Search results
Results From The WOW.Com Content Network
Protein dynamics and conformational changes allow proteins to function as nanoscale biological machines within cells, often in the form of multi-protein complexes. [14] Examples include motor proteins, such as myosin, which is responsible for muscle contraction, kinesin, which moves cargo inside cells away from the nucleus along microtubules ...
Polypeptides include proteins and shorter polymers of amino acids; some major examples include collagen, actin, and fibrin. Polysaccharides are linear or branched chains of sugar carbohydrates; examples include starch, cellulose, and alginate.
Protein–protein interactions (PPIs) are physical contacts of high specificity established between two or more protein molecules as a result of biochemical events steered by interactions that include electrostatic forces, hydrogen bonding and the hydrophobic effect. Many are physical contacts with molecular associations between chains that ...
Another way to extend half-life do is to bind serum albumin to the peptide. Human serum albumin is the most abundant plasma protein with a molecular weight of 66.4 kDa, [24] and it is involved in many essential bodily functions to maintain homeostasis. As a result, albumin binding would significantly increase the molecular weight of the peptide ...
Kinesin is a protein functioning as a molecular biological machine. It uses protein domain dynamics on nanoscales. A protein complex or multiprotein complex is a group of two or more associated polypeptide chains. Protein complexes are distinct from multidomain enzymes, in which multiple catalytic domains are found in a single polypeptide chain ...
The process starts with two partial proteins. These may represent two independent polypeptides (such as two parts of a heterodimer), or may have originally been halves of a single protein that underwent a fission event to become two polypeptides. The two proteins can later fuse together to form a single polypeptide.
A hairpin is a special case of a turn, in which the direction of the protein backbone reverses and the flanking secondary structure elements interact. For example, a beta hairpin connects two hydrogen-bonded , antiparallel β-strands (a rather confusing name, since a β-hairpin may contain many types of turns – α, β, γ, etc.).
Each of these molecules is required for life since each plays a distinct, indispensable role in the cell. [11] The simple summary is that DNA makes RNA, and then RNA makes proteins. DNA, RNA, and proteins all consist of a repeating structure of related building blocks (nucleotides in the case of DNA and RNA, amino acids in the case of proteins ...