Protiens

• Amino acid residues are connected to one another through peptide bonds between the carboxyl group of one amino acid and the amine group of another.
• Non-essential amino acids can be produced by the body from other compounds.
• Essential amino acids cannot be synthesized by the body and must be obtained through dietary sources.
• The primary structure of proteins consists of amino acids linked together by peptide bonds, forming polypeptides.
• Proteins are made up of amino acids, which can be classified as essential or non-essential.
• Protein is the most abundant substance in cells.
• Proteins have different shapes that determine their function.
• The primary structure is determined by the sequence of amino acids, which can be altered during protein synthesis or post-translational modification.
• The sequence of amino acids determines the structure, function, and properties of proteins.
• Essential amino acids cannot be synthesized by the human body and must be obtained from food sources.
• Secondary structures include alpha helices (coiled) and beta sheets (flat).
• The sequence of amino acids determines the protein's function and properties.
• The sequence of amino acids determines the unique properties of each protein.
• There are 20 different types of amino acids that make up proteins.
• Denaturation occurs when protein molecules lose their native conformation due to changes in environmental conditions.
• Protein folding is influenced by factors such as pH, temperature, salt concentration, and presence of cofactors or ligands.
• Amino acid sequence determines protein shape.
• There are about 20 different types of amino acids found in proteins.
• Secondary structure refers to local folding patterns within a polypeptide chain due to hydrogen bonding between certain amino acid side chains.
• Secondary structure refers to local folding patterns within a polypeptide chain due to hydrogen bonding between certain amino acid side chains.
• Each protein has its own unique sequence of amino acids that determines its shape and function.
• Secondary structures refer to local folding patterns within a polypeptide chain caused by hydrogen bonding between certain amino acid side chains.
• Ionic interactions involve charged groups on amino acid residues.
• Different sequences of amino acids result in different shapes and functions of proteins.
• Hydrophobic interactions occur between hydrophobic side chains.
• Amino acid sequences are read from N to C terminus.
• There are 20 common amino acids found in proteins.
• Different types of proteins include enzymes, structural proteins, transport proteins, hormones, antibodies, and storage proteins.
• Non-essential amino acids can be produced by the human body through metabolic processes.
• Enzymes catalyze chemical reactions in living organisms.
• Hydrophobic amino acids include alanine (A), valine (V), leucine (L), isoleucine (I), proline (P), phenylalanine (F), tryptophan (W), methionine (M).
• Amino acids are linked together to form polypeptide chains, with hydrogen bonds forming between adjacent peptides.
• Amino acid sequences can vary between species and individuals due to genetic variation.
• Secondary structure involves local folding patterns such as alpha-helices or beta sheets.
• The genetic code is degenerate, meaning that multiple codons can encode the same amino acid.
• Essential amino acids cannot be synthesized by humans and must be obtained through dietary sources.
• Primary structure is determined by the sequence of amino acids in a polypeptide chain.
• Translation occurs at ribosomes, which bind to mRNA molecules and use them as templates to build proteins.
• Protein synthesis involves the translation of mRNA into polypeptide chains by ribosomes using tRNAs as adaptors.
• Protein structure refers to the arrangement of atoms within a protein molecule.