MindMap Gallery Introduction to protein
Summary of protein and amino acid knowledge points, summarizing teaching key points, Teaching difficulties, physical and chemical properties of amino acids, additional knowledge points, etc.
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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.
Introduction to protein
Teaching focus
protein concept
It is a biological macromolecular substance with a relatively stable conformation and certain functions formed by condensation of many different α-amino acids through amide bonds according to a certain sequence.
Main elements of protein
C,H,O,N,S
Protein content calculation
The average nitrogen content is 16%. Measuring the nitrogen content can estimate the protein content.
Protein content = nitrogen content of protein sample *6.25
basic unit
20 kinds of L-type α-amino acids
Protein can be hydrolyzed by acids, alkalis, and proteases to release more than 20 amino acids.
3-letter representation of 20 amino acids
Ala - Alanine Asp - Aspartic acid Leu - Leucine Arg - Arginine Gly - Glycine Phe - Phenylalanine Ser - Serine Pro - Proline His - Histidine Lys - Lysine Met - methionine Thr - threonine Val - valine Ile - isoleucine Trp - tyrosine Tyr - Phenylamine Cys - Cysteine Glu - Glutamic acid Gln - Glutamine
The general structural formula of amino acids
Structural features
Configuration and optical activity
Configuration: The optically active three-dimensional structure caused by the asymmetry of the spatial arrangement of groups or atoms is called a stereotype.
L- (-)-type;-D- ( )-type
Determine based on the position of the amino group The amino group on the left is L-form The amino group on the right is D-form
All are α-amino acids (except Pro). All are L-α-amino acids. All are optically active (except Gly). Different α-amino acids have different R side chains.
Special amino acids, essential amino acids
The concept and calculation of isoelectric point
Amino acids exhibit amphoteric dissociation characteristics because they have α-amino groups, α-carboxyl groups and dissociable side chain groups. Under specific pH conditions, the positive charge generated by the dissociation of an amino acid is equal to the negative charge, and the net charge carried by the amino acid is zero. The pH of the solution at this time is called the isoelectric point of the amino acid.
The pH of a solution at which the net charge of an amino acid is zero *pH<pI, positive charge *pH=pI, no charge *pH>pI, negative charge
Ninhydrin reaction
Teaching difficulties
Calculation and application of isoelectric point
application
Commonly used methods to separate mixed amino acids: Certain amino acids can be precipitated from the mixture by utilizing the minimum solubility at the isoelectric point. Separation is carried out by utilizing the difference in charge of different amino acids at the same pH.
calculate
Neutral amino acids: pI=(pK-COOH pK-NH3)/2
Acidic amino acids: pI=(pK1-COOH pK2-COOH)/2
Basic amino acids: pI=(pK2-NH3 pK3-NH3)/2
The law of isoelectric point
First write the dissociation equation correctly: (pay attention to the degree of dissociation) Then take the average of the pK values of the groups on both sides of the zwitterionic ion
Find the zwitterion (zwitterionic ion) and write the dissociation equation correctly
How to write the dissociation equation correctly? Remember the strength of ionization: carboxyl > amino; main chain > side chain
The pK value of the zwitterion before and after dissociation
The amino, carboxyl and some side chain groups of amino acids can be dissociated
Physicochemical properties of amino acids
Amino acid molecular composition
Protein element composition
Basic elements: C, H, O, N, S
Trace elements: P, I, Se... Fe, Mn, Mg, Cu, Zn, Co...
Amino acid structural formula
Amino acid classification
non-polar
Also called hydrophobic amino acid
5 kinds of lipid amino acids (alanine, valine, leucine, isoleucine and methionine) 1 aromatic amino acid (phenylalanine) 2 types of heterocyclic amino acids (proline and tryptophan)
polarity
Uncharged
Belongs to hydrophilic amino acid
Contains 3 types of hydroxyl amino acids (serine, threonine and tyrosine) 2 types of amide amino acids (asparagine and glutamine) Contains mercaptocysteine and glycine, etc.
charged
Positive electricity
*Basic amino acids: lysine, arginine, histidine
Negative charge
*Acidic amino acids: aspartic acid, glutamic acid
A general name for a class of organic compounds containing amino and carboxyl groups
physical properties
color
1. Color status: Amino acids are usually colorless crystals, their color is unknown It appears as pure colorless or white crystalline form. Different amino acids may form different crystalline shapes due to their specific structures, and these shapes can be used to identify different amino acid types.
