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MindMap Gallery Protein structure and function mind map

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!

Edited at 2023-11-03 17:20:19

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Protein structure and function mind map

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Outline

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