The amino acid L-proline is considered to be inessential because human beings and other animals can biosynthesize it, generally from another inessential amino acid L-glutamic acid. Proline is uncommon because it is heterocyclic, and hence is the only natural amino acid which contains a secondary amine group. Just the L-enantiomer is found in nature.

Proline also is uncommon because it was synthesized before it was isolated from natural sources. In 1900, chemistry Nobel Reward– winning German chemist Richard M. Willstätter prepared the D,L-racemate from N-methylproline. The list below year, Emil Fischer, another German Nobel laureate, isolated the L-form from egg albumen and hydrolyzed casein.

Proline, like natural amino acids, is utilized for biosynthesizing proteins. The stiff five-membered ring in proline gives proteins made from it significantly various secondary structures from proteins made from open-chain proteins.

In 2002, Mohammed Movassaghi and Eric N. Jacobsen at Harvard University presented the notion that proline is the “simplest enzyme”. At that time, numerous scientists were utilizing proline as an uneven catalyst as though it was a new thing; earlier work using proline had been overshadowed by the arrival of metal-based asymmetric catalysts. Movassaghi and Jacobsen declared that it was about time for chemists to recognize that asymmetry could be accomplished with easy compounds and without the use of metals.

A couple of years later, Eric Smith of the Santa Fe Institute and coauthors elaborated on the simplest enzyme idea. They argued that “small molecule catalysis is a finding of utmost value for the origin of biochemistry”. To put it simply, small molecules, and not large, intricate enzymes, were the only catalysts offered to promote prebiotic development. [2]


L-Proline is a significant amino acid discovered in cartilage and is necessary for maintaining youthful skin in addition to repair work of muscle, connective tissue and skin damage. It is likewise essential for the body immune system, and for required balance of this formula. It is a vital component of collagen and is necessary for appropriate functioning of joints and tendons. L-Proline is extremely important for the appropriate functioning of joints and tendons. Assists maintain and strengthen heart muscles.

System of action

Glycogenic, by L-Proline oxidase in the kidney, it is ring-opened and is oxidized to form L-Glutamic acid. L-Ornithine and L-Glutamic acid are converted to L-Proline via L-Glutamic acid-gamma-semialdehyde. It is contained generously in collagen, and is totally associated with the function of arthrosis and chordae. [3]


Proline is biosynthetically originated from the amino acid L-glutamate. Glutamate-5-semialdehyde is first formed by glutamate 5-kinase (ATP-dependent) and glutamate-5-semialdehyde dehydrogenase (which needs NADH or NADPH). This can then either spontaneously cyclize to form 1-pyrroline-5-carboxylic acid, which is minimized to proline by pyrroline-5-carboxylate reductase (utilizing NADH or NADPH), or developed into ornithine by ornithine aminotransferase, followed by cyclisation by ornithine cyclodeaminase to form proline.

Biological activity

L-Proline has been discovered to function as a weak agonist of the glycine receptor and of both NMDA and non-NMDA (AMPA/kainate) ionotropic glutamate receptors. It has been proposed to be a prospective endogenous excitotoxin. In plants, proline build-up is a typical physiological reaction to different tensions however is likewise part of the developmental program in generative tissues (e.g. Pollen). A diet rich in proline was connected to an increased risk of anxiety in humans.

Residence in protein structure

The distinct cyclic structure of proline’s side chain offers proline a remarkable conformational rigidness compared to other amino acids. It also impacts the rate of peptide bond development in between proline and other amino acids. When proline is bound as an amide in a peptide bond, its nitrogen is not bound to any hydrogen, indicating it can not act as a hydrogen bond donor, however can be a hydrogen bond acceptor.

Peptide bond formation with incoming Pro-trnapro is substantially slower than with any other trnas, which is a basic feature of N-alkylamino acids. Peptide bond development is also sluggish in between an inbound trna and a chain ending in proline; with the production of proline-proline bonds slowest of all.

The remarkable conformational rigidity of proline affects the secondary structure of proteins near a proline residue and may represent proline’s greater frequency in the proteins of thermophilic organisms. Protein secondary structure can be explained in regards to the dihedral angles φ, ψ and ω of the protein foundation. The cyclic structure of proline’s side chain locks the angle φ at around − 65 °.

