- Title Information
- Title
- Using x-ray crystallography to determine the effect of the antibiotic streptomycin on bacterial protein translation
- Name:
Personal
- Name Part
- Rangwala, Aziz
- Role
- Role Term:
Text
- creator
- Name:
Personal
- Name Part
- Murphy, Eileen L.
- Role
- Role Term:
Text
- creator
- affiliation
- Brown University. Department of Molecular Biology, Cell Biology, and Biochemistry
- Name:
Personal
- Name Part
- Gregory, Steven T.
- Role
- Role Term:
Text
- advisor
- affiliation
- Brown University. Department of Molecular Biology, Cell Biology, and Biochemistry
- Name:
Personal
- Name Part
- Jogl, Gerwald
- Role
- Role Term:
Text
- advisor
- affiliation
- Brown University. Department of Molecular Biology, Cell Biology, and Biochemistry
- Name:
Corporate
- Name Part
- Brown University. Undergraduate Teaching and Research Award
- Role
- Role Term:
Text
- research program
- Genre (aat)
- posters
- Origin Information
- Place
- Place Term:
Text
- Providence, RI
- Publisher
- Brown University
- Date Created
(keyDate="yes", encoding="w3cdtf")
- 2016
- Physical Description
- Extent
- 1 poster
- digitalOrigin
- reformatted digital
- Abstract
- The ribosome is a molecular machine responsible for assembling proteins in cells using a process known as translation. Proteins are necessary for all life, so without properly functioning ribosomes, cells will die. Streptomycin is a common antibiotic that disrupts bacterial protein ribosomes by interfering with the ribosome's method of linking amino acids. With the rise of antibiotic-resistant strains of bacteria, it is essential to understand how these antibiotics halt bacterial growth. One such method to do so involves crystallizing both a normal strain of bacteria and a strain that is dependent on streptomycin for survival. Once we have determined the optimal crystallization conditions for these ribosome-antibiotic crystals, we can use X-ray diffraction to determine the three-dimensional structure of the interaction. Using this knowledge, we can then synthesize novel compounds that mimic this interaction for use in antibiotic-resistant strains of bacteria.
- Subject (LCSH)
- Topic
- Ribosomes
- Subject (LCSH)
- Topic
- Streptomycin
- Subject (LCSH)
- Topic
- Bacteria
- Subject (LCSH)
- Topic
- Crystallography
- Identifier:
DOI
- 10.26300/as5x-8332
- Type of Resource
- text