Advanced

Two-dimensional classification of interfacial and partitioning properties of amino acids

Casellas Soler, Josep LU (2011) KEMP37 20111
Department of Chemistry
Abstract
A classification of amino acid residues based on the interfacial and
partitioning properties was introduced by Khokhlov et al. [1] [2] Amino acid
residues are characterized by two parameters: the standard free energy of
adsorption of an amino acid at an octanol/water interface and the standard
free energy of the partition of an amino acid between octanol and water,
both of them normalized by kT. As a result, five groups of amino acids
having similar values of the parameters are identified.
This classification for the amino acids is based in trace correlations between
two one-dimensional parameters which are related with the interactions in
the biological environment: hydrophilic / hydrophobic behaviour (partition)
and activity at... (More)
A classification of amino acid residues based on the interfacial and
partitioning properties was introduced by Khokhlov et al. [1] [2] Amino acid
residues are characterized by two parameters: the standard free energy of
adsorption of an amino acid at an octanol/water interface and the standard
free energy of the partition of an amino acid between octanol and water,
both of them normalized by kT. As a result, five groups of amino acids
having similar values of the parameters are identified.
This classification for the amino acids is based in trace correlations between
two one-dimensional parameters which are related with the interactions in
the biological environment: hydrophilic / hydrophobic behaviour (partition)
and activity at the interface (surface tension). This method is believed to be
able to provide promising results in the search of correlation giving rise to
protein sequences.
A comparison of the parameters in question gives information on energetic
preferences of the molecules to be located at the interface or in a bulk
phase. This study is applied on serine, threonine, aspartic acid, glutamic acid
and tyrosine. (Less)
Abstract
Popular Science Summary
The protein folding is the physical process in which a protein withdraws into
its characteristic three-dimensional structure and function. Each protein
begins as a linear chain of amino acids, resulted from a sequence of our
genetic material, and does not have three-dimensional structure. However,
each amino acid chain has certain chemical characteristics that can influence
to the folding like hydrophobia and hydrophilia.
These amino acids interact with each other in their cellular environment to
produce a well-defined three-dimensional shape, the folded protein, known
as native state. The mechanism of protein folding is not completely
understood.
However, the three-dimensional protein structure is... (More)
Popular Science Summary
The protein folding is the physical process in which a protein withdraws into
its characteristic three-dimensional structure and function. Each protein
begins as a linear chain of amino acids, resulted from a sequence of our
genetic material, and does not have three-dimensional structure. However,
each amino acid chain has certain chemical characteristics that can influence
to the folding like hydrophobia and hydrophilia.
These amino acids interact with each other in their cellular environment to
produce a well-defined three-dimensional shape, the folded protein, known
as native state. The mechanism of protein folding is not completely
understood.
However, the three-dimensional protein structure is essential to perform its
function. If the protein does not fold into the desired shape, typically
produce inactive proteins with different properties including toxic. Some
neurodegenerative diseases among others are considered the consequence
of the accumulation of incorrectly folded proteins. Therefore it is important
to know which factors affect the protein folding and how we can predict its
final structure. (Less)
Please use this url to cite or link to this publication:
author
Casellas Soler, Josep LU
supervisor
organization
course
KEMP37 20111
year
type
H2 - Master's Degree (Two Years)
subject
keywords
Fysikalisk kemi
language
English
id
3222108
date added to LUP
2012-12-07 16:55:53
date last changed
2012-12-07 16:55:53
@misc{3222108,
  abstract     = {Popular Science Summary
The protein folding is the physical process in which a protein withdraws into
its characteristic three-dimensional structure and function. Each protein
begins as a linear chain of amino acids, resulted from a sequence of our
genetic material, and does not have three-dimensional structure. However,
each amino acid chain has certain chemical characteristics that can influence
to the folding like hydrophobia and hydrophilia.
These amino acids interact with each other in their cellular environment to
produce a well-defined three-dimensional shape, the folded protein, known
as native state. The mechanism of protein folding is not completely
understood.
However, the three-dimensional protein structure is essential to perform its
function. If the protein does not fold into the desired shape, typically
produce inactive proteins with different properties including toxic. Some
neurodegenerative diseases among others are considered the consequence
of the accumulation of incorrectly folded proteins. Therefore it is important
to know which factors affect the protein folding and how we can predict its
final structure.},
  author       = {Casellas Soler, Josep},
  keyword      = {Fysikalisk kemi},
  language     = {eng},
  note         = {Student Paper},
  title        = {Two-dimensional classification of interfacial and partitioning properties of amino acids},
  year         = {2011},
}