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Protein folding must be thermodynamically favorable within a cell in order for it to be a spontaneous reaction. Since it is known that protein folding is a spontaneous reaction, then it must assume a negative Gibbs free energy value. Gibbs free energy in protein folding is directly related to enthalpy and entropy. [12]
Chromatin is a complex of DNA and protein found in eukaryotic cells. [1] The primary function is to package long DNA molecules into more compact, denser structures. This prevents the strands from becoming tangled and also plays important roles in reinforcing the DNA during cell division , preventing DNA damage , and regulating gene expression ...
The unicellular algae known as dinoflagellates were previously thought to be the only eukaryotes that completely lack histones, [23] but later studies showed that their DNA still encodes histone genes. [24] Unlike the core histones, homologs of the lysine-rich linker histone (H1) proteins are found in bacteria, otherwise known as nucleoprotein ...
Inadvertently, H2A has been found to regulate gene expression. [10] DNA modification by H2A occurs in the cell nucleus. Proteins responsible for nuclear import of H2A protein are karyopherin and importin. [12] Recent studies also show that nucleosome assembly protein 1 is also used to transport of H2A into the nucleus so it can wrap DNA.
Heat shock protein chaperones are classified based on their observed molecular weights into Hsp60, Hsp70, Hsp90, Hsp104, and small Hsps. [5] The Hsp60 family of protein chaperones are termed chaperonins, and are characterized by a stacked double-ring structure and are found in prokaryotes, in the cytosol of eukaryotes, and in mitochondria.
Euchromatin (also called "open chromatin") is a lightly packed form of chromatin (DNA, RNA, and protein) that is enriched in genes, and is often (but not always) under active transcription. Euchromatin stands in contrast to heterochromatin, which is tightly packed and less accessible for transcription. 92% of the human genome is euchromatic. [1]
In the less extensive technique of equilibrium unfolding, the fractions of folded and unfolded molecules (denoted as and , respectively) are measured as the solution conditions are gradually changed from those favoring the native state to those favoring the unfolded state, e.g., by adding a denaturant such as guanidinium hydrochloride or urea.
This 'globin fold' typically consists of eight alpha helices, although some proteins have additional helix extensions at their termini. [4] Since the globin fold contains only helices, it is classified as an all-alpha protein fold. The globin fold is found in its namesake globin families as well as in phycocyanins. The globin fold was thus the ...