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The words protein, polypeptide, and peptide are a little ambiguous and can overlap in meaning. Protein is generally used to refer to the complete biological molecule in a stable conformation, whereas peptide is generally reserved for a short amino acid oligomers often lacking a stable 3D structure. But the boundary between the two is not well ...
The TIM/TOM complex is a protein complex in cellular biochemistry which translocates proteins produced from nuclear DNA through the mitochondrial membrane for use in oxidative phosphorylation. In enzymology , the complex is described as an mitochondrial protein-transporting ATPase ( EC 7.4.2.3 ), or more systematically ATP phosphohydrolase ...
Biochemistry is closely related to molecular biology, the study of the molecular mechanisms of biological phenomena. [5] Much of biochemistry deals with the structures, functions, and interactions of biological macromolecules such as proteins, nucleic acids, carbohydrates, and lipids.
In the unfolded wild-type protein, where the salt bridge is absent, His31 is reported to have a pK a of 6.8 in H 2 O buffers of moderate ionic strength. Figure 5 shows a pK a of the wild-type of 9.05. This difference in pK a is supported by the His31’s interaction with Asp70. To maintain the salt bridge, His31 will attempt to keep its proton ...
Protein metabolism denotes the various biochemical processes responsible for the synthesis of proteins and amino acids (anabolism), and the breakdown of proteins by catabolism. The steps of protein synthesis include transcription, translation, and post translational modifications.
Proteins : amino acid – glycine – arginine – lysine; peptide – primary structure – secondary structure – tertiary structure – conformation – protein folding; Chemical properties: molecular bond – covalent bond – ionic bond – hydrogen bond – ester – ethyl; molecular charge – hydrophilic – hydrophobic – polar; pH ...
Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from ...
Heat shock protein chaperones are classified based on their observed molecular weights into Hsp60, Hsp70, Hsp90, Hsp104, and small Hsps. [5] The Hsp60 family of protein chaperones are termed chaperonins, and are characterized by a stacked double-ring structure and are found in prokaryotes, in the cytosol of eukaryotes, and in mitochondria.