First, lets learn about collagen and gelatin. The more you know the better so I compiled a little crash course from various sources and hope this will help others understand it on another level.
collagen;
collagen is made from 3 amino acids, proline, glycine, hydroxyproline
Proline: aids production in complex molecules
Proline (symbol Pro or P)[4] is a proteinogenic amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated NH2+ form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain pyrrolidine, classifying it as a nonpolar (at physiological pH), aliphatic amino acid. It is non-essential in humans, meaning the body can synthesize it from the non-essential amino acid L-glutamate. It is encoded by all the codons starting CC (CCU, CCC, CCA, and CCG).

Glycine: its basically the foundation for collagen
Glycine (symbol Gly or G;[4] /ˈɡlaɪsiːn/)[5] is an amino acid that has a single hydrogen atom as its side chain. It is the simplest amino acid, with the chemical formula NH2‐CH2‐COOH. Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). Glycine is integral to the formation of alpha-helices* in secondary protein structure due to its compact form. For the same reason, >>>it is most abundant amino acid in collagen triple-helices.<<< Glycine is also an inhibitory neurotransmitter - interference with its release within the spinal cord (such as during a Clostridium tetani infection) can cause spastic paralysis due to uninhibited muscle contraction.
*The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a right hand-helix conformation in which every backbone N−H group donates a hydrogen bond to the backbone C=O group of the amino acid located three or four residues earlier along the protein sequence.

Hydroxyproline: stabilizes collagen
Hydroxyproline is produced by hydroxylation of the amino acid proline by the enzyme prolyl hydroxylase following protein synthesis (as a post-translational modification). The enzyme catalyzed reaction takes place in the lumen of the endoplasmic reticulum. Although it is not directly incorporated into proteins, hydroxyproline comprises roughly 4% of all amino acids found in animal tissue, an amount greater than seven other amino acids that are translationally incorporated.[2]
Hydroxyproline is a major component of the protein collagen,[3] comprising roughly 13.5% of mammalian collagen. Hydroxyproline and proline play key roles for collagen stability.[4] They permit the sharp twisting of the collagen helix

There is a total of about 16 known collagen varieties. 90% of the collagen in the body consist of Type I, II, and III.
Type I: skin, tendon, vasculature, organs, bone-
Type I collagen is the most abundant collagen of the human body. It forms large, eosinophilic fibers known as collagen fibers. It is present in scar tissue, the end product when tissue heals by repair, as well as tendons, ligaments, the endomysium of myofibrils, the organic part of bone, the dermis, the dentin, and organ capsules. Type I collagen is a fibrillar type collagen, and most likely the best investigated collagen. Type I collagen is the most abundant collagen and is the key structural composition of several tissues. It is expressed in almost all connective tissues and the predominant component of the interstitial membrane. Type I collagen mutations have documented important roles in a range of diseases, with particular focus on bone and connective tissue disease, in particular osteogenesis imperfecta and Ehlers–Danlos syndrome. Type I collagen is predominantly modified at the posttranslational level, with several crosslinks and other modifications. Several biomarkers of type I collagen have been developed, of both type I collagen degradation and formation, as surrogate makers of bone degradation and formation, respectively. Type I collagen formation is also associated with fibrosis, and fibrogenesis.

Type II: cartilage collagen, hyaline cartilage
Type II collagen is a fibrillar* collagen, and the main component of cartilage. Type II collagen is the cartilage collagen; it constitutes 95% of the collagens and approximately 60% of dry weight. Mutations in type II collagen result in several types of chondrodysplasia, leading to premature osteoarthritis. Type II collagen is typically coassembled with collagen XI, where it is covalently crosslinked to collagen IX and interacts with small leucine-rich proteoglycans. Its stability and strength provide the tissue with integrity and resiliency to stress. Type II collagen cleavage is primarily mediated by collagenases of the matrix metalloproteinase family, resulting in well-described biomarkers such as C-terminal telopeptide of type II collagen and C2C. In addition, several formation makers have been developed. Type II collagen has important binding partners such as fibronectin and other collagens.

Type III: reticulate (main component of reticular fibers**), commonly found alongside type I
Type III collagen is a fibrillar collagen, and it consists of only one collagen α chain, in contrast to most other collagens. It is a homotrimer containing three α1(III) chains supercoiled around each other in a right-handed triple helix. Type III collagen is secreted by fibroblasts and other mesenchymal cell types, thus making it a major player in various inflammation-associated pathologies such as lung injury, viral and nonviral liver diseases, kidney fibrosis, hernia, and vascular disorders. Type III collagen together with type I collagen are the main constituents of the interstitial matrix. Type III collagen mutations are associated with Ehlers–Danlos syndrome, vascular deficiency, and aortic and arterial aneurysms. Several biomarkers for type III collagen formation and degradation have been developed and used extensively. In particular, for fibrosis, type III collagen formations have proven valuable.

