a certain peptide chain
Spatial structure that does not involve the side chains of amino acid residues
Relative spatial structure of main chain atoms
However, residue side chains will affect the generation of secondary structure.
tertiary structure
Hydrophobic bonds remain stable
Refers to the relative spatial position of all amino acid residues
Do amino acid residues affect the tertiary structure?
Not all proteins with tertiary structure are biologically active
Constituent domain
Quaternary structure
It is composed of two or more polypeptide chains with tertiary structure.
Not further folding
interrelationships between subunits
special protein
sickle cell anemia
Insulin A chain and B chain are maintained by disulfide bonds
The combination of hemoglobin and oxygen is a positive cooperative allosteric effect
It's an s-curve
Protein physical and chemical properties
Nitrogen content 16%
Two-phase ionization
Isoelectric point
Colloidal particles are most unstable at the isoelectric point
Colloidal properties
Hydrophobic on the inside and hydrophilic on the outside
Remove the hydration film and lose its colloidal properties
Salting out
macromolecules
Ultrafiltration and dialysis separation
distinguished by density
ultracentrifugation
Chromatography methods for different molecular sizes
gel filtration
transsexual
Break non-covalent bonds, disulfide bonds
The essence is that the spatial conformation changes
Coagulation is an irreversible result of heat denaturation
Precipitates easily but not completely
Loss of original biological activity
Acid and alkaline solution
peptide bond cleavage
precipitation
Since the hydrophobic bonds are exposed on the outside
The use of raw milk to solve metal poisoning is the use of precipitation
Protein isolate does not want to be denatured: use inorganic salt solution