A protein is driven into its structure
by hydrophobic interactions with water. The final folding
of a protein is determined by its primary structure-by the
chemical nature of its side groups. Many proteins can be
fully unfolded ("denatured") and will spontaneously refold
back into their characteristic shape.
The stability of a protein, once it has folded into its 3-D
shape, is strongly influenced by how well its interior fits
together. When two nonpolar chains in the interior are in
very close proximity, they experience a form of molecular
attraction called van der Waal's forces. Individually quite
weak, these forces can add up to a strong attraction when
many of them come into play, like the combined strength
of hundreds of hooks and loops on a strip of Velcro. They
are effective forces only over short distances, however;
there are no "holes" or cavities in the interior of proteins.
That is why there are so many different nonpolar amino
acids (alanine, valine, leucine, isoleucine). Each has a different
sized R group, allowing very precise fitting of nonpolar
chains within the protein interior. That's
why a mutation that converts one nonpolar amino
acid within the protein interior (alanine) into another
(leucine) very often disrupts the protein's stability; leucine
is a lot bigger than alanine and disrupts the precise way the
chains fit together within the protein interior. A change in
even a single amino acid can have profound effects on protein
shape and can result in loss or altered function of the
protein.
chaperon protiens
No, out of a near infinitude of possible ways to fold, a protein picks one in just tens of microseconds.
They help fold and coil DNA to make it smaller.
Proteins are composed of amino acids, which are the building blocks of proteins. Amino acids are linked together through peptide bonds to form polypeptide chains, which then fold into complex three-dimensional structures to create functional proteins.
Ribosomes are the organelles responsible for manufacturing proteins within cells. They can be found free-floating in the cytoplasm or attached to the endoplasmic reticulum, forming rough ER. Ribosomes translate messenger RNA (mRNA) into polypeptide chains, which then fold into functional proteins.
chaperon protiens
yes
yup
No, out of a near infinitude of possible ways to fold, a protein picks one in just tens of microseconds.
They help fold and coil DNA to make it smaller.
They help fold and coil DNA to make it smaller.
Proteins have a lower limit to their size because they need to have a certain number of amino acids to fold into a functional three-dimensional structure. If a protein is too small, it may not be able to fold properly and perform its biological function.
Amino acids are the building blocks of proteins. They link together in a specific sequence to form long chains, which then fold into complex shapes to create proteins. This process is essential for the structure and function of proteins in the body.
Proteins are composed of amino acids, which are the building blocks of proteins. Amino acids are linked together through peptide bonds to form polypeptide chains, which then fold into complex three-dimensional structures to create functional proteins.
Proteins are built as chains of amino acids, which then fold into unique three-dimensional shapes. Bonding within protein molecules helps stabilize their structure, and the final folded forms of proteins are well-adapted for their functions.
Because enzymes are proteins. Short proteins are called poypeptides.
Proteins help condense chromosomes by binding to the DNA and causing it to coil and fold into a more compact structure. This helps organize the genetic material and allows it to fit inside the cell's nucleus.