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Biochemistry Module for BSED Students

This document contains information about different types of conjugated proteins including: - Nucleoproteins which contain DNA or RNA linked to a protein. - Chromoproteins which contain a pigmented group like heme that give blood its red color. - Lecithoproteins which are proteins derived from simple or conjugated proteins through physical processes. - Phosphoproteins which have phosphate bonded to serine, threonine, or tyrosine residues, regulating protein activity. - Glycoproteins which have carbohydrates bonded to serine, threonine, or asparagine residues, affecting solubility, lifespan, and extracellular/membrane functions.
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0% found this document useful (0 votes)
61 views2 pages

Biochemistry Module for BSED Students

This document contains information about different types of conjugated proteins including: - Nucleoproteins which contain DNA or RNA linked to a protein. - Chromoproteins which contain a pigmented group like heme that give blood its red color. - Lecithoproteins which are proteins derived from simple or conjugated proteins through physical processes. - Phosphoproteins which have phosphate bonded to serine, threonine, or tyrosine residues, regulating protein activity. - Glycoproteins which have carbohydrates bonded to serine, threonine, or asparagine residues, affecting solubility, lifespan, and extracellular/membrane functions.
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RYAN CHRISTOPHER A.

SODSOD
BSED-II-C-SCIENCE
BIOCHEMISTRY MODULE 7-8

PRE-TEST
1. D
2. A
3. B
4. C
5. E

Activity 1.
1. Nucleoprotein, conjugated protein consisting of a protein linked to a nucleic acid,
either DNA (deoxyribonucleic acid) or RNA (ribonucleic acid). The protein combined with DNA is
commonly either histone or protamine; the resulting nucleoproteins are found in chromosomes. Many
viruses are little more than organized collections of deoxyribonucleoproteins. Little is known about the
proteins linked with RNA; unlike protamine and histone, they appear to contain the amino
acid tryptophan.
2. A chromoprotein is a conjugated protein that contains a pigmented prosthetic group (or cofactor). A
common example is haemoglobin, which contains a heme cofactor, which is the iron-containing
molecule that makes oxygenated blood appear red. Other examples of chromoproteins include
other hemochromes, cytochromes, phytochromes and flavoproteins.[1]
In hemoglobin there exists a chromoprotein (tetramer MW:4 x 16.125 =64.500), namely heme,
consisting of Fe++ four pyrrol rings.
A single chromoprotein can act as both a phytochrome and a phototropin due to the presence and
processing of multiple chromophores. Phytochrome in ferns contains PHY3 which contains an unusual
photoreceptor with a dual-channel possessing both phytochrome (red-light sensing) and phototropin
(blue-light sensing) and this helps the growth of fern plants at low sunlight.
3. Lecithoproteins derived proteins. These are proteins derived from simple or conjugated proteins by
physical and are found in biological materials with different physical characteristics.
4. Phosphoproteins. These are proteins with a phosphate covalently bound to the side chain hydroxyl
groups of either serine, threonine or tyrosine. Phosphorylation often regulates the functional activity of
the protein to which it is bound (i.e. turning it on or off depending on the state of phosphorylation). This
regulation often is part of a signal transduction pathway from outside to inside the cell.
5. Glycoproteins. These have carbohydrate, typically covalently bonded to either Ser, Thr or Asn side
chains. Often confers added solubility, serves to regulate the in vivo half-life, and is a commonly
observed modification in extracellular and membrane-bound proteins. Can also function in cell-cell
communication and identity.

Activity 2.
1. A chemical digestion process called enzymatic hydrolysis can break the bonds holding the molecular
'building blocks' within the food together. In enzymatic hydrolysis reactions, an enzyme incorporates a
water molecule across the bond, allowing it to break.
2. Protein nitrogen turned out to be on average 95% of total nitrogen (Ntotal), which explains why
the average kA defined as true protein/Nprotein is with 5.6 only 5% larger compared to our already
mentioned average kp = true protein/Ntotal = 5.33.
3. Protein has many roles in your body. It helps repair and build your body's tissues, allows metabolic
reactions to take place and coordinates bodily functions. In addition to providing your body with a
structural framework, proteins also maintain proper pH and fluid balance.

P0ST-TEST
1. D
2. A
3. B
4. C
5. E

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