3D structure of Proteins :
-
A Terms to memorize A
·
conformation : the fold , or structure ; can refer to local or overall .
·
Native Conformation : the fold within biological activity
·
primary structure
:
the sequence of amino acids; No intrinsic fold
folds of the linear helixes and beta sheets
secondary structure : the
peptide takes ;
Alpha
·
·
tertiary structure : the folds of the alpha helixes and beta sheets of a
peptide adopt as a whole
structure : of multiple peptide associating form one
protein also referred
quaternary comprised chains to
·
to as subunits
that remain
Domains specific clusters of secondary structure elements in
tertiary configuration
·
:
folded even when separated from the rest of the protein
Prosthetic Groups
· :
Protein elements covalently joined to the protein that are NOT amino acids
* idea of what secondary structure and affects the behavior of
primary sequence gives
the protein *
secondary structure >
-
alpha helices & beta sheed
·
peptide bonds are not rotatable , however the N-C bond (Pphibond) is rotatabl ?
↳ taken in this order the bonds are Used a Ramachondran plot to measure the
, on
"Correctness" fold. Anything but
of the
protein outside of ideal angles may still
happen may import
stain- Strain can characteristics of the Protein
>
provide some
The C-C bond following the bond also rotates and is termed ↑
(psi)
Helix backbone atoms Side chains direct the creation of helix
Alpha created by Hydrogen-bonds between a
: .
but are not involved in
bunding
The C-O group hydrogen bonded to the N-H that is y acids away
is
group amiro
the atoms are arranged linearly to maximize hydrogen bond strength
·
3 6
.
residues for a
complete turn, and the
pince is 37
.
%
Problem structures can
disrupt these structures
,
Larg Side chains can care crowding , charges can cause problems
Beta sheets hydrogen bonding
: Extend
peptide backbone side chains NOT involved in the
,
pattern
brise above and below the
plain of .
the sheet Infrastrand & Interstand Parallel & antiparallel .
-
A Terms to memorize A
·
conformation : the fold , or structure ; can refer to local or overall .
·
Native Conformation : the fold within biological activity
·
primary structure
:
the sequence of amino acids; No intrinsic fold
folds of the linear helixes and beta sheets
secondary structure : the
peptide takes ;
Alpha
·
·
tertiary structure : the folds of the alpha helixes and beta sheets of a
peptide adopt as a whole
structure : of multiple peptide associating form one
protein also referred
quaternary comprised chains to
·
to as subunits
that remain
Domains specific clusters of secondary structure elements in
tertiary configuration
·
:
folded even when separated from the rest of the protein
Prosthetic Groups
· :
Protein elements covalently joined to the protein that are NOT amino acids
* idea of what secondary structure and affects the behavior of
primary sequence gives
the protein *
secondary structure >
-
alpha helices & beta sheed
·
peptide bonds are not rotatable , however the N-C bond (Pphibond) is rotatabl ?
↳ taken in this order the bonds are Used a Ramachondran plot to measure the
, on
"Correctness" fold. Anything but
of the
protein outside of ideal angles may still
happen may import
stain- Strain can characteristics of the Protein
>
provide some
The C-C bond following the bond also rotates and is termed ↑
(psi)
Helix backbone atoms Side chains direct the creation of helix
Alpha created by Hydrogen-bonds between a
: .
but are not involved in
bunding
The C-O group hydrogen bonded to the N-H that is y acids away
is
group amiro
the atoms are arranged linearly to maximize hydrogen bond strength
·
3 6
.
residues for a
complete turn, and the
pince is 37
.
%
Problem structures can
disrupt these structures
,
Larg Side chains can care crowding , charges can cause problems
Beta sheets hydrogen bonding
: Extend
peptide backbone side chains NOT involved in the
,
pattern
brise above and below the
plain of .
the sheet Infrastrand & Interstand Parallel & antiparallel .