Proline functions as a structural disruptor in the middle of regular secondary structure aspects such as alpha helices and beta sheets; however, proline is commonly discovered as the first residue of an alpha helix and likewise in the edge strands of beta sheets. Proline is likewise typically discovered in turns (another sort of secondary structure), and help in the development of beta turns. This may account for the curious reality that proline is usually solvent-exposed, in spite of having a totally aliphatic side chain.

Several prolines and/or hydroxyprolines in a row can produce a polyproline helix, the predominant secondary structure in collagen. The hydroxylation of proline by prolyl hydroxylase (or other additions of electron-withdrawing substituents such as fluorine) increases the conformational stability of collagen considerably. For this reason, the hydroxylation of proline is a vital biochemical procedure for keeping the connective tissue of higher organisms. Severe diseases such as scurvy can arise from problems in this hydroxylation, e.g., anomalies in the enzyme prolyl hydroxylase or lack of the essential ascorbate (vitamin C) cofactor.

Cis-trans isomerization

Peptide bonds to proline, and to other N-substituted amino acids (such as sarcosine), are able to populate both the cis and trans isomers. A lot of peptide bonds overwhelmingly embrace the trans isomer (generally 99.9% under unstrained conditions), mainly because the amide hydrogen (trans isomer) provides less steric repulsion to the preceding Cα atom than does the following Cα atom (cis isomer). By contrast, the cis and trans isomers of the X-Pro peptide bond (where X represents any amino acid) both experience steric clashes with the surrounding alternative and have a much lower energy distinction. Hence, the portion of X-Pro peptide bonds in the cis isomer under unstrained conditions is substantially raised, with cis fractions usually in the range of 3-10%. Nevertheless, these worths depend on the preceding amino acid, with Gly and fragrant residues yielding increased fractions of the cis isomer. Cis portions up to 40% have actually been identified for Aromatic-Pro peptide bonds.

From a kinetic perspective, cis-trans proline isomerization is a really sluggish process that can impede the development of protein folding by trapping several proline residues important for folding in the non-native isomer, particularly when the native protein requires the cis isomer. This is because proline residues are specifically synthesized in the ribosome as the trans isomer kind. All organisms have prolyl isomerase enzymes to catalyze this isomerization, and some germs have specialized prolyl isomerases related to the ribosome. However, not all prolines are vital for folding, and protein folding might proceed at a normal rate despite having non-native conformers of lots of X-Pro peptide bonds.


Proline is among the two amino acids that do not follow together with the normal Ramachandran plot, together with glycine. Due to the ring formation connected to the beta carbon, the ψ and φ angles about the peptide bond have less allowable degrees of rotation. As a result, it is frequently found in “turns” of proteins as its complimentary entropy (ΔS) is not as comparatively big to other amino acids and therefore in a folded form vs. Unfolded kind, the modification in entropy is smaller. In addition, proline is seldom found in α and β structures as it would decrease the stability of such structures, because its side chain α-N can just form one nitrogen bond.

Furthermore, proline is the only amino acid that does not form a red/purple colour when established by spraying with ninhydrin for uses in chromatography. Proline, rather, produces an orange/yellow colour. [4]

Proline metabolic process

Proline synthesis

Proline synthesis from glutamine, glutamate, arginine, and ornithine in animals is cell-, tissue-, and species-specific. All mammals can manufacture proline from arginine by means of arginase (both type I and type II), ornithine aminotransferase, and P5C reductase, with the mammary tissue, small intestine (postweaning animals), liver, and kidneys being quantitatively the most active tissues. In mammary tissue, the major products of arginine catabolism are proline, ornithine, and urea. Because proline oxidase activity is missing from mammary tissue, there is no deterioration of arginine-derived proline in the lactating gland. This guarantees maximal net production of proline from arginine by the breast feeding mammary gland. Due to the fact that P5C synthase is likewise missing from mammary tissue, there is no development of proline from glutamine or glutamate by this tissue. Hence, arginase plays a crucial function in proline synthesis by lactating mammary tissue. Surprisingly, the activity of P5C reductase is at least 50-fold greater than that of P5C dehydrogenase in breast feeding mammary tissue, thus preferring the conversion of arginine-derived P5C into proline rather than into glutamate and glutamine. The synthesis of proline from arginine assists to prevent a permanent loss of arginine carbons in nursing porcine mammary tissue. These findings likewise supply a biochemical description for the observation that the output of proline in sow’s milk significantly exceeds the uptake of plasma proline by the breast feeding mammary gland, whereas the output of arginine in sow’s milk is much lower than the uptake of plasma arginine by the breast feeding mammary gland. Because of substantial catabolism of arginine for proline synthesis via the arginase path and the absence of proline catabolism in lactating porcine mammary tissue, there is a relative enrichment of proline but a relative shortage of arginine in milk proteins.

