Explain in a detailed way for a first year mbbs student

Reading File

Running Command

cd /tmp/workspace/attachments/255b0e7c-95de-4be9-8319-99e03f3c6a83/ && python3 -c " import pdfplumber files = [ 'Med1001 lecture 1.pdf', 'Med1001 Lecture 2.pdf', 'Med1001 Lecture 3..pdf' ] for fname in files: print(f'\n\n========== {fname} ==========\n') try: with pdfplumber.open(fname) as pdf: print(f'Pages: {len(pdf.pages)}') for i, page in enumerate(pdf.pages): text = page.extract_text() if text: print(f'--- Page {i+1} ---') print(text) except Exception as e: print(f'Error: {e}') "

analyse_media

Running Command

python3 -c " import pdfplumber from pypdf import PdfReader files = [ '/tmp/workspace/attachments/255b0e7c-95de-4be9-8319-99e03f3c6a83/Med1001 lecture 1.pdf', '/tmp/workspace/attachments/255b0e7c-95de-4be9-8319-99e03f3c6a83/Med1001 Lecture 2.pdf', '/tmp/workspace/attachments/255b0e7c-95de-4be9-8319-99e03f3c6a83/Med1001 Lecture 3..pdf' ] for fname in files: print(f'\n========== {fname.split(\"/\")[-1]} ==========') reader = PdfReader(fname) for i, page in enumerate(reader.pages): text = page.extract_text() if text and text.strip(): print(f'-- Page {i+1} --') print(text.strip()) else: # Try extracting words words = [] try: with pdfplumber.open(fname) as pdf: p = pdf.pages[i] words = p.extract_words() if words: print(f'-- Page {i+1} (words) --') print(' '.join([w[\"text\"] for w in words])) except: pass "

Running Command

python3 -c " import subprocess, sys # Check if pymupdf or pdf2image is available try: import fitz print('fitz (PyMuPDF) available:', fitz.__version__) except ImportError: print('fitz not available') try: from pdf2image import convert_from_path print('pdf2image available') except ImportError: print('pdf2image not available') try: from PIL import Image print('PIL available') except ImportError: print('PIL not available') "

Running Command

python3 -c " from pdf2image import convert_from_path import os base = '/tmp/workspace/attachments/255b0e7c-95de-4be9-8319-99e03f3c6a83/' out_base = '/tmp/workspace/pdf_images/' os.makedirs(out_base, exist_ok=True) files = { 'lec1': base + 'Med1001 lecture 1.pdf', 'lec2': base + 'Med1001 Lecture 2.pdf', 'lec3': base + 'Med1001 Lecture 3..pdf' } for key, fpath in files.items(): out_dir = out_base + key + '/' os.makedirs(out_dir, exist_ok=True) images = convert_from_path(fpath, dpi=150) print(f'{key}: {len(images)} pages') for i, img in enumerate(images): img.save(f'{out_dir}page_{i+1:02d}.jpg', 'JPEG', quality=75) print(f' Saved to {out_dir}') "

Running Command

python3 -c " from PIL import Image import os for lec in ['lec1', 'lec2', 'lec3']: folder = f'/tmp/workspace/pdf_images/{lec}/' pages = sorted([f for f in os.listdir(folder) if f.endswith('.jpg')]) imgs = [] for p in pages: img = Image.open(folder + p) # Resize to width 800 to keep filesize manageable ratio = 800 / img.width new_h = int(img.height * ratio) img = img.resize((800, new_h), Image.LANCZOS) imgs.append(img) # Stack vertically total_h = sum(img.height for img in imgs) + (len(imgs)-1)*4 combined = Image.new('RGB', (800, total_h), (200, 200, 200)) y = 0 for img in imgs: combined.paste(img, (0, y)) y += img.height + 4 out_path = f'/tmp/workspace/pdf_images/{lec}_combined.jpg' combined.save(out_path, 'JPEG', quality=70) size = os.path.getsize(out_path) print(f'{lec}: {len(imgs)} slides -> {out_path} ({size//1024} KB)') "

analyse_media

Loading Image

Reading File

Searching the Web

Med1001 molecular basis of cell biochemistry first year MBBS lecture topics water acids bases pH biomolecules

