Proteins: Molecular Wonders in Three Dimensions

Author(s):  
Eugene H. Cordes

I grew up in a solid middle-class family, largely of German descent, in a city of modest size in central Nebraska. Like a lot of such families, our diet was based on meat and potatoes. It was an unwritten but religiously observed law in our home that two meals each day would include both meat and potatoes. The meat was turkey twice a year, ham on occasion, chicken or pork from time to time, but mostly beef. The potatoes were usually boiled or boiled potatoes subsequently sliced and fried. My brother and I also drank a lot of whole milk, at least a quart a day each and frequently more (skim milk was available, but no one gave much thought to “reduced fat” or “low fat” milk back in those days). On farms, a lot of people just drank what the cows had on tap. Between the meat, potatoes, and the whole milk, we got a lot of protein in our diet, which is good; we also got a lot of saturated fat in our diet and that is not so good. Adequate protein in our diet is essential for good health. Proteins in our diet break down to provide essential amino acids. Amino acids are the building blocks of proteins. The amino acids that are essential in our diet are those that our bodies cannot make or cannot make in adequate quantity for optimal health. For dietary proteins, two things matter: amount and quality. The amount of protein is a simple quantitative matter; it is measured in grams per day. The amount you need depends on several factors: your gender, age, size, level of exercise and other physical activity, and whether you are pregnant or lactating, for example. The quality of protein is not so easy to evaluate. Getting the essential amino acids in your diet is more important than getting the others. The highest quality proteins are those that contain an abundance of all the essential amino acids. Meats and dairy products are among the best sources of high-quality proteins.

1978 ◽  
Vol 29 (1) ◽  
pp. 145 ◽  
Author(s):  
H Dove

Jugular blood samples were obtained from 10.5 kg and 28 kg lambs receiving a diet of reconstituted cows' whole milk. The lambs were then given diets in which the proportion of essential amino acids (BAA) in the dietary crude protein was altered over a wide range. A second blood sample was taken after lambs had received such diets for 12 days. Plasma obtained from these samples was analysed for free amino acids, urea and ammonia. The pattern of plasma free amino acids (PFAA) in lambs given reconstituted cows' whole milk is described. In both the pre-treatment and post-treatment samples, the heavier lambs appeared to have lower plasma levels of all EAA, and high plasma levels of glycine, serine, urea and ammonia. In the lighter lambs, there were pronounced responses of PFAA levels to changes in the dietary proportion of EAA. At low proportions, the levels of most EAA in plasma were low. Lysine and phenylalanine were exceptions. In addition, levels of many non-essential amino acids (non-EAA), particularly serine and glycine, were high. At high proportions of EAA, plasma levels of all EAA, especially methionine, rose markedly. Within the non-EAA, serine, proline and glycine were reduced, while taurine and cystathionine increased. In the plasma of the heavier lambs, the response of some amino acids to a given dietary change differed from the response in the lighter lambs. This was especially true of methionine, tyrosine, phenylalanine and arginine. There was also marked between-animal variation in plasma levels. When expressed as molar proportions of total PFAA, results were similar to those of the lighter lambs. There was a pronounced similarity between the response of the PFAA to diets with a low proportion of EAA, and the PFAA pattern characteristic of developing kwashiorkor. __________________ *Part II, Aust. J. Agric. Res., 28, 933 (1977).


2019 ◽  
Vol 9 (1) ◽  

Protein structure is a hot topic, not only to the specialist, but with others like the physicists. So this review is targeting those who are not biologists and have to deal with the protein in their research. In this review we travel with the protein structures from the amino acids and its classifications, and how the polypeptide chain is formed from these building blocks up to the final 3D structure. We introduced the secondary structure species like helices with its different types and how it is formed; also the beta sheet formation and types are explained briefly. Finally the tertiary and quaternary structures are presented. The approaches of molecular modeling as well as other important computational methods present significant contribution to studying proteins.


1979 ◽  
Vol 41 (2) ◽  
pp. 311-319 ◽  
Author(s):  
A. P. Williams ◽  
D. Hewitt

1. Ten calves (50–58 kg live weight) were given a diet consisting of diluted whole milk, wheat gluten and supplemented with appropriate nutrients including amino acids but deficient in lysine. The lysine requirements of these calves, which were growing at approximately 0.25 kg/d, were estimated from responses to lysine supplementation of this diet. From plasma urea, plasma lysine, nitrogen retention and apparent digestibility of N responses the estimated lysine requirements were 8.5, 7.5, 7.2 and 7.6 g/d respectively.2. From the mean lysine requirement (7.8 g/d) and the ratio, lysine: other essential amino acids in carcasses of similar calves the estimated requirements were (g/d): methionine 2.1, cystine 1.6, threonine 4.9, valine 4.8, isoleucine 3.4, leucine 8.4, tyrosine 3.0, phenylalanine 4.4, histidine 3.0, arginine 8.5, tryptophan 1.0.


