Biomaterial Database

Hydrophobic microdomains as structural invariant regions in proteins. 1988

D Płochocka, and P Zielenkiewicz, and A Rabczenko

Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.

A procedure for finding clusters of interacting residues in protein hydrophobic cores is proposed. Such clusters have been located for six globular proteins of known structure. Assuming that sequences of the same protein from different biological sources encode the same tertiary structure, replacements within clusters were analysed after sequence alignment. An evolutionary conservation was found for residues in cluster positions showing that these microdomains play a structural role and are more invariant in proteins.

UI	MeSH Term	Description	Entries
D009113	Muramidase	A basic enzyme that is present in saliva, tears, egg white, and many animal fluids. It functions as an antibacterial agent. The enzyme catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. EC 3.2.1.17.	Lysozyme,Leftose,N-Acetylmuramide Glycanhydrolase,Glycanhydrolase, N-Acetylmuramide,N Acetylmuramide Glycanhydrolase
D009211	Myoglobin	A conjugated protein which is the oxygen-transporting pigment of muscle. It is made up of one globin polypeptide chain and one heme group.
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D005075	Biological Evolution	The process of cumulative change over successive generations through which organisms acquire their distinguishing morphological and physiological characteristics.	Evolution, Biological
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D001330	Electronic Data Processing	Applications that store and process large quantities of data.	Automatic Data Processing,Bar Codes,Computer Data Processing,Data Processing, Automatic,Information Processing, Automatic,Optical Readers,Information Processing,Automatic Information Processing,Bar Code,Codes, Bar,Data Processing, Computer,Data Processing, Electronic,Optical Reader,Processing, Automatic Data,Processing, Automatic Information,Processing, Computer Data,Processing, Electronic Data,Processing, Information
D012260	Ribonucleases	Enzymes that catalyze the hydrolysis of ester bonds within RNA. EC 3.1.-.	Nucleases, RNA,RNase,Acid Ribonuclease,Alkaline Ribonuclease,Ribonuclease,RNA Nucleases,Ribonuclease, Acid,Ribonuclease, Alkaline
D012995	Solubility	The ability of a substance to be dissolved, i.e. to form a solution with another substance. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)	Solubilities