Anda di halaman 1dari 2

Introduction

It is well known that helices and -sheets are the major stabilizing structures in proteins. Segments of the protein chain which are not helical nor sheet have been generally designated as random coil or irregular regions. These nonrepetitive motif elements include tight turns, bulges, and random coil structures (Richardson, 1981).

Tight Turns
There are different types of tight turns (Chou 2000) depending upon the number of atoms forming the turn. These are as follows: Delta-turn - It is the smallest tight turn which involves only two amino acid residues and the intraturn hydrogen bond for a delta-turn is formed between the backbone NH(i) and the backbone CO(i+1). Gamma-turn - It involves three amino acid residues and the intraturn hydrogen bond for a gamma-turn is formed between the backbone CO(i) and the backbone NH(i+2). Beta-turn - A beta-turn involves four amino acid residues and may or may not be stabilized by the intraturn hydrogen bond between the backbone CO(i) and the backbone NH(i+3). Alpha-turn - An alpha-turn involves five amino acid residues where the distance between the Calpha(i) and the Calpha(i+4) is less than 7 and the pentapeptide chain is not in a helical conformation. Pi-turn - It is the largest tight turn which involves six amino acid residues.

-turn
A -turn is a region of the protein involving four consecutive residues where the polypeptide chain folds back on itself by nearly 180 degrees (Lewis et al. 1971, 1973; Kuntz,1972; Crawford et al.,1973; Chou & Fasman ,1974). It is these chain reversals which give a protein its globularity rather than linearity. The -turn was originally identified, in model building studies, by Venkatachalam (1968). He proposed three distinct conformations based on phi,psi values (designated I,II and III) along with their related turns (mirror images) which have the phi, psi signs reversed (I',II' and III'), each of which could form a hydrogen bond between the main chain C=O(i) and the N-H(i+3). Subsequently, Lewis et al. (1973) examined the growing number of threedimensional protein structures and suggested a more general definition of a -turn. This stated that the distance between the C alpha(i) and the C alpha (i+3) was <7 and the residues involved were not helical. They found that 25% of their extended -turns did not possess the intraturn hydrogen bond suggested by Venkatachalam. To include the new data they extended the classification of -turns to 10 distinct types (I,I',II,II',III,III',IV,V,VI and VII). These classes were defined not only by phi,psi angles, but also less stringent criteria. Richardson (1981) has since reappraised the situation, and has suggested that there are only 6 distinct types (I,I',II,II',VIa and VIb) based on phi,psi ranges, along with a miscellaneous category IV. The Richardson classification is the system most widely used at present. Two main types of -turns are Type-I and Type-II with their mirror images I' and II'. Two types of -turns (Type-I and Type-II) A -turn consists of four consecutive residues defined by positions i, i+1, i+2, i+3 which are not present in alpha-helix; the distance between Calpha(i) and Calpha(i+3) is less than 7 (Richardson 1981;Rose et al. 1985) and the turn leads to reversal in the protein chain. -turns may or may not be accompained by the NH(i+3)-CO(i) hydrogen bond connecting the main chain atoms; CO of the ith residue and NH of (i+3)rd residue in the turn (Lewis et al 1973; Nemethy and Scheraga 1980).

Significane & Role in protein folding


Turns play an important role in globular proteins from both structural and functional points of view. A polypeptide chain cannot fold into a compact structure without the component of turns. Also, turns usually occur on the exposed surface of proteins and hence probably represent antigenic sites or involve molecular recognition. Thus, owing to the above reasons, the prediction of -turns in proteins is an important element of secondary structure prediction. Two hypotheses have been proposed for the role of turns in protein folding. In one view, turns play a critical role in folding by bringing together and enabling or allowing interactions between regular secondary structure elements. This view is supported by mutagenesis studies indicating a critical role for particular residues in the turns of some proteins. Also, nonnative isomers of X-Pro peptide bonds in turns can completely block the conformational folding of some proteins. In the opposing view, turns play a passive role in folding. This view is supported by the poor amino-acid conservation observed in most turns. Also, non-native isomers of many X-Pro peptide bonds in turns have little or no effect on folding.

Mold
Definition: Mold is a fungi that contains multiple identical nuclei. It grows in the form of hyphae of filaments. Mold has a fuzzy appearance and can be an orange, green, black, brown, pink or purple in color. Some molds are used in food production, for example,

Yeast
A type of fungi that contains only a single cell.

Appearance:

White and thready

Uses:

Ethanol production, baking,

Mold
Penicillium is used in the production of cheese, Neurospora in the production of oncom, which is made from the by-product of tofu. Energy Production: Secrete hydrolytic enzymes that degrade biopolymers such as starch, cellulose and lignin into simpler substances that can be absorbed. Can cause allergic reactions and respiratory problems

Yeast
vitaminsupplements, study of cell cycle.

Convert carbohydrates to alcohol and carbon dioxide in anaerobic through fermentation. Also obtain carbon from hexose sugars. Can cause infection in individuals with compromised immune systems. Very common. Can be found on fruit and berries, in the stomachs of mammals and on skin, among other places. 1500 known species 1% of all fungi. Most reproduce asexually through mitosis. Most common form called budding.

Health Hazards:

Habitat:

Typically found in damp, dark or steam-filled areas.

Species: Reproduction:

1000s of known species, including penicillium. Reproduce through small spores, which can be either sexual or asexual.

What type of tests determine bacteriostatic or bactericidal activity?

Answer:
Case History: Determining the _Effectiveness of a Food Preservative Background In order to determine whether a newly synthesized chemical might be a useful food preservative, the chemical was tested for its ability to inhibit bacterial growth. Control 500 ml of cottage cheese was inoculated with 2 ml of a 24-hr culture of Pseudomonas aeruginosa and incubated at 25C. Five hours after inoculation, a standard plate count showed there were 200 bacterial cells/ml in the cottage cheese. After 29 hours at 25C, there were 1,000,000 cells/ml in the cottage cheese. Experiment 500 ml of cottage cheese containing the preservative was inoculated with 2 ml of a 24-hr culture of P. aeruginosa. After 6 hours of incubation at 25C, a standard plate count was performed. There were 700 bacterial cells/ml in the cottage cheese. After 38 hours, there were 61,000,000 bacterial cells/ml in the cottage cheese. Number Log 1 0.00 2 0.30 5 0.70 6 0.78 24 1.38 32 1.51 200 2.30 700 2.85 1.00 x 106 6.00 6.10 x 106 6.79 6.10 x 107 7.79 Questions Does this type of test determine bacteriostatic or bactericidal activity? This would be determined by examination of the graph and comparing the ploted growth of the control and test data. However the wording of the Aim "its ability to inhibit bacterial growth" suggests were are looking for a bacteriostatic effect. The graph for a bacteriostatic preservative would show a slower gradient in log phase compared to the control as the bacteria struggle to reproduce. A graph for a bactericidal preservative would show a longer lag phase as initally many of the bacteria are killed which is equivelent to innoculating the culture with a lower number of bacteria.

Anda mungkin juga menyukai