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Secondary structure

The local folding of the polypeptide in some regions gives rise to the secondary structure    of the protein. The most common are the α -helix and β -pleated sheet structures ( [link] ). Both structures are the α -helix structure—the helix held in shape by hydrogen bonds. The hydrogen bonds form between the oxygen atom in the carbonyl group in one amino acid and another amino acid that is four amino acids farther along the chain.

The illustration shows an alpha helix protein structure, which coils like a spring, and a beta-pleated sheet structure, which forms flat sheets stacked together. In an alpha-helix, hydrogen bonding occurs between the carbonyl group of one amino acid and the amino group of the amino acid that occurs four residues later. In a beta-pleated sheet, hydrogen bonding occurs between two different lengths of peptide that are antiparallel to one another.
The α -helix and β -pleated sheet are secondary structures of proteins that form because of hydrogen bonding between carbonyl and amino groups in the peptide backbone. Certain amino acids have a propensity to form an α -helix, while others have a propensity to form a β -pleated sheet.

Every helical turn in an alpha helix has 3.6 amino acid residues. The R groups (the variant groups) of the polypeptide protrude out from the α -helix chain. In the β -pleated sheet, the “pleats” are formed by hydrogen bonding between atoms on the backbone of the polypeptide chain. The R groups are attached to the carbons and extend above and below the folds of the pleat. The pleated segments align parallel or antiparallel to each other, and hydrogen bonds form between the partially positive nitrogen atom in the amino group and the partially negative oxygen atom in the carbonyl group of the peptide backbone. The α -helix and β -pleated sheet structures are found in most globular and fibrous proteins and they play an important structural role.

Tertiary structure

The unique three-dimensional structure of a polypeptide is its tertiary structure    ( [link] ). This structure is in part due to chemical interactions at work on the polypeptide chain. Primarily, the interactions among R groups creates the complex three-dimensional tertiary structure of a protein. The nature of the R groups found in the amino acids involved can counteract the formation of the hydrogen bonds described for standard secondary structures. For example, R groups with like charges are repelled by each other and those with unlike charges are attracted to each other (ionic bonds). When protein folding takes place, the hydrophobic R groups of nonpolar amino acids lay in the interior of the protein, whereas the hydrophilic R groups lay on the outside. The former types of interactions are also known as hydrophobic interactions. Interaction between cysteine side chains forms disulfide linkages in the presence of oxygen, the only covalent bond forming during protein folding.

This illustration shows a polypeptide backbone folded into a three-dimensional structure. Chemical interactions between amino acid side chains maintain its shape. These include an ionic bond between an amino group and a carboxyl group, hydrophobic interactions between two hydrophobic side chains, a hydrogen bond between a hydroxyl group and a carbonyl group, and a disulfide linkage.
The tertiary structure of proteins is determined by a variety of chemical interactions. These include hydrophobic interactions, ionic bonding, hydrogen bonding and disulfide linkages.

All of these interactions, weak and strong, determine the final three-dimensional shape of the protein. When a protein loses its three-dimensional shape, it may no longer be functional.

Quaternary structure

In nature, some proteins are formed from several polypeptides, also known as subunits, and the interaction of these subunits forms the quaternary structure    . Weak interactions between the subunits help to stabilize the overall structure. For example, insulin (a globular protein) has a combination of hydrogen bonds and disulfide bonds that cause it to be mostly clumped into a ball shape. Insulin starts out as a single polypeptide and loses some internal sequences in the presence of post-translational modification after the formation of the disulfide linkages that hold the remaining chains together. Silk (a fibrous protein), however, has a β -pleated sheet structure that is the result of hydrogen bonding between different chains.

Questions & Answers

hetreothalism in fungi
Lekhram Reply
there are 3 trimester in human pregnancy
I don't know answer of this question can u help me
what is a cell
Fatima Reply
A cell is functional and structural unit of life.
what is genetic
Janet Reply
I join
what are the branchas of biology
Prisca Reply
zoology, ecology
genetics, microbiology,botany and embryology
what is a cell
Kulunbawi Reply
cell is smallest unit of life. cells are often cell the building blocks of life...
the first twenty element
Orapinega Reply
what are the characteristics of living things?
growth,respiration,nutrition,sensitivity, movement,irritability, excretion,death.
What is the difference between adaptation and competition in animals
Adeyemi Reply
What is biology
it is a natural science stadey about living things
Biology is the bronch of science which deals with the study of life is called biology
what is the x in 300 stands for?
Ogbudu Reply
the properties of life
Clarinda Reply
response to the environment, reproduction, homeostasis, growth,energy processing etc.....
what is reproduction
Reproduction is a fundamental feature of all known life,each individual organism exist as a result of re production.....or else Multiplying...
a complete virus particle known as
Darlington Reply
These are formed from identical protein subunitscalled capsomeres.
fabace family plant name
Pushpam Reply
in eukaryotes ...protein channel name which transport protein ...
Pushpam Reply
in bacteria ...chromosomal dna duplicate structure called
what is a prokaryotic cell and a eukaryotic cell
Matilda Reply
There are two types of cells. Eukaryotic and Prokaryotic cells. Prokaryotic cells don't have a nucleus or membrane enclosed organelles (little organs within that cell). They do however carry genetic material but it's not maintained in the nucleus. Prokaryotic cells are also one celled.
Prokaryotic cells are one celled (single celled).
Prokaryotic cells are Bacteria and Archea
Prokaryotic cells are smaller than Eukaryotic cells.
Eukaryotic cells are more complex. They are much bigger than Prokaryotic cells.
Eukaryotic cells have a nucleus and membrane bound organelles.
Eukaryotic cells are animals cells which also includes us.
Eukaryotic cells are also multicellular.
nice explaination
eukaryotic cells are individual cells .. but eukaryotes are multicellular organisms which consist of many different types of eukaryotic cells
also eukaryotic cells have mitochondria. prokaryotic cells do not
in prokaryotes only ribosomes are present... in eukaryotes mitochondria ...glogi bodies ..epidermis .....prokaryotes one envelop but eukaryotes compartment envelop....envelop mean membrane bound organelles......
prokaryotic cell are cells dat have no true nuclei i.e no cell membrane while eukaryotic cell are cell dat have true nuclei i.e have cell membrane
we have 46 pair of somatic cell and 23 pair of chromosomes in our body, pls can someone explain it to me. pls
Matilda Reply
we have 22 pairs of somatic chromosomes and one pair of sex chromosome
we have 23 pairs of chromosomes,22 pairs of somatic and one pair of sex chromosomes
23 chromosomes from dad & 23 chromosomes from mom 23 +23=46 total chromosomes
X & Y chromosomes are called sex cells, the very presence of a Y chromosome means the person is Male.
XX Female XY Male
If a Karyotype has more than 46 Chromosomes then nondisjunction occured. For example, having an extra chromosome 21 will cause Down Syndrome.
am caira I want to join
caira,whrere are u from
I'm a Ghanaian

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