The a-helix (right handed)-saccharide used as gelling agent in many foods. The most commons source of this polysaccharide is seaweedthe most abundant sugar i. The consequence is that they are all the maximum distance apart.tt
The a-helix is a common feature of many proteins. Much of myoglobin consists of this structure. Note the hydrogen bonds maintaining the structure and linking the CO of the nth residue and NH of the (n+4)th residue. The core of the a-helix is tightly packed.))))))))))))f molecular mass in the millions
Haemoglobin S (HbS) is a mutant form of haemoglobin where a surface glutamate is replaced by a valine. The valine is then able to bind to a hyrophobic pocket on another molecule of HbS. This video shows two HbS molecules linked by the valine residue (yellow). The haem groups are shown in red.
Biotin - Streptavidin complex
ose - open chain form
a-Helix (right handed))
a-Helix
Bacteriorhodopsin is a light-activated proton pump found in Halobacterium halobium. This video illustrates the conformational change which occurs when light interacts with bacteriorhodopsin. Initially the model shows cis retinal bound and after illumination the all-trans retinal is shown, with a shift in retinal binding.arranged in an equatorial manner. The consequence is that they are all the maximum distance apart..
Biotin is an essential human nutrient. It functions as a carbon dioxide carrier. Biotin forms very stable complexes with avidin and streptavidin. Biotin deficiency results from consumption of raw eggs which are rich in avidin. The role of the avidin in eggs is to serve as a bacteriostatic agent.......ain conformation and the result is that both alpha and beta anomer of the ring form are possibleximum distance apart..
Porin is a pore-forming membrane protein. Much of the periphery of the protein consists of hydrophobic residues in contact with the membrane lipid. The pore is lined with hydrophilic amino acids with acidic residues shown in red and basic residues shown in blue...he parts of the which forms a po..
Silk fibroin is produced by insects and spiders. It consists of long repeating stretches of the sequence Gly-Ser-Gly-Ala-Gly-Ala. These chains form antiparallel b-pleated sheets with the Gly's on one face and the Ala's and Ser's on the other. The sheets stack with like faces associating together.un parallel to the axis of the silk fibre and The Glys
Metallothioneins are metal ion binding proteins. They bind to cadmium, copper and zinc. The metal ion binding ability is a function of the clusters of cysteine sulphydryl groups that they possess. The video shows the chelation of a metal ion by such a cluster of cysteines.
Collagen
cose - open chain form
Porin
eenan
Myoglobin is a muscle protein which binds oxygen and facilitates its transport in actively respiring tissue. The oxygen molecule is bound to the haem group which is located in a hydrophobic pocket. Myoglobin has seven a-helices. A histidine residue binds to the haem iron atom.nd the haem.all of the hydroxyl groups are arranged in an equatorial manner. The consequence is that they are all the maximum distance apart..
Collagen is the most abundant vertebrate protein. It forms strong, insoluble fibres and is a stress-bearing component of connective tissues. Collagen is a rope-like triple helix of repeating Gly-X-Y sequences, around 1000 amino acids long. Proline and hydroxyproline are also major constituents..nts..s.en.s of collagen. the result is that both alpha and beta anomer of the ring form are possibleximum distance apart..
The a-helix (right handed)-saccharide used as gelling agent in many foods. The most commons source of this polysaccharide is seaweedthe most abundant sugar i. The consequence is that they are all the maximum distance apart.tt
The a-helix is a common feature of many proteins. Much of myoglobin consists of this structure. Note the hydrogen bonds maintaining the structure and linking the CO of the nth residue and NH of the (n+4)th residue. The core of the a-helix is tightly packed.))))))))))))f molecular mass in the millions
Haemoglobin S (HbS) is a mutant form of haemoglobin where a surface glutamate is replaced by a valine. The valine is then able to bind to a hyrophobic pocket on another molecule of HbS. This video shows two HbS molecules linked by the valine residue (yellow). The haem groups are shown in red.
Biotin - Streptavidin complex
ose - open chain form
d)Helix (right handed))
a-Helix
Bacteriorhodopsin is a light-activated proton pump found in Halobacterium halobium. This video illustrates the conformational change which occurs when light interacts with bacteriorhodopsin. Initially the model shows cis retinal bound and after illumination the all-trans retinal is shown, with a shift in retinal binding.arranged in an equatorial manner. The consequence is that they are all the maximum distance apart..
Biotin is an essential human nutrient. It functions as a carbon dioxide carrier. Biotin forms very stable complexes with avidin and streptavidin. Biotin deficiency results from consumption of raw eggs which are rich in avidin. The role of the avidin in eggs is to serve as a bacteriostatic agent.......ain conformation and the result is that both alpha and beta anomer of the ring form are possibleximum distance apart..
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