I started lifting a couple of years ago. Having minimal knowledge of programmes, I started off with full body workouts as advised by the gym owner.
I would do the core lifts (Squats, Bench Press, OHP, BB rows & DL) 3x per week for 2 weeks before moving on to Stronglifts 5x5. SL5x5 worked relatively well for me. I made progress (newbie gains) in terms of strength and body composition.
Throughout these years, I've never been one to stick with gym. Reasons for such varies from succumbing to injury due to poor form to losing motivation because I didn't get results like those in '90 day transformation' videos.
Attempting to emulate their results, I changed my diet drastically. I would cut out all high calorie foods (nasi lemak, fried chicken etc.) and eat a clean high protein diet (oats, porridge, steamed chicken). Like you would have guessed, I did not manage to maintain the new diet. In a year, my weight would fluctuate between 10-20 kg because of this.
Looking back, the only way I would succeed (enjoy gym) was if I achieved all of the following;
-I manage to increase the weight for all my lifts every session (expecting linear progress)
-I eat clean
-I enjoy eating clean
-the scale would show that I'm losing 1kg / week
I was setting myself up for failure. Some of the above are truly unrealistic/unhealthy goals.
Having said that, I've decided to make some changes and give it another shot. This will be my 4th attempt this year (2017). I've lost count of the number of times I've started and slacked off over the years.
This time, I'll start smaller and instead of focusing on the result at the end of 90 days, I'll
I feel good whenever I:
Steps; Show up for gym OR
Steps; Am on track with my macros OR
Steps; Learn something new related to Health and Fitness OR
Steps; Notice physical improvements OR
Micro goals; Increase my lifts by 1.25kg/side OR
Macro goals; Increase plates on lifts
"Trade your expectations for appreciation and your world changes instantly"
~TR
I was on;
[S1-S35]
StrongLifts 5x5 (15 Dec, 2017-16 Mar, 2018)
"Getting strong and getting big aren't mutually exclusive"
I used SL's App to track progress.
SL 5x5 Progress
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5x5 Squats:
50kg-97.5kg
5x5 Bench
35kg-60kg
5x5 OHP
20kg-32.5kg
5x5 Rows
35kg-55kg
1x5 DL
60kg-95kg
Timeline
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Squats 5x5
50kg 19 Dec
55kg 23 Dec
60kg 27 Dec
65kg 31 Dec, 2017
70kg 05 Jan
75kg 09 Jan
80kg 31 Jan
85kg 13 Feb
90kg 18 Feb
95kg 27 Feb
97.5kg 01 Mar, 2018
Bench 5x5
35kg 17 Dec
40kg 29 Dec, 2017
45kg 07 Jan
50kg 27 Jan
55kg 05 Feb
60kg 27 Feb, 2018
OHP 5x5
20kg 19 Dec
25kg 27 Dec, 2017
30kg 09 Jan
32.5kg 01 Mar, 2018
Rows 5x5
35kg 17 Dec
40kg 29 Dec, 2017
45kg 07 Jan
50kg 27 Jan
55kg 05 Feb, 2018
Deadlift 1x5
60kg 19 Dec
65kg 27 Dec
70kg 31 Dec, 2017
75kg 05 Jan
80kg 09 Jan
85kg 25 Jan
95kg 09 Mar, 2018
I am now on;
5/3/1 for Beginners by Jim Wendler.
I’m using 531 Strength to track progress.
Useful reads & links
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Layne Norton
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Protein Balance
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Net protein balance = muscle protein synthesis - muscle protein breakdown.
Inhibition of muscle protein degradation impairs muscle protein synthesis. 7 our of 8 AA used to synthesise new proteins comes from degraded protein.
Both MPS & MPB increases when we eat protein (assuming sufficient quantity & quality). MPS>MPB.
To build muscle rate of MPS> rate of MPB.
Protein Synthesis
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DNA contain instructions needed for an organism to develop, survive and reproduce. DNA's instructions are used to make proteins in a two-step process.
First, enzymes read the information in a DNA molecule and transcribe it into an intermediary molecule called messenger ribonucleic acid, or mRNA.
Next, the information contained in the mRNA molecule is translated into the "language" of amino acids, which are the building blocks of proteins. This language tells the cell's protein (ribosome) the precise order in which to link the amino acids to produce a specific protein. There are 20 types of amino acids, which placed in different orders form different proteins. Most hormones are proteins. Insulin for example is a protein.
