MindMap Gallery Protein molecular composition
Covers the basic concepts of proteins, the structure and classification of amino acids, peptide bonds and polypeptide chains, the quaternary structure of proteins, the properties of proteins, protein synthesis, protein functions and other knowledge points.
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This is a mind map about the interpretation and summary of the relationship field e-book, Main content: Overview of the essence interpretation and overview of the relationship field e-book. "Relationship field" refers to the complex interpersonal network in which an individual influences others through specific behaviors and attitudes.
This is a mind map about accounting books and accounting records. The main contents include: the focus of this chapter, reflecting the business results process of the enterprise, the loan and credit accounting method, and the original book of the person.
Protein molecular composition
Basic concepts of protein
definition
Biological macromolecules formed by amino acids linked by peptide bonds
Is one of the main bearers of life activities
Function
Main component of cells and tissues
enzymes involved in catalyzing biochemical reactions
Participate in cell signaling
Maintain cell structure and morphology
Structure and classification of amino acids
basic structure of amino acids
The central carbon atom is connected to an amino group, a carboxyl group, a hydrogen atom and a side chain (R group)
Classification
Classification based on side chain properties
nonpolar amino acids
Such as glycine, alanine
polar uncharged amino acids
Such as serine, threonine
polar positively charged amino acids
Such as lysine, arginine
polar negatively charged amino acids
Such as aspartic acid, glutamic acid
Classified according to whether the human body can synthesize it
essential amino acids
The human body cannot synthesize it and must be ingested through diet
non-essential amino acids
It can be synthesized by the human body and does not necessarily need to be ingested through diet.
Peptide bonds and polypeptide chains
formation of peptide bonds
Amino acids form peptide bonds through dehydration and condensation reactions
Connect the carboxyl and amino groups of adjacent amino acids
The structure of a polypeptide chain
A chain structure formed by multiple amino acids connected by peptide bonds
The length and amino acid sequence of the polypeptide chain determine the structure and function of the protein
quaternary structure of protein
primary structure
amino acid sequence
The basic structure of a protein, determined by a specific sequence of amino acids
Sequence changes can lead to changes or loss of protein function
secondary structure
local spatial structure
alpha helix
A tightly coiled helix of amino acid chains
beta sheet
Amino acid chains fold into sheets
tertiary structure
overall spatial structure
Formed by primary structure folding through interactions between amino acid side chains
Determines the three-dimensional shape and biological activity of proteins
Quaternary structure
Structure of multi-subunit proteins
Composed of two or more polypeptide chains
Each subunit is stabilized through non-covalent interactions
Protein properties
solubility
Affected by amino acid composition and protein structure
Proteins with many polar amino acids are usually soluble in water
isoelectric point
The pH value at which protein surface charge is zero
Different proteins have different isoelectric points
Denaturation and renaturation
transsexual
Destruction of protein three-dimensional structure and loss of function
Usually caused by changes in temperature, pH, or organic solvents
Restoration
Denatured proteins restore their original structure and function under certain conditions
Not all proteins can be renatured
protein synthesis
genetic code
The nucleotide sequence on the mRNA determines the amino acid sequence
Every three nucleotides correspond to one amino acid
translation process
performed on ribosomes
tRNA carries amino acids that are paired according to the codons on the mRNA
Form polypeptide chains and fold into the correct spatial structure
post-translational modification
Chemical modifications that proteins may undergo after synthesis
Such as phosphorylation, glycosylation, cleavage, etc.
Affect protein activity, stability and localization
protein function
Enzyme catalysis
Accelerate the rate of biochemical reactions
Highly specific and efficient
structural support
Make up the cytoskeleton and tissue structure
Such as collagen, muscle protein, etc.
signaling
Participate in the transmission of signals inside and outside cells
Such as hormone receptors, cytokines, etc.
transportation and storage
Transport molecules such as oxygen, ions, etc.
Storage molecules such as ferritin store iron ions
immune defense
Antibodies participate in immune responses
Identify and neutralize foreign pathogens