The small intestine of postweaning pigs deteriorates approximately 40% of arginine in the enteral diet, with proline being a major item. Furthermore, both glutamate and glutamine in the enteral diet plan are nearly totally deteriorated by the small intestine, with proline being a substantial item. In the postabsorptive state, one-third of glutamine in arterial blood is extracted by the pig small intestine. Products of glutamate and glutamine deterioration in enterocytes consist of not just proline but likewise ornithine, citrulline, arginine, and alanine. Studies with jejunum-cannulated young pigs showed net release of proline from the small intestine of food-deprived piglets. De novo synthesis and the hydrolysis of small peptides in enterocytes and the digestive tract lumen might be sources of this gut-derived proline. Glucocorticoids are significant hormonal agents that manage proline synthesis from arginine and glutamine in cells and tissues.

In contrast to mammals, birds have low arginase activity in tissues and, for that reason, a restricted ability to transform arginine into proline. For that reason, proline is a nutritionally important AA for avian species, consisting of chickens. In addition, carnivores (e.g., felines and ferrets) do not have P5C synthase in enterocytes and other cell types, and can not convert glutamine and glutamate into proline in the body. Hence, arginine is the only substrate for proline synthesis in these types. Owing to a high need for dietary arginine for multiple synthetic procedures and the lack of its endogenous synthesis, arginine is a nutritionally important AA for carnivores. Dietary supplements with proline may make up for some arginine in these animals due to an inhibition of arginase by proline-derived ornithine.

Proline destruction

Except for mammary tissue, most tissues express proline oxidase activity. A by-product of this mitochondrial enzyme is superoxide anion (O2 −), which can be converted into H2O2 and other reactive oxygen species. In tissues and cells (e.g., porcine placenta and enterocytes of neonatal pigs) that do not include arginase activity, proline is the only substrate for the synthesis of ornithine and, therefore, polyamines (putrescine, spermidine, and spermine). This is of enormous significance in both nutrition and physiology because (1) polyamines are key particles managing DNA and protein synthesis, in addition to cell proliferation, distinction, and migration; (2) both placentae and neonatal small intestine grow very rapidly. In ruminants, placentae consist of both arginase and proline oxidase, which helps to compensate for fairly low concentrations of proline in maternal blood.

Although all cells can recycle P5C into proline by P5C reductase and transform P5C into ornithine by ornithine aminotransferase, the utilization of P5C for the synthesis of citrulline is highly cell- and tissue-specific. Of particular note, just mammalian enterocytes are capable of manufacturing citrulline from P5C, suggesting an unique function for the small intestine in proline metabolic process. Although the mammalian liver can transform P5C into ornithine by means of the urea cycle, there is no net synthesis of arginine in this organ due to the fact that exceptionally high arginase activity quickly hydrolyzes arginine into ornithine and urea (Wu and Morris 1998). In liver and kidneys, P5C can be oxidized entirely to CO2 via the formation of α-ketoglutarate by P5C dehydrogenase. Nevertheless, in placentae and enterocytes with limited P5C dehydrogenase activity, oxidation of proline to CO2 is minimal. This prevents a permanent loss of proline carbons and takes full advantage of the accessibility of P5C for the synthesis of polyamines. Engaging proof reveals that polyamines play an essential function in intestinal development, function, and health throughout the neonatal duration.

Because the whole particle of P5C is included into citrulline by means of ornithine aminotransferase and ornithine carbamoyltransferase in enterocytes, proline supplies its nitrogen and carbon skeleton for citrulline and arginine synthesis in the small intestine which reveals these 2 enzymes and P5C synthase. An absence of knowledge or misconception of these basic biochemical reactions can lead scientists to make erroneous conclusions regarding the contribution of proline carbons to endogenous synthesis of arginine. Such errors, which have actually just recently occurred with glutamine studies, will surely not advance the field of mammalian arginine metabolic process but rather will lead to much deceptive confusion in literature. [5]

What are the Health Benefits of Proline?

