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MCQ on Leucine Zipper (Structure and Functions)
A leucine zipper is a structural motif in proteins involved in DNA binding and protein-protein interactions. It consists of repeated leucine residues at regular intervals, […]
A leucine zipper is a structural motif in proteins involved in DNA binding and protein-protein interactions. It consists of repeated leucine residues at regular intervals, […]
The helix-turn-helix (HTH) domain is a DNA-binding motif in proteins, typically found in transcription factors. It consists of two alpha helices connected by a short […]
The helix-loop-helix (HLH) domain is a protein structural motif involved in DNA binding and protein dimerization. Commonly found in transcription factors, it consists of two […]
GPCR, or G protein-coupled receptor, is a cell membrane protein that detects external signals and activates intracellular responses. It plays a crucial role in cell […]
Tertiary structure refers to the overall three-dimensional arrangement of a single polypeptide chain in a protein. It results from the folding and interactions between distant […]
The secondary structure of a protein involves local folding patterns, primarily α-helices and β-sheets, stabilized by hydrogen bonds between amino acids in the polypeptide chain. […]
Quaternary structure refers to the arrangement of multiple polypeptide subunits in a functional protein. It results from the interaction and assembly of individual subunits, forming […]
The primary structure of proteins refers to the linear sequence of amino acids in a polypeptide chain. It is determined by the specific order of […]
Heat shock proteins (HSPs) are a family of cellular proteins that help cells respond to stress, such as high temperatures or other environmental challenges. They […]