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Polar residues mediate differential ...

Dawson, Jessica P.

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Polar residues mediate differential effects of transmembrane helix association.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Polar residues mediate differential effects of transmembrane helix association./
作者:	Dawson, Jessica P.
面頁冊數:	103 p.
附註:	Source: Dissertation Abstracts International, Volume: 64-10, Section: B, page: 4768.
Contained By:	Dissertation Abstracts International64-10B.
標題:	Biology, Molecular. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3109387
ISBN:	0496569291

Polar residues mediate differential effects of transmembrane helix association.
Dawson, Jessica P.

Polar residues mediate differential effects of transmembrane helix association. - 103 p.

Source: Dissertation Abstracts International, Volume: 64-10, Section: B, page: 4768.

Thesis (Ph.D.)--Yale University, 2003.

This dissertation examines the varying effects of polar residues on transmembrane alpha-helix homo-oligomerization. The polar residues examined here can be divided into two categories, those that contain one polar group in their side chain (serine and threonine) and those that contain two polar groups (glutamine, glutamate, asparagine and aspartate). The results presented in this thesis show that the ability of each of these polar residues to promote helix association is strongly dependent upon their type, number of occurrences, and the context created by other nearby residues.

ISBN: 0496569291Subjects--Topical Terms:

1017719
Biology, Molecular.

Polar residues mediate differential effects of transmembrane helix association.
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245 1 0 $a Polar residues mediate differential effects of transmembrane helix association.
300 $a 103 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-10, Section: B, page: 4768.
500 $a Director: Donald M. Engelman.
502 $a Thesis (Ph.D.)--Yale University, 2003.
520 $a This dissertation examines the varying effects of polar residues on transmembrane alpha-helix homo-oligomerization. The polar residues examined here can be divided into two categories, those that contain one polar group in their side chain (serine and threonine) and those that contain two polar groups (glutamine, glutamate, asparagine and aspartate). The results presented in this thesis show that the ability of each of these polar residues to promote helix association is strongly dependent upon their type, number of occurrences, and the context created by other nearby residues.
520 $a Previous work indicated that while glutamine, glutamate, asparagine and aspartate can drive strong helix association, an individual serine and threonine residues cannot. In the present work, serine motifs that drive helix association were discovered by selection from a randomized library of transmembrane domains designed to identify amino acid motifs that promote homo-oligomerization. Selection of this library identified two serine-rich motifs, SxxSSxxT and SxxxSSxxT. Mutation of any residue in these motifs greatly reduced oligomerization, indicating that the interaction between helices having serine and threonine in these positions is specific and requires an extended motif. Computational modeling of these sequences produced several chemically plausible structures that contain multiple hydrogen bonds between the serines and threonines. While single serine or threonine side chains do not appear to promote helix association, motifs can drive strong and specific association through a cooperative network of interhelical hydrogen bonds.
520 $a In a second set of experiments, we tested whether the strongly polar residues glutamine, glutamate, asparagine and aspartate can drive helix association independent of surrounding side chain environments. Asparagine and aspartate were substituted for wild type amino acids in four consecutive positions in the transmembrane domain of the major coat protein from filamentous phage, creating four distinct contexts around the helix. Glutamine and glutamate mediated associations were examined in five naturally occurring transmembrane domains. The association of each of these transmembrane domains was examined using the TOXCAT system. The results indicate that these polar residues mediate helix interactions with a wide range of affinities that are modulated by their surrounding residues. These findings indicate that the potentially strong interaction between polar residues can be attenuated and controlled by the sequence environment, suggesting that not all instances of polar residues in transmembrane helices drive strong and nonspecific helix association.
590 $a School code: 0265.
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650 4 $a Biophysics, General. $3 1019105
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791 $a Ph.D.
792 $a 2003
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