Protein Structure - TRQ Flashcards
Dense hydrophobic cores are typical of…
Globular protein
Collagen is found in a(n)…
triple helix
Peptide bonds have a structure and geometry which is …
Rigid and planar
Secondary structure is stabilized by …
Hydrogen bonds
Silk fibroin is found in a(n) …
beta conformation
Beta-turns link together two adjacent segments of …
Antiparallel beta sheets
A recognizable folding pattern involving two or more elements of secondary structure is called…
Motif
a loss of 3-D structure sufficient to cause loss of function is called …
denaturation
A part of a polypeptide chain that is independently stable or could undergo movements as a single entity is known as a …
Domain
A visual description of the combinations of dihedral angles that are permitted in a peptide backbone is called …
Ramachandran plot
An example of a family of chaperones is …
Hsp70
An idealized alpha-helix contains how many residues per turn?
3.6 residues/turn
Biochemists can estimate the fraction of protein made up of a helix or beta sheet using …
Circular dichroism (CD) spectroscopy
In the beta conformation of polypeptide chains, the backbone is extended into a …
Zigzag
In alpha-keratins, the cross-links stabilizing quaternary structure are …
Disulfide bonds
Most enzymes and regulatory proteins are …
Globular proteins
Proteins can be denatured by …
Heat and extremes of pH
Proteins in their functional, folded conformations are called …
Native proteins
Proteins that catalyze the accurate folding of proteins are called …
Chaperones
Proteins with polypeptide chains folded into a spherical or globular shape are called …
Globular proteins
Proteins with polypeptide chains arranged in long strands or sheets are called …
Fibrous proteins
Proteins with significant similarity primary structure and/or tertiary structure and function are said to be in the same …
protein family
Returning to conditions in which the native conformation is stable is called …
Renaturation
Since the loss of structure in one part of the protein destabilizes other parts, the process of unfolding is …
Cooperative
Some multimeric proteins have a repeated unit consisting of a singe subunit or group of subunits called …
Protomer
The C-N bond in a peptide group cannot rotate freely because of …
Partial double-bond characters
The coiled-coil motif is found in …
alpha-Keratin
The local spatial arrangement of polypeptides is called …
Secondary structure
The spatial arrangement of atoms in a protein or any part of a protein is called its …
Conformation
The arrangement of two or more separate polypeptide chains in 3-D complexes is termed …
Quaternary structure
The elements that connect segments of antiparallel beta sheets are called …
beta turns
The major contributor in stabilizing the globular form of most soluble proteins is …
Hydrophobic interactions
The overall 3-D arrangement of all atoms in a protein, including longer-range aspects of amino acid sequence, is termed …
Tertiary structure
The structures that provide support, shape, and external protection to vertebrates are made of …
fibrous proteins
These proteins constitute hair, nails, wools, and much of the outer layer of skin.
alpha-keratin
This enzyme catalyzes the interchange of disulfide bonds until the native conformation is formed.
Protein disulfide isomerase (PDI)
This enzyme catalyzes the interconversion of the cis and trans isomers of Pro residue peptide bonds.
Peptide prolyl cis-trans isomerase (PPI)
This protein structure is found int he beta conformation and has soft, flexible filaments.
silk fibroin
This type of protein is found in connective tissue , such as tendon or cartilage.
collagen