Maintains Skin Health and Fixes Wounds

Collagen makes up skin and connective tissue. Proline is an important part of collagen. Without proline (or actually, without collagen) injuries would not recover due to the fact that the body would not have the ability to reconstruct skin when you get injured. Also, your skin would droop due to the fact that there ‘d be absolutely nothing to hold it in place. Connective tissue links things together. Everything breaks down without it. Consuming enough amino acids to make collagen, especially proline, hydroxyproline, and glycine, helps keep skin firm, healthy, and looking youthful.

Supports Digestion Function

Proline may help treat leaky gut syndrome by strengthening the gut lining. Leaking gut happens when tiny holes open up in the gut lining, permitting pathogens to get in. This sets off swelling. Amino acids, consisting of proline, are required to rebuild any damaged intestinal tract cells, keeping the lining intact. Proline likewise helps in reducing inflammation and enhance immune function in the digestion system. A common recommendation for attempting to heal dripping gut is to take bone broth regularly, partly due to its high proline content.

Lowers Danger of Heart Disease

Cardiovascular disease stays the leading cause of death in the US. Fatty build-ups in the artery walls trigger cardiovascular disease and strokes due to blockage. This avoids the blood from streaming through. However, proline helps launch some of this stuck fat, helping get rid of the blockage. This sends it back into the blood stream for usage somewhere else. Proline might help in reducing the danger of a cardiac arrest.

Decreases Inflammation and Helps Manage Tension

Proline assists lower inflammation, which promotes a healthy body immune system. It also helps set off a cascade of anti-inflammatory compounds and genes that assist with healing from ecological stress (5 ). Proline aids in more effective energy production, enabling us to much better handle tension. Moreover, it repair work DNA damaged by oxidative tension and promotes liver detoxification. All of these functions result in an improved body immune system and lower swelling. This reduces overall danger of illness, making you feel your finest.

Reinforces Joints and Other Connective Tissue

Because proline belongs to collagen, it is required to fix connective tissue of all kinds. Connective tissue assists hold your bones in place and acts like a shock absorber. Ask anybody without connective tissue in a knee to tell you how uncomfortable life is without it! Bones grinding versus bones– no thanks!

Proline assists preserve and repair connective tissue. You need it to make another amino acid called hydroxylysine, among the primary components of collagen, tendons, and muscle.

We naturally produce less collagen with age, and joints begin to weaken over time. This is exacerbated by bad diet, stress to the joints, and being overweight. Consuming more amino acids that assist form collagen may help support the development of brand-new connective tissue, cartilage, and even strengthen bones. Proline assists lower swelling, which preserves joint movement and function and minimizes discomfort associated with aging.

Proline Food Sources

Since proline is an amino acid, you’ll find it in high protein foods, particularly those high in collagen. Usually, animal foods with collagen consist of those with connective tissue. For instance, a whole chicken (with bones and skin) includes more collagen than a chicken breast with bones and skin eliminated.

People nowadays often choose boneless, skinless meat (a downer for upping proline). To get some, add collagen sources to your diet. No recommended everyday requirement for proline exists. “Non-essential” amino acids are discovered in many foods. If you consume any sort of food with protein (even vegetarian sources) you more than likely fulfill your needs.

The foods greatest in proline consist of:

  • Bone Broth
  • Gelatin
  • Organ meats, like liver
  • Collagen supplements
  • L-proline supplements
  • Beef
  • Chicken
  • Wild-caught fish
  • Eggs [6]

It is found in greatest concentrations in natural sources of collagen. The very best sources of proline and collagen in the diet plan are bone broth and other high-protein foods, specifically animal items, such as organ meats like liver, grass-fed beef, pasture-raised chicken, wild-caught fish and eggshell membranes.

When you consume animals “nose to tail,” you take in proline and collagen from parts of the animal, including the bones, connective tissue and muscle tissue.

Focused collagen protein powder and gelatin are two other fantastic sources of proline. Collagen powder is made from sources consisting of chicken collagen, bovine/beef collagen, eggshell membrane collagen and fish collagen. Gelatin is a kind of hydrolyzed beef collagen, which implies it’s basically a part of broken-down collagen that is primarily utilized in desserts or food production because it creates a gel-like texture.

