Why is Milk White?

Milk is mostly made up of water, with smaller amounts of fat, protein, minerals, and other compounds. Fats and water don’t usually mix, but in milk the fat and water form an emulsion. It is also a suspension of a multitude of different proteins in water.

The Chemistry of Milk - Click here for more.

In milk, proteins cluster together to form structures called micelles. These clusters grow from small clusters of calcium phosphate, which help hold them together. There are a number of different models of these micelles, with the exact structure still being subject to scrutiny.

It’s the protein micelles which give milk its white appearance. The micelles are on average about 150 nanometres in diameter, and this very small size means they are able to scatter light that hits them. The overall effect of this scattering by the huge number of micelles in milk is that it looks white.

For a fuller explanation and for more information please visit:-

http://www.compoundchem.com/2018/06/02/milk/

A guide to the twenty common amino acids

Have you ever thought about what makes up your body? Only 20 amino acids! Take a look at the graphic below, to discover the structure of each of these, plus information on the notation used to represent them.

Source: Compound Interest. Click to enlarge.

Amino acids are organic compounds containing amine (-NH2) and carboxyl (-COOH) functional groups, along with a side chain (R group) specific to each amino acid. The key elements of an amino acid are carbon, hydrogen, oxygen, and nitrogen, although other elements are found in the side chains of certain amino acids. About 500 amino acids are known and can be classified in many ways. They can be classified according to the core structural functional groups' locations as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, pH level, and side chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acid residues form the second-largest component (water is the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis.

In biochemistry, amino acids having both the amine and the carboxylic acid groups attached to the first (alpha-) carbon atom have particular importance. They are known as 2-, alpha-, or α-amino acids (generic formula H2NCHRCOOH in most cases, where R is an organic substituent known as a "side chain"); often the term "amino acid" is used to refer specifically to these. They include the 22 proteinogenic ("protein-building") amino acids, which combine into peptide chains ("polypeptides") to form the building-blocks of a vast array of proteins. These are all L-stereoisomers ("left-handed" isomers), although a few D-amino acids ("right-handed") occur in bacterial envelopes, as a neuromodulator (D-serine), and in some antibiotics. 

Twenty of the proteinogenic amino acids are encoded directly by triplet codons in the genetic code and are known as "standard" amino acids. The other two ("non-standard" or "non-canonical") are selenocysteine (present in many noneukaryotes as well as most eukaryotes, but not coded directly by DNA), and pyrrolysine (found only in some archea and one bacterium). Pyrrolysine and selenocysteine are encoded via variant codons; for example, selenocysteine is encoded by stop codon and SECIS element. N-formylmethionine (which is often the initial amino acid of proteins in bacteria, mitochondria, and chloroplasts) is generally considered as a form of methionine rather than as a separate proteinogenic amino acid. Codon–tRNA combinations not found in nature can also be used to "expand" the genetic code and create novel proteins known as alloproteins incorporating non-proteinogenic amino acids.

Many important proteinogenic and non-proteinogenic amino acids have biological functions. For example, in the human brain, glutamate (standard glutamic acid) and gamma-amino-butyric acid ("GABA", non-standard gamma-amino acid) are, respectively, the main excitatory and inhibitory neurotransmitters. Hydroxyproline, a major component of the connective tissue collagen, is synthesised from proline. Glycine is a biosynthetic precursor to porphyrins used in red blood cells. Carnitine is used in lipid transport.

Nine proteinogenic amino acids are called "essential" for humans because they cannot be created from other compounds by the human body and so must be taken in as food. Others may be conditionally essential for certain ages or medical conditions. Essential amino acids may also differ between species.

Because of their biological significance, amino acids are important in nutrition and are commonly used in nutritional supplements, fertilizers, and food technology. Industrial uses include the production of drugs, biodegradable plastics, and chiral catalysts.

For more information visit:-

http://www.compoundchem.com/2014/09/16/aminoacids/

https://en.wikipedia.org/wiki/Amino_acid

http://www.prlabs.co.uk/lab-supplies.php?N=l-arginine-for-biochemistry&Id=22533

Celebrating women in science on International Women’s Day: Dorothy Mary Hodgkin

Dorothy Mary Hodgkin OM FRS (12 May 1910 – 29 July 1994), known professionally as Dorothy Crowfoot Hodgkin or simply Dorothy Hodgkin, was a British biochemist who developed protein crystallography, for which she won the Nobel Prize in Chemistry in 1964.

She advanced the technique of X-ray crystallography, a method used to determine the three-dimensional structures of biomolecules. Among her most influential discoveries are the confirmation of the structure of penicillin that Ernst Boris Chain and Edward Abraham had previously surmised, demonstrating (contrary to scientific opinion at the time) that it contains a β-lactam ring. She also confirmed the structure of vitamin B12, for which she became the third woman to win the Nobel Prize in Chemistry.  In 1945, working with C. H. (Harry) Carlisle, she published the first such structure of a steroid, cholesteryl iodide (having worked with cholesteryls since the days of her doctoral studies). 

In 1948, Hodgkin first encountered vitamin B12 and created new crystals. Vitamin B12 had first been discovered by Merck earlier that year. Vitamin B12 had a structure at the time that was almost completely unknown, and when Hodgkin discovered it contained cobalt, she realized the structure actualization may be determined by x-ray crystallography analysis. The large size of the molecule, and that the atoms were largely unaccounted for - aside from cobalt - posed a challenge in structure analysis that hadn't been previously explored.

Molecular structure of vitamin B12, by NEUROtiker (Own work) [Public domain], via Wikimedia Commons

From these crystals, she deduced the presence of a ring structure because the crystals were pleochroic, a finding which she later confirmed using X-ray crystallography. The B12 study published by Hodgkin was described by Lawrence Bragg as being as significant "as breaking the sound barrier." Scientists from Merck had previously crystallised B12, but had published only refractive indices of the substance. The final structure of B12, for which Hodgkin was later awarded the Nobel Prize, was published in 1955.

In 1969, after 35 years of work and five years after winning the Nobel Prize, Hodgkin was able to decipher the structure of insulin. X-ray crystallography became a widely used tool and was critical in later determining the structures of many biological molecules where knowledge of structure is critical to an understanding of function. She is regarded as one of the pioneer scientists in the field of X-ray crystallography studies of biomolecules.

For more information visit:-

https://en.wikipedia.org/wiki/Dorothy_Hodgkin

http://www.prlabs.co.uk/lab-supplies.php?N=300l-msia-darts-protein-ag&Id=19593