1998 ◽  
Vol 61 (2) ◽  
pp. 235-239 ◽  
Author(s):  
LAURA PIZZOFERRATO ◽  
PAMELA MANZI ◽  
VITTORIO VIVANTI ◽  
ISABELLA NICOLETTI ◽  
CLAUDIO CORRADINI ◽  
...  

Chemical reactions occurring during industrial treatments or storage of foods can lead to the formation of ε-deoxyketosyl compounds, the Amadori products. Food protein value can be adversely affected by these reactions, and in particular lysine, an essential amino acid having on its side chain a free amino group, can be converted to nonbioavailable N-substituted lysine or blocked lysine. By acid hydrolysis of ε-deoxyketosyl compounds, furosine is formed. In this paper furosine prepared from milk-based commercial products has been evaluated by use of a recently developed HPLC method using a microbore column and phosphate buffer as the mobile phase at controlled temperature. Furosine levels have been used, together with protein, total amino acids, and lysine content, as an estimate of protein quality of a few different products such as cooked-cream dessert, yogurt mousse, white chocolate, milk chocolate, milk chocolate with a soft nougat and caramel center, milk chocolate with a whipped white center, chocolate spread, part-skim milk tablets, milk-based dietetic meals, and baby foods. The protein content of the analyzed products ranged from 34.3 g · kg−1 (milk nougat) to 188.4 g · kg−1 (milk tablets). The Maillard reaction caused a loss in available lysine that varied from 2.5% (cooked cream) to 36.2% (condensed milk). The contribution to the lysine average daily requirement is heavily affected by this reaction and varied from 13% (milk tablets and soft nougat) to 61% (dietetic meal). Variable results were also obtained for the other essential amino acids.


1983 ◽  
Vol 50 (2) ◽  
pp. 383-390 ◽  
Author(s):  
Kyu-Il Kim ◽  
Henry S. Bayley

1. Piglets were weaned at 3 d of age and were introduced to liquid diets in which 400 g/kg protein was supplied as skim-milk powder and the balance as a mixture of free amino acids. The skim milk contributed 2·3 g methionine and 1·4 g cystine/kg diet; the experimental diets were made by supplementing these levels with free amino acids.2. The adequacy of the test level of the amino acid in the diet was assessed by measuring the oxidation of [1−14]phenylalanine as an indicator of the partition of the essential amino acids between incorporation into protein and degradation. Radioactivity recovered as carbon dioxide was used as a measure of catabolism.3. Addition of 0·2, 0·4, 0·7, 1·2 and 1·7 g L-methione/kg to a diet containing 5 g cystine and 3 g choline chloride/kg showed that phenylalanine catabolism was minimal for the diet with 2·7 g methionine/kg indicating that this is the dietary requirement for methionine to serve as a source of methionine residues for protein synthesis.4. Addition of D-methionine to produce a series of diets with graded levels of methionine showed that the D-isomer was less effective than the L-isomer in reducing phenylalanine catabolism: the addition of 0·8 g D-methionine/kg diet was needed to produce the same effect as 0·4 g L-methionine/kg diet showing that the replacement value of D-methionine for L-methionine was 50% in the young pig.5. To investigate the influence of cystine on methionine requirement, diets with varying levels of methionine and cystine were prepared. Oxidation of [U-14C]methionine was used as an indication of an excess of methionine, and the results showed that increasing the dietary methionine level above 3·0 g/kg in diets containing 1·4 g cystine/kg provided an excess of methionine for oxidation. This indicated a sulphur amino acid requirement of 4·4 g/kg, one-third of this being supplied as cystine.


1992 ◽  
Vol 43 (6) ◽  
pp. 1353 ◽  
Author(s):  
PJ Reis ◽  
DA Tunks ◽  
SG Munro

The relative importance for wool growth of energy-yielding nutrients compared with amino acids required for incorporation into wool proteins was assessed in an experiment in which most nutrients were supplied via the abomasum. Nine nutritional treatments, providing three levels of protein (53, 99 and 145 g/day) to the intestines at three levels of energy (5.2, 7.5 and 9.7 MJ/day), were given to 12 Merino sheep during three consecutive periods of 3 weeks in a balanced lattice design. Abomasal nutrients consisted of varying proportions of casein, whole milk, glucose and glycerol. There was a large effect of protein supply on all components of wool growth, but there was no significant effect of energy. There was a significant interaction between the effects of protein and energy supply on diameter, length growth rate and volume of wool, but it was small relative to the main effect of protein. Extra energy appeared to enhance wool growth at the highest level of protein but reduce it at the lowest level of protein. The concentration of urea, cystine, methionine and other essential amino acids in plasma increased with protein level. Increasing energy supply reduced the concentration of urea and essential amino acids in plasma but not that of cystine or methionine. The experiment confirmed the major role of amino acid supply in controlling wool growth but indicated that there may be a small interaction with energy supply.


