| LDR |  | 00000nmm u2200205   4500 | 
| 001 |  | 000000331395 | 
| 005 |  | 20241115163138 | 
| 008 |  | 181129s2018    |||    |   | |      eng d | 
| 020 |    | 
    ▼a 9780438193505 | 
| 035 |    | 
    ▼a (MiAaPQ)AAI10917780 | 
| 040 |    | 
    ▼a MiAaPQ
    ▼c MiAaPQ
    ▼d 248032 | 
| 049 | 1  | 
    ▼f DP | 
| 082 | 0  | 
    ▼a 574 | 
| 100 | 1  | 
    ▼a Gaines, Jennifer Christine. | 
| 245 | 10 | 
    ▼a Computational Studies of Protein Structure. | 
| 260 |    | 
    ▼a [S.l.] :
    ▼b Yale University.,
    ▼c 2018 | 
| 260 |  1 | 
    ▼a Ann Arbor :
    ▼b ProQuest Dissertations & Theses,
    ▼c 2018 | 
| 300 |    | 
    ▼a 101 p. | 
| 500 |    | 
    ▼a Source: Dissertation Abstracts International, Volume: 79-11(E), Section: B. | 
| 500 |    | 
    ▼a Adviser: Corey S. O'Hern. | 
| 502 | 1  | 
    ▼a Thesis (Ph.D.)--Yale University, 2018. | 
| 520 |    | 
    ▼a Although much is known about the experimentally measurable properties of individual proteins, we do not have a solid understanding of the universal properties that control protein structure and stability. The amount of protein crystal structure | 
| 520 |    | 
    ▼a My work, building on prior protein structural studies, uses the new plethora of protein crystal structure data to develop a deeper understanding of the physical properties of proteins. I focus on using an atomistic model of proteins, involving s | 
| 520 |    | 
    ▼a This dissertation presents three related computational studies of the properties of protein structures. In the first study, I present an analysis of the packing fraction of protein cores. I show that protein cores are composed of random close pa | 
| 520 |    | 
    ▼a I then take a more detailed look at protein cores to quantify the amount of side chain dihedral angle movement possible in the core. To do this, I apply a hard-sphere model with stereochemical constraints to rotate the side chain dihedral angles | 
| 520 |    | 
    ▼a Finally, I expand both of these studies to two other protein types: protein-protein interfaces and transmembrane proteins. For both datasets, I investigate the packing fraction and side chain predictability of both core and solvent exposed amino | 
| 520 |    | 
    ▼a This thesis work challenges the commonly accepted properties of protein structure, in particular that proteins have a high packing fraction similar to crystalline packing of spheres and that transmembrane proteins are fundamentally different fro | 
| 590 |    | 
    ▼a School code: 0265. | 
| 650 |  4 | 
    ▼a Bioinformatics. | 
| 650 |  4 | 
    ▼a Biophysics. | 
| 650 |  4 | 
    ▼a Computational physics. | 
| 690 |    | 
    ▼a 0715 | 
| 690 |    | 
    ▼a 0786 | 
| 690 |    | 
    ▼a 0216 | 
| 710 | 20 | 
    ▼a Yale University. | 
| 773 | 0  | 
    ▼t Dissertation Abstracts International
    ▼g 79-11B(E). | 
| 773 |    | 
    ▼t Dissertation Abstract International | 
| 790 |    | 
    ▼a 0265 | 
| 791 |    | 
    ▼a Ph.D. | 
| 792 |    | 
    ▼a 2018 | 
| 793 |    | 
    ▼a English | 
| 856 | 40 | 
    ▼u http://www.riss.kr/pdu/ddodLink.do?id=T15000815
    ▼n KERIS | 
| 980 |    | 
    ▼a 201812
    ▼f 2019 | 
| 990 |    | 
    ▼a 관리자
    ▼b 관리자 |