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020 ▼a 9780355613582
035 ▼a (MiAaPQ)AAI10690891
035 ▼a (MiAaPQ)purdue:22056
040 ▼a MiAaPQ ▼c MiAaPQ ▼d 247004
0820 ▼a 631
1001 ▼a Xiang, Ning.
24510 ▼a Investigation of Interaction Between Peptide and Lipid Bilayer by Molecular Dynamics Simulation.
260 ▼a [S.l.]: ▼b Purdue University., ▼c 2017.
260 1 ▼a Ann Arbor: ▼b ProQuest Dissertations & Theses, ▼c 2017.
300 ▼a 152 p.
500 ▼a Source: Dissertation Abstracts International, Volume: 79-07(E), Section: B.
500 ▼a Adviser: Ganesan Narsimhan.
5021 ▼a Thesis (Ph.D.)--Purdue University, 2017.
506 ▼a This item is not available from ProQuest Dissertations & Theses.
520 ▼a Antimicrobial peptides (AMPs) inactivate microbial cells through pore formation in cell membrane. Because of their different mode of action compared to antibiotics, AMPs can be effectively used to combat drug resistant bacteria in human health.
520 ▼a The effects of (i) number of total and net charges, (ii) hydrophobicity (iii) hydrophobic moment and (iv) helicity of peptides from soy protein on their ability to bind to lipid bilayer and their transmembrane aggregates to form pores were inves
520 ▼a MD simulation was also employed to investigation interaction between amyloid beta (Abeta) peptide and lipid bilayer. Some amyloid-related proteins/peptides are involved in aggregation and pore formation in phospholipid membranes (cell membranes)
590 ▼a School code: 0183.
650 4 ▼a Agricultural engineering.
650 4 ▼a Food science.
650 4 ▼a Computational chemistry.
690 ▼a 0539
690 ▼a 0359
690 ▼a 0219
71020 ▼a Purdue University. ▼b Agricultural and Biological Engineering.
7730 ▼t Dissertation Abstracts International ▼g 79-07B(E).
773 ▼t Dissertation Abstract International
790 ▼a 0183
791 ▼a Ph.D.
792 ▼a 2017
793 ▼a English
85640 ▼u http://www.riss.kr/pdu/ddodLink.do?id=T14996789 ▼n KERIS ▼z 이 자료의 원문은 한국교육학술정보원에서 제공합니다.
980 ▼a 201812 ▼f 2019
990 ▼a ***1012033