Phospholipids will form a bilayer in water because they contain hydrophobic (Water fearing.. in this cause water "hating") tails and hydrophilic heads (water loving). So they form a bilayer to remove the tails from water likewise, this satisfies the hydrophilic heads because they are still exposed to water.
The question is incomplete. The complete question is as follows:
Which of the following mutations is most likely to cause a phenotypic change?
A) a duplication of all or most introns
B) a large inversion whose ends are each in intergenic regions
C) a nucleotide substitution in an exon coding for a transmembrane domain
D) a single nucleotide deletion in an exon coding for an active site
E) a frameshift mutation one codon away from the 3' end of the nontemplate strand
Answer: D) a single nucleotide deletion in an exon coding for an active site
Explanation:
Deletion or insertion of a single nucleotide in an axon coding for an active site is called frameshift mutation.
The sequence of codons is read during translation, in order to synthesize a amino acids chain and form a protein from the nucleotide sequence. Frameshift mutations occur when the usual codon sequence is broken by the deletion or addition of one or more nucleotides. For example, if only one nucleotide is removed from the axon sequence during the RNA splicing process, then there will be a disrupted reading frame for all codons before and after the mutation. This may result in several incorrect amino acids being introduced into the protein. Disruption in protein sequence will cause phenotypic change.
Hence, the correct option is D) a single nucleotide deletion in an exon coding for an active site
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I believe those are both non-contact forces bc it's not something physical
The affinity of hemoglobin for oxygen is less than its structural analog myoglobin. However, this does not affect hemoglobin's usefulness for the body; on the contrary, it allows hemoglobin to be a more efficient carrier than myoglobin. This is because hemoglobin can release oxygen more easily than can myoglobin. It is both important for oxygen to be carried to different areas and also to be released when needed. The higher affinity of a given protein for oxygen, the harder it will be for that protein to release oxygen when needed. Therefore, hemoglobin's lower affinity for oxygen serves it well because it allows hemoglobin to release oxygen more easily in the body.
