The correct answer is option B, that is, Cannon-Bard theory.
The Cannon-Bard theory of emotion also called the Thalamic theory of emotion. It is a physiological illustration of emotion created by Walter Cannon and Philip Bard. The theory states that one feels emotions and encounter physiological responses like trembling, sweating, and muscle-tension at the same time.
The Cannon-Bard theory suggests that one encounters physiological arousal and emotion at the similar time. The theory offers more attention to the role of outward behavior or thought that than was done by James-Lange.
1. Y-axis is type of sound being measured X-axis is the decibels/sound level for type of sound being measured
2. Whisper - 20 decibels, normal taking - 60 decibels, rock concert - 120 decibels
3. every ten decibels is ten times as loud. If a whisper is 20 decibels and normal talking is 60 decibels then normal talking is 40 times as intense as whispering
4. Rock concert, pain threshold and jet plane could be painful if exposed to them
Protein structure is the three-dimensional arrangement of atoms in a protein molecule. Proteins are polymers — specifically polypeptides — formed from sequences of amino acids, the monomers of the polymer. A single amino acid monomer may also be called a residue (chemistry) indicating a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond. By convention, a chain under 30 amino acids is often identified as a peptide, rather than a protein.[1] To be able to perform their biological function, proteins fold into one or more specific spatial conformations driven by a number of non-covalent interactions such as hydrogen bonding, ionic interactions, Van der Waals forces, and hydrophobic packing. To understand the functions of proteins at a molecular level, it is often necessary to determine their three-dimensional structure. This is the topic of the scientific field of structural biology, which employs techniques such as X-ray crystallography, NMR spectroscopy, and dual polarisation interferometry to determine the structure of proteins.
Protein structures range in size from tens to several thousand amino acids.[2] By physical size, proteins are classified as nanoparticles, between 1–100 nm. Very large aggregates can be formed from protein subunits. For example, many thousands of actin molecules assemble into a microfilament.
A protein may undergo reversible structural changes in performing its biological function. The alternative structures of the same protein are referred to as different conformational isomers, or simply, conformations, and transitions between them are called conformational changes.