2021 ◽  
Author(s):  
Sarah L Gautrey ◽  
Mirre J P Simons

Dietary restriction (DR) is one of the most potent ways to extend health- and lifespan. Key progress in understanding the mechanisms of DR, and ageing more generally, was made when dietary protein, and more specifically essential amino acids (EAA), were identified as the key dietary component to restrict to obtain DRs health and lifespan benefits. This role of dietary amino acids has strongly influenced work on ageing mechanisms, especially in nutrient sensing, e.g. Tor and insulin(-like) signalling networks. Experimental biology in Drosophila melanogaster has been instrumental in generating and confirming the now dominant hypothesis that EAA availability is central to ageing. Here, we expand on previous work testing the involvement of EAA in DR through large scale (N=6,238) supplementation experiments across four diets and two genotypes in female flies. Surprisingly, we find that EAA are not essential to DRs lifespan benefits. Importantly, we do identify the fecundity benefits of EAA supplementation suggesting the supplemented EAA were bioavailable. Furthermore, we find that the effects of amino acids on lifespan vary by diet and genetic line studied and that at our most restricted diet fecundity is constrained by other nutrients than EAA. We suggest that DR for optimal health is a concert of nutritional effects, orchestrated by genetic, diet and environmental interactions. Our results question the universal importance of amino acid availability in the biology of ageing and DR.


2018 ◽  
Vol 19 (1) ◽  
pp. 47-57 ◽  
Author(s):  
Carla Maris Machado Bittar ◽  
Jackeline Thais da Silva ◽  
Hugh Chester-Jones

SUMMARY Other than crude protein (CP), crude energy (CE) and crude fiber (CF) content, the adequate supply of essential amino acids (EAA) is an important factor in milk replacer evaluation. The aim of this study was to analyze milk replacer samples as regard to nutrients, especially EAA, composition and simulate the attainability of calves' requirements in different feeding systems. Forty-one milk replacer samples were collected from 14 brands and analyzed for nutrient composition. The near infrared spectroscopy technique was used for AA content estimation. Samples presented adequate levels of CP (21.2±2.90%) and ether extract (14.5±3.41%) for calves fed according to the conventional (4L/d), but not for intensive milk feeding system (>6L/d). High values of CF were observed in the samples (1.6±0.86%). The EAA composition of milk replacer samples was lower than expected for a liquid feed supposed to replace whole milk. None of the analyzed samples presented adequate lysine (5.72±1.09% CP) or methionine (1.65±0.38% CP) to meet calves' daily requirements, regardless of feeding system. Higher crude protein milk replacers are needed. Alternatively, supplementation of milk replacers with EAA is recommended.


Author(s):  
Helen Carrasco Hope ◽  
Robert J. Salmond

AbstractT cell activation, differentiation and proliferation is dependent upon and intrinsically linked to a capacity to modulate and adapt cellular metabolism. Antigen-induced activation stimulates a transcriptional programme that results in metabolic reprogramming, enabling T cells to fuel anabolic metabolic pathways and provide the nutrients to sustain proliferation and effector responses. Amino acids are key nutrients for T cells and have essential roles as building blocks for protein synthesis as well as in numerous metabolic pathways. In this review, we discuss the roles for uptake and biosynthesis of non-essential amino acids in T cell metabolism, activation and effector function. Furthermore, we highlight the effects of amino acid metabolism and depletion by cancer cells on T cell anti-tumour function and discuss approaches to modulate and improve T cell metabolism for improved anti-tumour function in these nutrient-depleted microenvironments.


1983 ◽  
Vol 49 (3) ◽  
pp. 343-354 ◽  
Author(s):  
R. F. Hurrell ◽  
P. A. Finot ◽  
J. E. Ford

1. Whole-milk powders containing 25 g water/kg were stored for up to 9 weeks in sealed aluminium containers at elevated temperatures. Lysine and other essential amino acids were measured by chemical and microbiological methods.2. Storage at 60° resulted in the progressive formation of lactulosyl-lysine. After 9 weeks, 30% of the lysine groups were present in this form. The powders still retained their natural colour and the levels of tryptophan, methionine, cyst(e)ine and leucine remained unchanged.3. Storage at 70° resulted in the formation of lactulosyl-lysine followed by its complete degradation with the development of browning. Available tryptophan, methione, leucine and isoleucine decreased progressively during storage.4. The different methods for lysine determination gave widely dissimilar results. The direct fluorodinitrobenzene (FDNB) technique and reactive lysine from furosine were considered to be the most reliable methods. The FDNB-difference, dye-binding lysine, Tetrahymena and Pediococcus methods all seriously underestimated reactive or available lysine in heat-damaged milk powders. Tetrahymena and Pediococcus appeared to utilize lactulosyl-lysine as a source of lysine.5. The results are discussed in relation to storage and distribution of milk powders in hot climates.


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