Type IV: forms basal lamina, the epithelium-secreted layer of the basement membrane***
Type IV collagen is the main collagen component of the basement membrane. It is a network-forming collagen that underlies epithelial and endothelial cells and functions as a barrier between tissue compartments. Type IV collagen has many binding partners and forms the backbone of the basement membrane. It holds important signaling potential as subdomains such as tumstatin are released when the protein is degraded by special proteases. Consequently, type IV collagen is both the most important structural collagen of the basement membrane and it entails key signaling potential, which is important for various physiological and pathological functions. The most well-studied mutations in type IV collagen cause Alport syndrome, a chronic kidney disease. Several biomarkers of type IV collagen have been developed, both formation and degradation fragments as well as whole domains such as 7S, documenting the importance of type IV collagen turnover in most, if not all, connective tissue diseases.

Type V: cell surfaces(facia), hair, and placenta
Type V collagen is a fibrillar collagen. Type V collagen is essential for fibrillation** of types I and III collagen, and consequently for optimal fibrillary formation and tissue quality. Type V collagen contributes to the bone matrix; corneal stroma; and the interstitial matrix of muscles, liver, lungs, and placenta.

*Fibrils are structural biological materials found in nearly all living organisms. Not to be confused with fibers or filaments, fibrils tend to have diameters ranging from 10-100 nanometers. Fibrils are not usually found alone but rather are parts of greater hierarchical structures commonly found in biological systems. Fibrillation is an act or process of forming fibers or fibrils

**Reticular fibers, reticular fibres or reticulin is a type of fiber in connective tissue[1] composed of type III collagen secreted by reticular cells.[2] Reticular fibers crosslink to form a fine meshwork (reticulin). This network acts as a supporting mesh in soft tissues such as liver, bone marrow, and the tissues and organs of the lymphatic system.[3]

***The basement membrane is a thin, fibrous, extracellular matrix of tissue that separates the lining of an internal or external body surface from underlying connective tissue in metazoans.[1] This surface may be epithelium (skin, respiratory tract, gastrointestinal tract, etc.), mesothelium (pleural cavity, peritoneal cavity, pericardial cavity, etc.) and endothelium (blood vessels, lymph vessels, etc.)


>>Foods high in vitamin C and sulfur aid in the development of collagen as do some bone broths and collagen protein powders and supplements.<<


Gelatin-a vital source of collagen
Gelatin or gelatine (from Latin: gelatus meaning "stiff" or "frozen") is a translucent, colorless, flavorless food ingredient, derived from collagen taken from animal body parts. Brittle when dry and gummy when moist, it is also called hydrolyzed collagen, collagen hydrolysate, gelatine hydrolysate, hydrolyzed gelatine, and collagen peptides. It is commonly used as a gelling agent in food, medications, drug and vitamin capsules, photographic films and papers, and cosmetics.

Digestibility

The bioavailability of hydrolyzed collagen in mice was demonstrated in a 1999 study; orally administered 14C hydrolyzed collagen was digested and more than 90% absorbed within 6 hours, with measurable accumulation in cartilage and skin.[4] A 2005 study in humans found hydrolyzed collagen absorbed as small peptides in the blood.[5]
Effects on skin

Ingestion of hydrolyzed collagen may affect the skin by increasing the density of collagen fibrils and fibroblasts, thereby stimulating collagen production.[6] It has been suggested, based on mouse and in vitro studies, that hydrolyzed collagen peptides have chemotactic properties on fibroblasts[7] or an influence on growth of fibroblasts.[8]


Collagen Hydrolysate vs. Gelatin

Collagen hydrolysate (which is the same thing as hydrolyzed collagen) is not exactly the same thing as gelatin. In the hydrolyzed form, the collagen is processed more intensively, which actually breaks up the proteins into smaller pieces. They both have the same amino acids, but different chemical properties.

The benefits of collagen are mostly from the amino acids, and you break down both gelatin and hydrolyzed collagen into the same amino acids in your digestive system anyway, so in terms of health benefits, hydrolyzed collagen and gelatin should be roughly equivalent. But on the other hand, some people with may find the hydrosylate easier to digest, and they do have culinary differences in terms of how you’ll use them.

Tldr;
Gelatin is made out of collagen. As you know gelatin is made from animals(mostly, there are vegan substitutes), and animal bones and tissues ect are the easiest cheapest way to get a source of regular gelatin in your life. There is a lot of evidence to suggest that ingesting gelatin is more efficent for skin care(bones, tissue, ligaments organs ect as well) as it enters your bloodstream and your body can replace and heal more effectively for an inside out therapy. You don't have to throw away your creams, but think about diet too!

So after learning all of this I realize one of the best things to do is make a batch of the most bombin' soup broth. Chicken feet, if you can stomach it, are rich in collagens and cheap to throw in with a whole chicken. You can use any meat and bone really, chicken is just cheap. The more concentrated the better you can let is simmer low for a little over 24 hours as long as you check on it to make sure it isn't burning or getting too low on water. Can it up and store it in the fridge, drinking it is a great source of gelatin in itself, use it in recipes whatever you want with it. Boom, a cheap and delicious source of gelatin in your diet.