Reading Web Page

http://bauinternational.edu.ge/files/faculties/faculty-of-me…

Finding Sources

Reading File

Finding Sources

Reading File

Finding Sources

Reading File

Important note about your PDFs: All three lecture files are image-based slide decks (the text is embedded in images, not as selectable text). I was able to extract only the title from Lecture 1. I've used the BAU International Med 1001 course syllabus, your visible slide content, and the authoritative textbook Basic Medical Biochemistry: A Clinical Approach (6e) to give you the most accurate and complete explanation of what this course covers.

Med 1001: Molecular Basis of Cell - Biochemistry

Complete Study Notes for First-Year MBBS Students

Lecturer: MS Elene Bezhanidze | BAU International University

LECTURE 1 - Water, Acids, Bases, and pH

Why Should a Medical Student Care About This?

About 60% of your body is water, and every biochemical reaction in your body happens dissolved in it. The hydrogen ion concentration (acidity/alkalinity) of your blood must stay within a razor-thin range (pH 7.35-7.45). Go outside that range and your enzymes stop working, your heart rhythm fails, and you die. Learning water chemistry and acid-base balance is the foundation of understanding blood gas interpretation, IV fluid therapy, and dozens of clinical emergencies.

1. Water - Structure and Properties

The molecular structure:

Water (H₂O) has a bent shape. The oxygen atom is highly electronegative (pulls electrons toward itself), so:

The oxygen end carries a partial negative charge (δ-).
The two hydrogen ends carry partial positive charges (δ+).

This makes water a polar (dipolar) molecule - it has unequal charge distribution.

Hydrogen bonds:

Because of this polarity, water molecules attract each other: the δ+ hydrogen of one molecule attracts the δ- oxygen of a neighbouring molecule. This attraction is called a hydrogen bond.

Key facts about hydrogen bonds:

Strength: only ~4 kcal/mol (about 1/20th of a covalent bond)
Duration: each bond lasts only ~10 picoseconds (10 × 10⁻¹² seconds)
They break and re-form constantly - this is why water flows (liquidity)

Why polarity makes water the "universal solvent":

Polar and ionic substances dissolve in water because water molecules surround them:

Na⁺ (positive ion) → surrounded by the negative (oxygen) ends of water - called a hydration shell
Cl⁻ (negative ion) → surrounded by the positive (hydrogen) ends
Glucose, ATP, proteins → all polar → all dissolve easily in water

Non-polar substances (fats, oils) do NOT dissolve in water (hydrophobic = "water-fearing"). This is critical for the cell membrane - the lipid tails of phospholipids are hydrophobic, so they form the interior of the bilayer.

Water and temperature regulation:

High heat capacity: water absorbs a lot of heat without a large temperature rise - protects organs from temperature fluctuations
High heat of vaporization: evaporating sweat cools the body (skin cooling)
High thermal conductivity: heat from the brain and muscles is distributed via blood water throughout the body

Clinical example: In severe diabetic ketoacidosis (DKA), glucose and ketone bodies pour into the urine (osmotic diuresis). Water follows them out. This causes intracellular dehydration - brain cells shrink, leading to confusion and coma.

2. Body Water Compartments and Electrolytes

Total body water (~60% of body weight) is distributed into:

Compartment	% of body weight	Main cation	Main anion
Intracellular fluid (ICF) - inside cells	~40%	K⁺ (150 mmol/L)	HPO₄²⁻ (100 mmol/L)
Extracellular fluid (ECF) - outside cells	~20%	Na⁺ (145 mmol/L)	Cl⁻ (105 mmol/L)

ECF is further divided into plasma (in blood vessels) and interstitial fluid (between cells).
The unequal distribution of Na⁺ and K⁺ is maintained by the Na⁺/K⁺-ATPase pump, which uses ATP to pump 3 Na⁺ out and 2 K⁺ in for each cycle.
This gradient is what allows nerve impulses and muscle contraction.