state
2. Solubility: Most amino acids are soluble in water, especially in warm water. Except for cystine and tyrosine, the rest of the amino acids are also better soluble in cold water. For organic solvents, amino acids are generally insoluble or slightly soluble in ethanol, ether, etc., with the exception of proline and hydroxylamine (not one of the 20 standard amino acids), which are soluble in ethanol and ether.
smell
3.Taste: Amino acids have a variety of different flavors, including sour, sweet, bitter and umami. For example, glutamic acid (monosodium glutamate, the main component of MSG) has a distinct umami taste, glycine is sweet, and some amino acids may be bitter or tasteless.
Color status: colorless crystals, specific crystal shapes vary. Solubility: Easily soluble in water and dilute acid and alkali solutions. Some amino acids can be soluble in specific organic solvents. Taste: It has various taste characteristics such as sour, sweet, bitter, umami, etc. The specific taste depends on the type of amino acid.
chemical properties
Zwitterion
concepts, features
Amino acids have zwitterionic properties, which are reflected in the fact that their molecules have both basic (amino-NH₂) and acidic (carboxyl-COOH) functional groups. At a specific pH (isoelectric point), the amino and carboxyl groups are ionized to the same degree, and the amino acid becomes neutral and becomes a Zwitterion. Its charge state changes with the pH of the environment, which has an important impact on the solubility of amino acids in solution, charge properties, biochemical reactions and life activities (such as protein structure and function).
Isoelectric point (pI)
concept
Amino acids exhibit amphoteric dissociation characteristics because they have α-amino groups, α-carboxyl groups and dissociable side chain groups. Under specific pH conditions, the positive charge generated by the dissociation of an amino acid is equal to the negative charge, and the net charge carried by the amino acid is zero. It moves neither toward the anode nor the cathode in the electric field. The pH of the solution at this time is called the isotopic value of the amino acid. electric point
At the isoelectric point, the solubility of amino acids is minimum and it is easy to precipitate. This property can be used to separate and prepare amino acids.
The pH of a solution at which the net charge of an amino acid is zero *pH<pI, positive charge *pH=pI, no charge *pH>pI, negative charge
calculate
Neutral amino acids: pI=(pK-COOH pK-NH3)/2
Acidic amino acids: pI=(pK1-COOH pK2-COOH)/2
Basic amino acids: pI=(pK2-NH3 pK3-NH3)/2
The law of isoelectric point
First write the dissociation equation correctly: (pay attention to the degree of dissociation) Then take the average of the pK values of the groups on both sides of the zwitterionic ion
Find the zwitterion (zwitterionic ion) and write the dissociation equation correctly
How to write the dissociation equation correctly? Remember the strength of ionization: carboxyl > amino; main chain > side chain
The pK value of the zwitterion before and after dissociation
The amino, carboxyl and some side chain groups of amino acids can be dissociated
chemical reaction
Ninhydrin reaction
DNFB reaction
UV absorption properties
Amino acids containing conjugated double bonds (tyrosine, phenylalanine, and tryptophan) have UV-absorbing properties
There is a characteristic UV absorption peak at 280nm Derived from aromatic amino acid side chain groups Trp >Tyr > Phe Can be used to determine the content of amino acids and proteins
Only aromatic amino acids have UV absorption capabilities (because they contain the R side chain of a benzene ring conjugated double bond). Tyrosine λmax: 275nm Phenylalanine λmax: 259nm Tryptophan λmax: 279nm
Therefore, by measuring the light absorption value of the sample at 280 nm, the concentration of protein in the solution can be known. This method is quick and easy.
Additional knowledge points
Are there only 20 amino acids that make up protein?
Hydroxyproline
* Found in collagen *Pro Hydroxylation requires Vitamin C
γ-carboxyglutamate
subtopic
*Exists in coagulation factors *Glu modification requires vitamin K
cystine
Cys is formed through disulfide bonds
Are there any amino acids that are not involved in protein composition?
A variety of non-protein amino acids can be produced during the metabolic process *Citrulline and ornithine: L-α-amino acids, urea synthesis intermediates *Gamma-aminobutyric acid (GABA) and beta-alanine GABA: important neurotransmitters β-Alanine: breakdown product of pyrimidines; forms pantothenic acid *D-amino acid: widely found in plants and various microorganisms