An insight in the mechanism of beta sheet formation via CSAW.

Protein folding problem is an emerging eld in biophysics and great progress has been seen in experiments, theories and computations for the last 40 years. Approaching the problem with theoretical and computational studies, Conditioned Self-Avoiding Walk (CSAW) model is developed in the aim of st...

Full description

Saved in:
Bibliographic Details
Main Author: Goh, Boon Chong.
Other Authors: Chew Lock Yue
Format: Final Year Project
Language:English
Published: 2011
Subjects:
Online Access:http://hdl.handle.net/10356/45172
Tags: Add Tag
No Tags, Be the first to tag this record!
Institution: Nanyang Technological University
Language: English
id sg-ntu-dr.10356-45172
record_format dspace
spelling sg-ntu-dr.10356-451722023-02-28T23:11:17Z An insight in the mechanism of beta sheet formation via CSAW. Goh, Boon Chong. Chew Lock Yue School of Physical and Mathematical Sciences DRNTU::Science::Physics::Atomic physics::Statistical physics DRNTU::Science::Biological sciences::Biophysics Protein folding problem is an emerging eld in biophysics and great progress has been seen in experiments, theories and computations for the last 40 years. Approaching the problem with theoretical and computational studies, Conditioned Self-Avoiding Walk (CSAW) model is developed in the aim of studying the key interactions resulted in folding of a protein. The earlier versions of CSAW model consider hydrophobic interaction and hydrogen bonding while neglecting all other interactions. Though simple, these models have successfully formed hydrophobic core and alpha helix. However, none of them has consistently folded a beta sheet, the complementary secondary structure of alpha helix. In my Final Year Project, I consolidated various ideas in our research group and introduced the neighboring hydrogen bond interaction, also named as the 4-body interaction. After incorporating the 4-body interaction into CSAW, beta sheets are consistently formed. We continued to investigate the folding of polyalanine of di erent lengths and attempt to fold two real proteins in CSAW. At low temperatures, the polypeptides were folded into alpha helix while they formed beta sheet at higher temperatures. We observed as the length of protein increases, the transition temperature from alpha helix to beta sheet increases. Bachelor of Science in Physics 2011-06-09T07:41:46Z 2011-06-09T07:41:46Z 2011 2011 Final Year Project (FYP) http://hdl.handle.net/10356/45172 en 112 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic DRNTU::Science::Physics::Atomic physics::Statistical physics
DRNTU::Science::Biological sciences::Biophysics
spellingShingle DRNTU::Science::Physics::Atomic physics::Statistical physics
DRNTU::Science::Biological sciences::Biophysics
Goh, Boon Chong.
An insight in the mechanism of beta sheet formation via CSAW.
description Protein folding problem is an emerging eld in biophysics and great progress has been seen in experiments, theories and computations for the last 40 years. Approaching the problem with theoretical and computational studies, Conditioned Self-Avoiding Walk (CSAW) model is developed in the aim of studying the key interactions resulted in folding of a protein. The earlier versions of CSAW model consider hydrophobic interaction and hydrogen bonding while neglecting all other interactions. Though simple, these models have successfully formed hydrophobic core and alpha helix. However, none of them has consistently folded a beta sheet, the complementary secondary structure of alpha helix. In my Final Year Project, I consolidated various ideas in our research group and introduced the neighboring hydrogen bond interaction, also named as the 4-body interaction. After incorporating the 4-body interaction into CSAW, beta sheets are consistently formed. We continued to investigate the folding of polyalanine of di erent lengths and attempt to fold two real proteins in CSAW. At low temperatures, the polypeptides were folded into alpha helix while they formed beta sheet at higher temperatures. We observed as the length of protein increases, the transition temperature from alpha helix to beta sheet increases.
author2 Chew Lock Yue
author_facet Chew Lock Yue
Goh, Boon Chong.
format Final Year Project
author Goh, Boon Chong.
author_sort Goh, Boon Chong.
title An insight in the mechanism of beta sheet formation via CSAW.
title_short An insight in the mechanism of beta sheet formation via CSAW.
title_full An insight in the mechanism of beta sheet formation via CSAW.
title_fullStr An insight in the mechanism of beta sheet formation via CSAW.
title_full_unstemmed An insight in the mechanism of beta sheet formation via CSAW.
title_sort insight in the mechanism of beta sheet formation via csaw.
publishDate 2011
url http://hdl.handle.net/10356/45172
_version_ 1759853233741758464