New muscle protein is synthesised by a process called Muscle Protein Synthesise (MPS). The limiting factor of protein synthesis is not the amount of amino acids delivered to a transfer RNA, but initiation of translation (on surface of ribosome).
Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy. Insulin is a positive regulator of mTOR. Insulin signals mTOR mediated by AKT. Insulin does not increase MPS in humans.
AMPK is a negative regulator of mTOR. AMPK regulates energy balance at cellular and whole body levels.
In a caloric deficit, ATP decreases, AMP increases, activity of AMPK increases which inhibits mTOR. Therefore, being in a caloric deficit is typically not anabolic.
Leucine seems to be the most potent nutritional regulator of mTOR. Increased concentrations of leucine signals mTOR that sufficient dietary protein exists, and switches on overall protein synthesis. Leucine increases activity of mTOR. However, only taking leucine to increase MPS is not practical as other amino acids are needed in the synthesis of proteins by the ribosome and this will be the bottleneck of MPS. In a high protein diet, other amino acids are not the limiting factor in MPS but supplementary intake of leucine is debatable. However, it is notable that leucine is a muscle recovery agent.
mTOR phosphorylates eIF4B. Typically, eIF4B binds with eIF4E which decreases the availability of eIF4E to bind with eIF4G. Phosphorylation of eIF4B takes away the inhibition of eIF4E to bind with eIF4G. eIF4E is now free to bind with eIF4G. When eIF4E binds with eIF4G, production of eIF4F increases which leads to increase of ribosomal attachment to mRNA, increase in translation and thus increase in muscle protein synthesis. Phosphorylation of EIF4B is the rate limiting step.
mTOR also activates ribosomal protein p70S6K. p70S6K increases production of specific proteins involved in the process of MPS. Capacity of MPS is increased by this protein.
The genetic limit of a person as to how much muscle he can carry may be described by the ‘myonuclear domain’ theory where it is limited by the number of satellite cells that is available to fuse as myonuclei. The myonuclear number is governed by two opposing mechanisms: the gain of myonuclei by the fusion of muscle stem cells/satellite cells into hypertrophying muscle fibers and the loss of myonuclei by apoptosis/necrosis in atrophying muscle fibers.
Energy Balance; Calories in, Calories out
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'By definition if you're not losing weight, you're not on a caloric deficit diet'
Calories in>Calories out = Weight gain
Calories out>Calories in = Weight loss
Calories in = Food intake
Calories out = BMR + NEAT + EA + TEF
Food intake (very very modifiable)
BMR (not very modifiable)
NEAT (very modifiable)
EA (very modifiable)
TEF (slightly modifiable)
TEF
Protein ~30%
Carbs ~6-8%
Fats ~2-3%
Fibre ~30%
Food labels may have errors up to 10-20%; calories & macros
Protein is harder to be stored as fats. Calories from proteins most likely creates a caloric cushion for carbs and fats to be stored as fats.
On a long term caloric deficit BMR, NEAT, EA and TEF may decrease.
Reduced LBM and fat mass may decrease BMR. Plus metabolic adaptations also reduce BMR
NEAT may reduce up to 500kcals
EA decreases as body becomes more efficient in performing an activity assuming all things constant
TEF may decrease over time as the body becomes more adept in extracting calories
Therefore, maintenance calories can change over time. Solution is either to decrease caloric intake or increase EA.
Fat Metabolism
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Most of the fat in the human diet is in the form of triacylglycerol (TAG); three fatty acids linked to glycerol. Our fat stores are also TAG. In the digestive tract, TAG is hydrolyzed by the enzyme pancreatic lipase, to release free fatty acids and monoglycerides.
The main issue in the digestion and absorption of fats is one of solubility: lipids are hydrophobic, and thus are poorly soluble in the aqueous environment of the digestive tract. Pancreatic lipase is water soluble and can only work at the surface of fat globules. Emulsification greatly increases the surface area of TAG to be acted upon by pancreatic lipase.
Emulsification is the process of breaking up large fat globules into smaller emulsion droplets. This is aided by the action of bile (containing phospholipids and bile salt where both are amphipathic).Motility in the small intestine breaks fat globules apart and prevents reassociation with the aid of bile.
Another factor that aids digestion is colipase. Colipase, a protein and also amphipathic in nature, anchors pancreatic lipase to the surface of emulsion droplets where TAG are hydrolysed to FFA and monoglycerides.