Utilizing bone broth or collagen powders/supplements can really can be found in handy since these save you loads of time and effort. For instance, slow-cooked bone broth is made over the course of one to two days, however when you use focused bone broth protein powder you can get the benefits of bone broth practically instantly.

Chicken collagen consists of glycine, glutamine and proline, plus chondroitin and glucosamine, two substances that assist rebuild cartilage. You can take in some by eating chicken prepared on the bone with its skin or by making chicken broth, soup, stew and other tasty recipes with a range of animal parts (organs, bones, and so on).

You can also get percentages of proline from consuming fish collagen, such as by eating pieces of fish which contain small bones, tissues or scales, or by making fish stock/broth, soup and stew (such as with fish heads).

Another source is yokes of cage-free eggs. A fantastic way to up your proline/collagen consumption is to include some collagen powder to scrambled eggs or a omelette.

Is proline discovered in plants? Yes, although eating plant foods like vegetables or fruits will not provide you with extremely high quantity. In plants elements, such as pollen, proline build-up is really an action to physiological stresses and also involved in structure development.

Proline vs. Glycine vs. Lysine

What is various about proline compared to other amino acids?

Around one-third of collagen is composed of glycine. Glycine is an amino acid that’s necessary for various muscle, cognitive and metabolic functions. It is among the primary amino acids used to form collagen and gelatin. The best sources of glycine are similar to proline sources, such as bone broth, collagen protein powder and other protein foods.

Of one glycine’s functions includes helping break down and transportation nutrients like glycogen and fat to be utilized by cells for energy. It’s called an “anti-aging amino acid” because of how it assists maintain lean muscle mass and promotes the secretion of human development hormonal agent. Glycine is used to deal with lots of health conditions, such as muscle wasting (scaropenia), ulcers, arthritis, leaking gut syndrome, diabetes, kidney and cardiac arrest, neurobehavioral conditions, and tiredness.

Lysine (or l-lysine) is an important amino acid that is found in protein foods like meat, beans, cheeses and eggs, as well as readily available in supplement type. Like proline, L-lysine aids in the development and upkeep of bones and connective tissue by assisting kind to collagen. It is also very crucial in the creation of carnitine, which transforms fats into energy.

L-lysine may help repair the gastrointestinal system, lower cholesterol levels and be handy for taking in calcium, which secures against blood clots and other problems.

Other benefits credited to l-lysine consist of dealing with cold sores, stress and anxiety, diarrhea and even the development of cancer. The very best dietary sources of L-lysine are beef, chicken, turkey, fish like tuna, white beans, pumpkin seeds and eggs.

Arginine is another amino acid discovered in collagen. It is discovered in protein foods, including beef and other kinds of red meat, poultry, fish, eggs and dairy products. Arginine may provide benefits for heart health, exercise efficiency, mental abilities and far more.

How to Get Proline in Your Diet Plan + Recipes

1. Consume Bone Broth

To consume more proline, it’s perfect to consume real bone broth practically daily, which likewise supplies many other nutrients beyond just amino acids. Bone broth is among the absolute best ways not just to get more collagen into your diet plan, but also trace minerals, electrolytes, and useful substances like chondroitin sulfate, glucosamine sulfate and hyaluronic acid.

For the most advantages, objective to have about 8 to 16 ounces of bone broth per day. You can make your own homemade bone broth utilizing traditional recipes that take one to 2 days or by consuming dried or powdered bone broth/bone broth protein. Bone broth can be taken in by itself, contributed to shakes or healthy smoothies, or utilized it in all sorts of sweet and savory recipes, such as marinades, stews, or even shakes and smoothies.

2. Take Collagen Powder/Collagen Supplements

You can likewise utilize collagen protein in healthy smoothies, shakes or other dishes. I recommend a multi-collagen powder which contains a number of collagen types, such as types 1, 2, 3, 5 and 10. Each type of collagen has unique functions and benefits, so it’s finest to supplement with more than one type.

Collagen is unsavory, odor free and simple to mix into all kinds of recipes– plus it’s gluten-free, dairy-free, nut-free and soy-free. Include some to baked recipes like muffins, bars or pancakes to increase the protein material. You can likewise utilize collagen powder just like gelatin to thicken healthy smoothies, desserts or recipes that have a gel-like texture. Constantly ensure to buy a collagen powder that is stemmed from grass-fed or pasture-raised, healthy animals (preferably that are naturally raised).

