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020 ▼a 9780438269422
035 ▼a (MiAaPQ)AAI10957201
040 ▼a MiAaPQ ▼c MiAaPQ ▼d 248032
0820 ▼a 574.191
1001 ▼a Virrueta, Alejandro.
24510 ▼a Predicting side-chain dihedral angles of protein cores and beyond: An exploration of the limits of the hard-sphere model.
260 ▼a [S.l.] : ▼b Yale University., ▼c 2018
260 1 ▼a Ann Arbor : ▼b ProQuest Dissertations & Theses, ▼c 2018
300 ▼a 130 p.
500 ▼a Source: Dissertation Abstracts International, Volume: 79-12(E), Section: B.
500 ▼a Adviser: Corey S. O'Hern.
5021 ▼a Thesis (Ph.D.)--Yale University, 2018.
520 ▼a Existing computational approaches for protein structure modeling and prediction typically involve a multi-term potential energy function, more commonly referred to as a 'force field'. These force fields typically model various physical phenomena
520 ▼a To address this problem, my dissertation examines the extent to which a simplified energy function that includes only stereochemical constraints and repulsive hard-sphere interactions can correctly predict side-chain dihedral angles of amino aci
520 ▼a This dissertation presents three major computational studies. I first examine the hard-sphere predictions of single and multiple repacking of residues in protein cores, and demonstrate that steric interactions are the dominant force in specifyin
520 ▼a This work contributes to the forefront of computational protein design by providing an alternate, simplified approach to protein modeling and an understanding of the limitations of the hard-sphere model. With this information, we can gain fundam
590 ▼a School code: 0265.
650 4 ▼a Biophysics.
650 4 ▼a Computational physics.
690 ▼a 0786
690 ▼a 0216
71020 ▼a Yale University.
7730 ▼t Dissertation Abstracts International ▼g 79-12B(E).
773 ▼t Dissertation Abstract International
790 ▼a 0265
791 ▼a Ph.D.
792 ▼a 2018
793 ▼a English
85640 ▼u http://www.riss.kr/pdu/ddodLink.do?id=T15001238 ▼n KERIS
980 ▼a 201812 ▼f 2019
990 ▼a 관리자