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Etiolation / iː t i ə ˈ l eɪ ʃ ən / is a process in flowering plants grown in partial or complete absence of light. [1] It is characterized by long, weak stems; smaller leaves due to longer internodes; and a pale yellow color . The development of seedlings in the dark is known as "skotomorphogenesis" and leads to etiolated seedlings.
Etiolation of the seedling causes it to become elongated, which may facilitate it emerging from the soil. A seedling that emerges in darkness follows a developmental program known as skotomorphogenesis (dark development), which is characterized by etiolation. Upon exposure to light, the seedling switches rapidly to photomorphogenesis (light ...
When injected into plants, these proteins can enter the nucleus of the plant cell, bind plant promoter sequences, and activate transcription of plant genes that aid in bacterial infection. [7] Plants have developed a defense mechanism against type III effectors that includes R (resistance) genes triggered by these effectors.
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 ...
A coiled coil is a structural motif in proteins in which 2–7 [1] alpha-helices are coiled together like the strands of a rope. (Dimers and trimers are the most common types.) They have been found in roughly 5-10% of proteins and have a variety of functions. [2] They are one of the most widespread motifs found in protein-protein interactions.
Robotic preparation of MALDI mass spectrometry samples on a sample carrier. Proteomics is the large-scale study of proteins. [1] [2] Proteins are vital macromolecules of all living organisms, with many functions such as the formation of structural fibers of muscle tissue, enzymatic digestion of food, or synthesis and replication of DNA.
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 ...
The protein protein interactions are displayed in a signed network that describes what type of interactions that are taking place [74] Protein–protein interactions often result in one of the interacting proteins either being 'activated' or 'repressed'. Such effects can be indicated in a PPI network by "signs" (e.g. "activation" or "inhibition").