MindMap Gallery Biochemistry Chapter 1 Protein
Chapter 1 of Biochemistry, Protein, covers chemical composition, molecular structure, the relationship between protein structure and function, and the physical and chemical properties of proteins. Everyone is welcome to study.
Edited at 2023-10-12 22:08:28This 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.
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
chemical components
Elemental composition
Carbon, hydrogen, oxygen, nitrogen, phosphorus and sulfur (mainly)
Nitrogen (13%-19%)
The nitrogen content of various proteins is very close, with an average of about 16%. The protein content in 100g sample = grams of nitrogen per gram of sample * 6.25 * 100
basic unit
amino acids
There are only 20 types of amino acids that make up human protein
General structural formula
H-C(COOH)(R)-NH2
structure
Except for glycine and proline, the other amino acids are all L-α-amino acids. The glycine group is H and has no symmetry, so there is no distinction between D and L.
Structure and classification
nonpolar hydrophobic amino acids
A Valerian Is Liang Bing Gan Preserved
Features: The side chain is a non-polar hydrophobic gene
non-ionizing polar amino acids
Su Gusi half day
Side chains are polar but uncharged
Acidic amino acids (negatively charged)
Glutamic acid, aspartic acid
Basic amino acids (positively charged)
Histidine, arginine, lysine
Amino acids containing aromatic rings
Phenylalanine Tyrosine Tryptophan
Peptides and Bioactive Peptides
Amino acids are connected by peptide bonds
The α-carboxyl group of an amino acid molecule and the α-amino group of an amino acid molecule undergo dehydration and condensation to form a covalent bond.
Two amino acids are condensed into dipeptides, three are tripeptides, less than ten are oligopeptides, 10-50 are polypeptides, and more than 50 are proteins.
Various bioactive peptides
Glutathione (GSH)
Contains sulfhydryl groups and has strong reducing properties
Molecular Structure
Primary structure of protein (planar)
The sequence of amino acids in a polypeptide chain from the N-terminus to the C-terminus
The main chemical bonds that stabilize the structure are peptide bonds, and some have disulfide bonds.
Protein secondary structure (space)
peptide plane
The length of the peptide bond is between single and double bonds, so it has the properties of a partial double bond and cannot rotate freely, so that the six atoms involved in the formation of the peptide bond are on the same plane.
The relative spatial position of the backbone atoms of a certain segment of the main chain in a protein molecule, that is, the local spatial structure of a certain segment of the peptide chain.
α-helix (main)
right hand spiral
The R group side chain is outside the helix
3.6 residues per turn, pitch 0.54nm
Maintained by hydrogen bonds, the central axis is parallel
β-sheet (β-sheet)
Fully extended, serrated
Single reply/multiple parallels
The R-based side chains are staggered up and down the plane
cisparallel and antiparallel
Maintained by hydrogen bonds, perpendicular to the long axis
β-turn
random curl
Tertiary structure (space) of protein
The overall arrangement of all atoms in a polypeptide chain in three-dimensional space
main chemical bonds
Hydrophobic bond Ionic bond (salt bond) Hydrogen bond Van der Waals force
Features
Folded into a tight ball shape
Contains a variety of secondary structural units
Hydrophobic groups are located inside the molecule and hydrophilic groups are located on the surface of the molecule
Mainly maintained by secondary bonds
Protein quaternary structure (space)
Features
Composed of multiple peptide chains (subunits)
Subunits can be the same or different
Subunits are linked by non-covalent bonds
Polymerization and depolymerization between subunits
main chemical bonds
hydrogen bond ionic bond
The relationship between protein structure and function
molecular disease
Changes in the primary structure are gene mutations, eg: sickle cell anemia
protein conformational diseases
Protein folding errors occur, the primary structure remains unchanged, the secondary structure changes, and the protein conformation changes affect its function.
Conformational changes in hemoglobin subunits can affect the binding of subunits to oxygen
positive synergy
allosteric effect
Physicochemical properties of protein
Zwitterionic properties
In a certain pH solution, the number of positive and negative charges carried by the protein is equal, the net charge is equal to 0, and the protein is a zwitterionic ion. At this time, the pH of the solution is the isoelectric point (pI) of the protein. When pH < pI, it is positively charged, pH >pI, negatively charged
Colloidal properties
The hydration film and surface charge of protein molecules become two stabilizing factors that maintain the hydrophilic colloidal particles of protein molecules. If either one is damaged, the protein will precipitate.
Denaturation, renaturation and precipitation
transsexual
Under the action of certain physical and chemical factors, the specific spatial conformation of proteins is destroyed, resulting in changes in their physical and chemical properties and loss of biological activity.
Application in medicine
Produce and store protein hormones, enzymes, antibodies and serum under low temperature conditions to prevent their denaturation and inactivation
Disinfect with alcohol and ultraviolet steam to denature the proteins of viruses and bacteria to achieve the purpose of sterilization
UV absorption properties
Aromatic amino acids such as tryptophan and tyrosine containing conjugated double bonds have a maximum absorption peak at 280 nm in ultraviolet light.
color reaction
biuret
Purple red complex
Test the degree of protein hydrolysis
Ninhydrin
purple compound