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Protein structure databases are critical for many efforts in computational biology such as structure based drug design, both in developing the computational methods used and in providing a large experimental dataset used by some methods to provide insights about the function of a protein. [34]
According to IUPAC, the functionality of a monomer is defined as the number of bonds that a monomer's repeating unit forms in a polymer with other monomers. Thus in the case of a functionality of f = 2 a linear polymer is formed by polymerizing (a thermoplastic). Monomers with a functionality f ≥ 3 lead to a branching point, which can lead to ...
A monomer (/ ˈ m ɒ n ə m ər / MON-ə-mər; mono-, "one" + -mer, "part") is a molecule that can react together with other monomer molecules to form a larger polymer chain or three-dimensional network in a process called polymerization.
Proteins are functional macromolecules responsible for catalysing the biochemical reactions that sustain life. [1]: 3 Proteins carry out all functions of an organism, for example photosynthesis, neural function, vision, and movement. [13]
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location ...
The conformational differences that accompany conversion between oligomers may be similar to the protein motions necessary for function of some proteins. [19] The morpheein model highlights the importance of conformational flexibility for protein functionality and offers a potential explanation for proteins showing non- Michaelis-Menten ...
Proteins are often synthesized in an inactive precursor form; typically, an N-terminal or C-terminal segment blocks the active site of the protein, inhibiting its function. The protein is activated by cleaving off the inhibitory peptide. Some proteins even have the power to cleave themselves.
Cell surface (cortical) actin remodeling is a cyclic (9-step) process where each step is directly responsive to a cell signaling mechanism. Over the course of the cycle, actin begins as a monomer, elongates into a polymer with the help of attached actin-binding-proteins, and disassembles back into a monomer so the remodeling cycle may commence again.