3. Eat Enough Protein and an Overall Healthy Diet

You’ll get the most gain from consuming proline and other amino acids discovered in collagen if you consume a nutrient-dense diet that includes plenty of protein and great deals of anti-oxidants. This is practical for preserving higher collagen levels and preventing collagen deterioration since it decreases inflammation and totally free radical damage (also called oxidative tension).

You can enhance the amount of proline you absorb and use by consuming foods that function as “collagen cofactors,” such as plenty of fresh vegetables, fresh fruits, fresh herbs and spices; various sources of “tidy” protein; and foods high in vitamin C, vitamin A, copper and iron. [7]

Possible Adverse Effects of L-Proline

A naturally taking place amino acid that your body produces by itself, L-proline may be taken in extra kind to decrease the accumulation of arterial deposits and lower the danger of heart disease. In addition, this amino acid may likewise assist your body develop collagen, which is a main structural tissue in connective tissue. L-proline supplements have no recognized negative effects.

Why Take Proline

Your body currently produces enough of the amino acid proline, so it appears unneeded to take it supplementally. Having an abundance of this amino acid, a foundation of protein, in your system, though, can improve the health of your joints, the look of your skin and effectiveness of your body immune system. L-proline is readily available in meat, dairy and eggs; if your diet plan is low in these protein sources, you might have trouble producing optimal levels of this amino acid. Some people also have a problem metabolizing, and thus utilizing, L-proline; vitamin C deficiency can cause this challenge.

Your body currently produces enough of the amino acid proline, so it appears unnecessary to take it supplementally.

L-proline is easily offered in meat, dairy and eggs; if your diet plan is low in these protein sources, you may have difficulty producing optimum levels of this amino acid.

Just how much

Difficult research study supporting using proline supplements to improve complexion and joint vitality is doing not have. Leon Chaitow, in the book “Amino Acids for Therapy,” took a look at the role of proline in the conversion to hydroxyproline, a foundation of collagen. He recommends that supplements might assist with soft tissue pressure, injury healing, hypermobile joints and the drooping skin associated with aging. Chaitow recommends taking between 500 and 1,000 milligrams daily, along with additional vitamin C.

Difficult research supporting using proline supplements to enhance skin tone and joint vigor is lacking.

Leon Chaitow, in the book “Amino Acids for Treatment,” examined the function of proline in the conversion to hydroxyproline, a foundation of collagen.

Protein Waste

Too much proline can give you a raised amino-acid consumption. This causes your body to develop protein waste that need to be expelled by the liver and, especially, the kidneys– putting a lot of stress on these organs. Many people can handle the extra amino acids, but if you have liver or kidney disease, speak with your medical professional prior to adding any additional amino acid to your diet plan. [8]

Unique Preventative Measures and Cautions

When taken by mouth: Proline is LIKELY SAFE when taken by mouth in food quantities. There isn’t enough trustworthy details to know if proline is safe when utilized in larger quantities as medicine or what the adverse effects might be.

When applied to the skin: There isn’t enough dependable info to know if proline is safe or what the negative effects might be. Pregnancy and breast-feeding: There isn’t sufficient reputable details to know if proline is safe to utilize when pregnant or breast-feeding. Remain on the safe side and stay with the amounts discovered in foods.

Kids: Proline is LIKELY SAFE when taken by mouth in food amounts.


We presently have no info for PROLINE Interactions. [9]

The Bottom Line

We say amino, and scientists say “imino.” But in any case, L-proline is an active chemical in the body. It interacts with other amino acids and vitamin C to form collagen that assists develop tissues, and it’s constantly on the alert for body repair work. Capillary, digestive tract lining, joints and skin are all target areas that take advantage of proline.

The just known side effects are responses from taking excessive L-proline, like all amino acids. It triggers toxicity levels and amino acid imbalances in your body. Talk with your medical practitioner about taking any amino acid if you have kidney or liver illness.

Your body efficiently makes proline when an individual’s diet includes adequate-protein, and vitamin C facilitates its absorption. Conditions such as arteriosclerosis, joint discomfort, leaking gut, skin issues and requiring sports routines may gain from a proline increase.

Drinking bone broth, including protein-packed foods or taking a supplement are all methods to guarantee you are getting enough. Whichever method you get it, proline seems to be a vital piece of the body’s puzzle. [10]


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