Next, FFA and monoglycerides associate with phospholipids and bile salts to form micelles. Micelles act as transport vehicles to move FFA and monoglycerides to the surface of enterocytes (intestinal lining) where they are absorbed. Only freely dissolved monoglycerides and fatty acids can be absorbed, not the micelles.
Once inside the enterocyte, monoglycerides and fatty acids are re-synthesized into TAG. The TAG is then packaged, along with cholesterol and fat soluble vitamins, into chylomicrons. Chylomicrons are lipoproteins designed to transport lipids. Chylomicrons are too large to enter capillaries but flow into general circulation (bloodstream) via lymphatic system (via lacteals).
Chylomicrons deliver TAG to our cells. To be absorbed by cells (e.g. fat cells, muscle cells), TAG in chylomicrons together with other lipoproteins are first hydrolysed to FFA and monoglycerides.
Usually when rates of fat oxidation is high, rates of gluconeogenesis is also high. Glycerol is transported to the liver to be repackaged into glucose. Fatty acids on the hand are repackaged into fat cells.
In a High Fat, Low Carb diet assuming Caloric Surplus;
Insulin is low
Fat oxidation is high (used as fuel source)
Fat storage is high
Insulin is not required to store body fat
Assuming fat oxidation is high, the body will spare blood glucose and glycogen. Muscle glycogen is usually depleted during high intensity physical activity.
More fat is stored rather than oxidised because of being in a positive energy balance
In a Low Fat, High Carb diet assuming Caloric Deficit;
Insulin is high
Fax oxidation is low
Fat storage is low
Carbs can be stored as fats via a process call de novo lipogenesis. However, fat storage via this pathway is minuscule unless on a very high carb, very low fat diet.
Less fat is stored rather than oxidised because of being in a negative energy balance
Calorie Partitioning
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Ways to increase fat loss
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QUOTE(mikehuan @ Jul 26 2013, 11:32 AM)
How to choose a good protein supplement
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QUOTE(darklight79 @ Jun 19 2014, 05:46 PM)
Original article by Daniel H from Sports Nutrition
Amino spiking!? How can I be sure my whey protein is quality??
Okay firstly I want to say something which is probably a little bit contradictory to the point of this whole discussion - but generally protein shakes don't differ a lot from each other. It all comes down to clever marketing.
Men's is marketed at gaining lean muscle, and has big muscular men on the advertising. Women's is marketed as 'slim' etc, and has petite and thin women in the advertising. Basically the product is exactly the same, men's just comes in larger packaging and with larger serving sizes. Yeah some contain blends of soy or pea proteins etc etc, but mostly are all milk based, and contain whey or casein protein.
ALRIGHT!! Here comes the tricky part.... Dan’s science lesson about protein. Tips and lessons to know what to avoid, and which proteins are quality. I hate it how companies label protein. Commonly the first ingredient will be some kind of protein matrix, which is bracketed, and combines all the different types of protein and aminos. Now this gives the impression as it is the first listed ingredient that it will be abundant in BCAA. However, sometimes this can be as littled as a couple of hundred mg!! Taurine is a common added 'amino'. Taurine is similar to an amino acid, but it slightly differs as it is not used for protein synthesis. One of the few known naturally occurring sulfonic acids; in the strict sense, it is not an amino acid, as it lacks a carboxyl group the molecule does not have the amino acid structure. Taurine is often referred to as a “nonessential” amino acid, or more generously as a “conditionally essential” amino acid.
Taurine is a derivative of cysteine and is DID YOU READ THAT!?! IS NOT USED FOR PROTEIN SYNTHESIS. SO WHY IS IT IN MY PROTEIN??
AMINO SPIKING. Heard of it?? Probably not. It’s when companies add cheap amino acids to their protein formulas because substances such as glycine and taurine cost manufacturers half as much as a pure whey product would, saving them money. So these tricky guys in the marketing department will say thngs like for "time release" or "enhanced amino profile" to justify their bullshit protein ‘blend’. I’ve seen products that contain around 10 grams of protein from whey, and then all this glycine/taurine/ alanine /creatine/amino matrix bullshit to bring it up to 23 grams or so of ‘proteins’. Have you ever read an article about the awesome performance enhancing qualities of glycine? Or its properties as a muscle-builder of fat-burner? Nope. That’s because it’s not even an essential amino acid. OUR BODY PRODUCES IT NATURALLY!!
So why would we want to supplement it?? Or even dilute our precious whey?? Because it’s cheap and it makes the product look like it’s 23 grams (or whatever) of whey protein when it’s really 18 grams plus five grams of a worthless amino.
