For each blank select one entry from the corresponding column of choices.
Fill all blanks in the way the best completes the text.

For each blank select one entry from the corresponding column of choices.
Fill all blanks in the way the best completes the text.

As Ellen Donkin explains, in 18th England, writing plays (i)_____ women. Even when the (ii)_______ meant that playwriting did not bring personal fame, the work nevertheless enabled them to present their own views to the public and offered the possibility of acquiring capital.

For each blank select one entry from the corresponding column of choices.
Fill all blanks in the way the best completes the text.

Within the culture as a whole, natural science has been so successful that the word “scientific” is used in (i)_______ manner; it is often assumed that to call something “scientific” is to imply that its reliability has been (ii)_______ by research whose results cannot reasonably be (iii)______.

Within the culture as a whole, natural science has been so successful that the word “scientific” is used in (i)_______ manner; it is often assumed that to call something “scientific” is to imply that its reliability has been (ii)_______ by research whose results cannot reasonably be (iii)______.

Only an effective collaboration between filmmakers and art historians can create films that will enhance viewers’ perceptions of art. Filmmakers need to resist the impulse to move the camera quickly from detail to detail for fear of boring the viewer, to frame the image for the sake of drama alone, to add music for fear of silence. Filmmakers are aware that an art object demands concentration and, at the same time, are concerned that it may not be compelling enough―and so they hope to provide relief by interposing “real” scenes that bear only a tangential relationship to the subject. But a work of art needs to be explored on its own terms. On the other hand, art historians need to trust that one can indicate and analyze, not solely with words, but also by directing the viewer’s gaze. The specialized written language of art history needs to be relinquished or at least tempered for the screen.

Historically, sociologists have presumed that people will attribute certain characteristics to a member of a particular group when it is generally believed that most members of that group possess the characteristics in question. For sociologists Hepburn and Locksley, such social stereotyping has led to the broader question of whether people are cognizant of their own stereotyping behavior. Seemingly, if one knows that one holds a stereotypical notion such as “all members of a certain ethnic group are natural musicians,” then one might also be aware that the notion that “a particular musician of that ethnic group is a great musician” is a corollary of that stereotype. However, people are most aware of their stereotyping when they have no information. When given information that conforms to their beliefs and the individual case observed, people become less aware of their tendency to stereotype and therefore more likely to engage in stereotyping.

Q. The author of the passage is primarily concerned with

Geologists believe that one of the largest volcanic eruptions in human history occurred 74,000 years ago, the Toba supereruption. In one area, Middle Paleolithic tools of similar styles have been found and dated to closely before and after the Toba supereruption, indicating that the humans who lived after the supereruption were members of the population that had lived in that area prior to the eruption.

Select the two answer choices that, when used to complete the sentence,
fit the meaning of the sentence as a whole and produce completed sentences that are alike in meaning.

As people age, their cells become less efficient and less able to replace damaged components. At the same time their tissues stiffen. For example, the lungs and the heart muscle expand less successfully, the blood vessels become increasingly rigid, and the ligaments and tendons tighten.

Few investigators would attribute such diverse effects to a single cause. Nevertheless, researchers have discovered that a process long known to discolor and toughen foods may also contribute to age- related impairment of both cells and tissues. That process is nonenzymatic glycosylation, whereby glucose becomes attached to proteins without the aid of enzymes. When enzymes attach glucose to proteins (enzymatic glycosylation), they do so at a specific site on a specific protein molecule for a specific purpose. In contrast, the nonenzymatic process adds glucose haphazardly to any of several sites along any available peptide chain within a protein molecule.

This nonenzymatic glycosylation of certain proteins has been understood by food chemists for decades, although few biologists recognized until recently that the same steps could take place in the body. Nonenzymatic glycosylation begins when an aldehyde group (CHO) of glucose and an amino group (NH2) of a protein are attracted to each other. The molecules combine, forming what is called a Schiff base within the protein. This combination is unstable and quickly rearranges itself into a stabler, but still reversible, substance known as an Amadori product.

If a given protein persists in the body for months or years, some of its Amadori products slowly dehydrate and rearrange themselves yet again, into new glucose-derived structures. These can combine with various kinds of molecules to form irreversible structures named advanced glycosylation end products (AGE’s). Most AGE’s are yellowish brown and fluorescent and have specific spectrographic properties. More important for the body, many are also able to cross-link adjacent proteins, particularly ones that give structure to tissues and organs. Although no one has yet satisfactorily described the origin of all such bridges between proteins, many investigators agree that extensive cross-linking of proteins probably contributes to the stiffening and loss of elasticity characteristic of aging tissues.

In an attempt to link this process with the development of cataracts (the browning and clouding of the lens of the eye as people age), researchers studied the effect of glucose on solutions of purified crystallin, the major protein in the lens of the eye. Glucose-free solutions remained clear, but solutions with glucose caused the proteins to form clusters, suggesting that the molecules had become cross-linked. The clusters diffracted light, making the solution opaque. The researchers also discovered that the pigmented cross-links in human cataracts have the brownish color and fluorescence characteristic of AGE’s. These data suggest that nonenzymatic glycosylation of lens crystallins may contribute to cataract formation.

As people age, their cells become less efficient and less able to replace damaged components. At the same time their tissues stiffen. For example, the lungs and the heart muscle expand less successfully, the blood vessels become increasingly rigid, and the ligaments and tendons tighten.

Few investigators would attribute such diverse effects to a single cause. Nevertheless, researchers have discovered that a process long known to discolor and toughen foods may also contribute to age- related impairment of both cells and tissues. That process is nonenzymatic glycosylation, whereby glucose becomes attached to proteins without the aid of enzymes. When enzymes attach glucose to proteins (enzymatic glycosylation), they do so at a specific site on a specific protein molecule for a specific purpose. In contrast, the nonenzymatic process adds glucose haphazardly to any of several sites along any available peptide chain within a protein molecule.

This nonenzymatic glycosylation of certain proteins has been understood by food chemists for decades, although few biologists recognized until recently that the same steps could take place in the body. Nonenzymatic glycosylation begins when an aldehyde group (CHO) of glucose and an amino group (NH2) of a protein are attracted to each other. The molecules combine, forming what is called a Schiff base within the protein. This combination is unstable and quickly rearranges itself into a stabler, but still reversible, substance known as an Amadori product.

If a given protein persists in the body for months or years, some of its Amadori products slowly dehydrate and rearrange themselves yet again, into new glucose-derived structures. These can combine with various kinds of molecules to form irreversible structures named advanced glycosylation end products (AGE’s). Most AGE’s are yellowish brown and fluorescent and have specific spectrographic properties. More important for the body, many are also able to cross-link adjacent proteins, particularly ones that give structure to tissues and organs. Although no one has yet satisfactorily described the origin of all such bridges between proteins, many investigators agree that extensive cross-linking of proteins probably contributes to the stiffening and loss of elasticity characteristic of aging tissues.

In an attempt to link this process with the development of cataracts (the browning and clouding of the lens of the eye as people age), researchers studied the effect of glucose on solutions of purified crystallin, the major protein in the lens of the eye. Glucose-free solutions remained clear, but solutions with glucose caused the proteins to form clusters, suggesting that the molecules had become cross-linked. The clusters diffracted light, making the solution opaque. The researchers also discovered that the pigmented cross-links in human cataracts have the brownish color and fluorescence characteristic of AGE’s. These data suggest that nonenzymatic glycosylation of lens crystallins may contribute to cataract formation.