examples for protein essays Flashcards
dystrophin
essential for muscle function, has multiple domains that are involved in binding to actin filaments, anchoring the protein to the cell membrane, and interacting with other proteins involved in signaling pathways
ferritin
multiple domains, iron function, self-assembly into a spherical cage-like structure, efficient storage of iron and release iron while maintaining structural integrity.
calmodulin
diff functions and conforms as flexible linkers, has four EF-hand domains, which are calcium-binding domains that are connected by flexible linkers. When calcium levels in the cell increase, calmodulin binds calcium ions and undergoes a conformational change that allows it to interact with target proteins. calmodulin can activate enzymes involved in calcium signaling, such as calcium/calmodulin-dependent protein kinase (CaMK) and nitric oxide synthase (NOS), or it can inhibit proteins such as calcineurin, a protein phosphatase involved in immune response.
Collagen
main component of connective tissues such as bone and cartilage, has multiple domains that are involved in forming a triple helix structure - stabilised by interactions between the different domains, which help to prevent the protein from denaturing or breaking down.
elastin
found in elastic tissues such as skin and blood vessels, has multiple domains that are involved in forming a cross-linked network. The cross-linked network provides elastin with the ability to stretch and recoil, while maintaining its structural integrity.
p53
a tumor suppressor protein that plays a critical role in regulating the cell cycle and preventing the formation of cancerous cells. p53 has several domains, including a DNA-binding domain, a tetramerization domain, and a regulatory domain. mutations - make cancer. can be influenced by a variety of factors, making it difficult to predict how the protein will function in different contexts.
Receptor tyrosine kinases
class of membrane receptors that are activated by ligand binding and phosphorylate themselves and other proteins to transmit signals within the cell. composed of extracellular ligand-binding domain, a transmembrane domain, and an intracellular catalytic domain. extracellular - vary in length composition so diff RTKs bind to diff ligands. he intracellular domain can be modified by alternative splicing or post-translational modifications, which can affect the catalytic activity and signaling specificity of the RTK.
myoglobin
earliest protein structure structured by X-ray crystallography.
ubiquitin
NMR, revealed a compact fold stabilized by a network of hydrogen bonds and hydrophobic interactions
bacterial Type VI secretion system
Cryo-EM arge protein complex that mediates bacterial competition and virulence. The Cryo-EM structure revealed a dynamic complex composed of multiple subunits, with a channel-like structure that can be opened and closed in response to signals.
DNA binding proteins
the crystal structure of the DNA binding domain of the transcription factor NF-kappaB revealed how the protein recognizes its DNA binding site and provided insights into the mechanism of transcriptional regulation.