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- W6983265 abstract "This chapter discusses the four major categories of tertiary structure within which subtypes that are more specific described: (1) antiparallel a, (2) parallel α/β, (3) antiparallel β, and (4) small irregular proteins. Within this first major category, the simplest type of structure is the up-and-down helix bundle: an approximate cylinder of α-helices with each connected to its nearest neighbor. In the second major group of tertiary structures, the first subcategory is made up of large but remarkably simple domains with a central, eight stranded, parallel β-barrel and a concentric outer cylinder of eight α-helices. As in the antiparallel α proteins, the simplest type of antiparallel β domain forms an approximate cylinder, or barrel, with up-and-down nearest-neighbor connectivity between the strands all around. The fourth major category of protein structure is different logically from the other three, which are dominated by patterns of secondary structure. Although each protein structure is highly individual in what are probably its most significant aspects, there are three important advantages to be gained from relating its gross morphology to the overall classifications described. One of the advantages is that many of the tertiary structure types are recognizable even at low resolution, while use of the statistical preferences of each category in terms of handedness, twist, topology can greatly improve the chances of a correct chain tracing at intermediate resolution." @default.
- W6983265 created "2016-06-24" @default.
- W6983265 creator A5046412779 @default.
- W6983265 date "1985-01-01" @default.
- W6983265 modified "2023-09-23" @default.
- W6983265 title "Describing patterns of protein tertiary structure" @default.
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- W6983265 doi "https://doi.org/10.1016/0076-6879(85)15025-1" @default.
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