Protein synthesis – essential amino acid levels
If a diet is inadequate in any essential amino acid, protein synthesis cannot proceed beyond the rate at which that amino acid is available. This is called a limiting amino acid. A good interpretation of a limiting amino acid is thinking of a barrel of liquid. The amino acids are the individual pieces of plank making up the barrel. If one plank (amino acid) is shorter than the others (limiting), the barrel can only be filled to the level of the shortest plank. This shortage of one of the essential amino acids will reduce growth rate and performance. On the other hand, when a diet is balanced for the most limiting amino acid – for example another protein source is added, other amino acids are usually in excess of one’s requirements.
Protein Digestibility Corrected Amino Acid Score (PDCAAS) is a method of evaluating the protein quality based on both the amino acid requirements of humans and their ability to digest it. The PDCAAS rating was adopted by the US Food and Drug Administration (FDA) and the Food and Agricultural Organization of the United Nations/World Health Organization (FAO/WHO) in 1993 as "the preferred 'best'" method to determine protein quality. Whey protein is one of four foods (egg white, soy protein & casein) with a PDCAA of 1.
This means the body can readily use the whole protein source. When the profile of the amino acids is changed, the PDCAAS value of the protein is reduced, therefore less amino acids are absorbed and readily used by the body. If the natural EAA profile of whey is changed, i.e. cheap aminos added, then more of the shake must be consumed to receive optimum EAA levels. This questions the logic of supplementing BCAA such as Leucine with a Whey shake to make it ‘more anabolic’. Adding leucine to a whey protein drink doesn't stimulate any additional muscle protein synthesis, according to research on whey: "Our results indicate that the whey protein plus leucine in healthy young volunteers results in an anabolic response in muscle that is not greater than the previously reported response to whey protein alone."
Determining protein content: Nitrogen content & combined amino acids weight
There is no official Association of Analytical Communities (AOAC) method for amino acid determination in foods. A standardized method with support for collaborative research and scientific consensus are needed in order to bring this about For many years, the protein content of foods has been determined on the basis of total nitrogen content (determined by Kjeldahl or Dumas method) multiplied by a specific factor. This method has been around for over 100 years. Nitrogen content is then multiplied by a factor to arrive at protein content. This approach is based on two assumptions: that dietary carbohydrates and fats do not contain nitrogen, and that nearly all of the nitrogen in the diet is present as amino acids in proteins. Although more expensive, it is considered more accurate to base protein content of foods on amino acid data. A study on the nutrient composition of beef analysed the full amino-acid profile of fifteen retail cuts from three age groups and six fat codes, as well as determined total nitrogen content to determine proximate protein composition. On average, the sum of amino acids per cut amounted to 91% of total determined protein for the same cut. The amount of protein in a food is calculated through the sum of individual amino acid residues (the molecular weight of each amino acid less the molecular weight of water) plus free amino acids. In this method, food composition tables should reflect protein by sum of amino acids. Because proteins are made up of chains of amino acids joined by peptide bonds, they can be hydrolysed to their component amino acids, which can then be measured by ion-exchange, gas-liquid or high-performance liquid chromatography.
The sum of the amino acids then represents the protein content (by weight) of the food. This is sometimes referred to as a “true protein” or “complete protein”. When a manufacturer submits their protein product to most analytical chemistry labs around the country, the labs determine the total nitrogen content to calculate the protein content. However, they're unable to differentiate the nitrogen found in protein from the nitrogen found in non-protein sources! Not only do these aminos and nitrogen-containing compounds (like creatine) show up as “protein”, they register as 110% & 143% protein! This means for every gram of glycine, it registers as 1.1 grams of protein... If you have read this far, I hope you are still with me!! okay, I have attached two images, one has a good protein profile, basically protein, plus carbs, plus fat = serving sizes. Contains no amino blends, or added singular amino acids. The second profile, carbs plus fat plus protein still leaves a bunch of grams leftover. FILLERS!! also when you look at the ingredients list, it contains an amino blend, and has added taurine/glycine.. BAD!!
So basically if you want a good protein, read the label. You want around 30 serve [not 40!] to have around 23-27 grams of protein [depending on concentrate or isolate] with 2-4 grams carbs and fat combined.
Check the ingredients to check there's no cheeky taurine or glycine in there
Cheers!
DeAct
This post has been edited by DeAct: Mar 24 2018, 08:57 AM