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30 relations: Alanine, Alpha helix, Aspartame, Bacillus, Beta sheet, Biomolecular structure, C-terminus, Calcium, Calcium in biology, Chaperone (protein), Denaturation (biochemistry), Enzyme, Extracellular, Fast parallel proteolysis, Gram-positive bacteria, Hydrolysis, MEROPS, Metalloproteinase, N-terminus, Peptide bond, Periplasm, Phenylalanine, Proline, Protein domain, Protein precursor, Signal peptidase, Signal peptide, Site-directed mutagenesis, Threonine, Twin-arginine translocation pathway.
Alanine
Alanine (symbol Ala or A) is an α-amino acid that is used in the biosynthesis of proteins.
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Alpha helix
The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a righthand-spiral conformation (i.e. helix) in which every backbone N−H group donates a hydrogen bond to the backbone C.
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Aspartame
Aspartame (APM) is an artificial non-saccharide sweetener used as a sugar substitute in some foods and beverages.
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Bacillus
Bacillus is a genus of gram-positive, rod-shaped bacteria and a member of the phylum Firmicutes.
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Beta sheet
The β-sheet (also β-pleated sheet) is a common motif of regular secondary structure in proteins.
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Biomolecular structure
Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function.
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C-terminus
The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH).
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Calcium
Calcium is a chemical element with symbol Ca and atomic number 20.
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Calcium in biology
Calcium ions (Ca2+) play a vital role in the physiology and biochemistry of organisms and the cell.
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Chaperone (protein)
In molecular biology, molecular chaperones are proteins that assist the covalent folding or unfolding and the assembly or disassembly of other macromolecular structures.
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Denaturation (biochemistry)
Denaturation is a process in which proteins or nucleic acids lose the quaternary structure, tertiary structure, and secondary structure which is present in their native state, by application of some external stress or compound such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), radiation or heat.
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Enzyme
Enzymes are macromolecular biological catalysts.
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Extracellular
In cell biology, molecular biology and related fields, the word extracellular (or sometimes extracellular space) means "outside the cell".
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Fast parallel proteolysis
Fast parallel proteolysis (FASTpp) is a method to determine the thermostability of proteins by measuring which fraction of protein resists rapid proteolytic digestion.
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Gram-positive bacteria
Gram-positive bacteria are bacteria that give a positive result in the Gram stain test, which is traditionally used to quickly classify bacteria into two broad categories according to their cell wall.
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Hydrolysis
Hydrolysis is a term used for both an electro-chemical process and a biological one.
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MEROPS
MEROPS is an on-line database for peptidases (also known as proteases, proteinases and proteolytic enzymes) and their inhibitors.
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Metalloproteinase
A metalloproteinase, or metalloprotease, is any protease enzyme whose catalytic mechanism involves a metal.
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N-terminus
The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide referring to the free amine group (-NH2) located at the end of a polypeptide.
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Peptide bond
A peptide bond is a covalent chemical bond linking two consecutive amino acid monomers along a peptide or protein chain.
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Periplasm
The periplasm is a concentrated gel-like matrix in the space between the inner cytoplasmic membrane and the bacterial outer membrane called the periplasmic space in gram-negative bacteria.
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Phenylalanine
Phenylalanine (symbol Phe or F) is an α-amino acid with the formula.
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Proline
Proline (symbol Pro or P) is a proteinogenic amino acid that is used in the biosynthesis of proteins.
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Protein domain
A protein domain is a conserved part of a given protein sequence and (tertiary) structure that can evolve, function, and exist independently of the rest of the protein chain.
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Protein precursor
A protein precursor, also called a pro-protein or pro-peptide, is an inactive protein (or peptide) that can be turned into an active form by post-translational modification, such as breaking off a piece of the molecule or adding on another molecule.
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Signal peptidase
Signal peptidases are enzymes that convert secretory and some membrane proteins to their mature forms by cleaving their signal peptides from their N-terminals.
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Signal peptide
A signal peptide (sometimes referred to as signal sequence, targeting signal, localization signal, localization sequence, transit peptide, leader sequence or leader peptide) is a short peptide (usually 16-30 amino acids long) present at the N-terminus of the majority of newly synthesized proteins that are destined towards the secretory pathway.
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Site-directed mutagenesis
Site-directed mutagenesis is a molecular biology method that is used to make specific and intentional changes to the DNA sequence of a gene and any gene products.
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Threonine
Threonine (symbol Thr or T) is an amino acid that is used in the biosynthesis of proteins.
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Twin-arginine translocation pathway
The twin-arginine translocation pathway (Tat pathway) is a protein export, or secretion pathway found in plants, bacteria, and archaea.
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Bacillus thermoproteolyticus neutral proteinase, EC 3.4.24.27, Thermoase Y10.
References
[1] https://en.wikipedia.org/wiki/Thermolysin