3. The pH Scale

Water dissociates very slightly:

H₂O ⇌ H⁺ + OH⁻

At 25°C, both H⁺ and OH⁻ concentrations = 1 × 10⁻⁷ mol/L.

pH is defined as the negative logarithm of the hydrogen ion concentration:

pH = -log₁₀ [H⁺]

For pure water: pH = -log(10⁻⁷) = 7.0 (neutral)

pH	Meaning	Example
< 7	Acidic (more H⁺)	Stomach acid (pH ~1-2), lemon juice (pH ~2)
= 7	Neutral	Pure water
> 7	Alkaline/Basic (fewer H⁺)	Blood (pH 7.4), pancreatic juice (pH 8)

Why a log scale? Because H⁺ concentrations in biology range from 10⁻¹ to 10⁻¹⁴ mol/L - an enormous range. Each pH unit represents a 10-fold change in H⁺ concentration. So blood at pH 7.4 has 10 times more H⁺ than at pH 8.4.

Normal body pH values:

Arterial blood: 7.35 - 7.45
Venous blood: ~7.32
Intracellular: ~7.0-7.2
Urine: 4.5-8.0 (varies)
Gastric juice: 1.5-3.5

4. Acids and Bases

Bronsted-Lowry Definition (used in biochemistry):

Acid = a proton (H⁺) donor
Base = a proton (H⁺) acceptor

HCl → H⁺ + Cl⁻ (HCl donates H⁺ → it is an acid)

NaOH → Na⁺ + OH⁻ (OH⁻ accepts H⁺ → OH⁻ is a base)

OH⁻ + H⁺ → H₂O (neutralisation - this was on your slide!)

Strong vs. Weak Acids:

Property	Strong Acid	Weak Acid
Dissociation in water	Complete (100%)	Partial (often <10%)
Example	HCl (hydrochloric acid), H₂SO₄ (sulfuric acid)	CH₃COOH (acetic acid), H₂CO₃ (carbonic acid), lactic acid
Clinical relevance	Strong acids cause rapid acidosis	Weak acids are physiologically bufferable

Strong vs. Weak Bases:

	Strong Base	Weak Base
Example	NaOH, KOH	NH₃ (ammonia)
Dissociation	Complete	Partial

Conjugate acid-base pairs: When an acid (HA) gives up its proton, what remains (A⁻) is its conjugate base. They always come in pairs:

Acid	H⁺	Conjugate Base
H₂CO₃ (carbonic acid)	H⁺	HCO₃⁻ (bicarbonate)
H₂PO₄⁻	H⁺	HPO₄²⁻
NH₄⁺	H⁺	NH₃

5. Ka, pKa, and the Henderson-Hasselbalch Equation

For a weak acid dissociating:

HA ⇌ H⁺ + A⁻

The acid dissociation constant Ka:

Ka = [H⁺][A⁻] / [HA]

Higher Ka → stronger tendency to donate protons → stronger acid
pKa = -log(Ka) → lower pKa = stronger acid

Key rule: At pH = pKa, the acid is exactly 50% dissociated (equal amounts of HA and A⁻).

The Henderson-Hasselbalch Equation:

pH = pKa + log ([A⁻] / [HA])

For the most important clinical buffer (bicarbonate):

pH = 6.1 + log ([HCO₃⁻] / [H₂CO₃])

At normal blood pH 7.4, the ratio of HCO₃⁻ to H₂CO₃ is 20:1. This equation is what doctors use to interpret arterial blood gas (ABG) results.

6. Buffers - The Body's pH Protection System

A buffer is a mixture of a weak acid and its conjugate base. It resists large pH changes when small amounts of H⁺ or OH⁻ are added.

How it works:

Add acid (H⁺) → the conjugate base absorbs it:

A⁻ + H⁺ → HA (H⁺ is "mopped up" - pH barely changes)
Add base (OH⁻) → the weak acid donates H⁺ to neutralise it:

HA + OH⁻ → A⁻ + H₂O

Buffer effectiveness depends on:

pKa close to the target pH (a buffer works best within ±1 pH unit of its pKa)
High concentration (more buffer = greater capacity to absorb H⁺ or OH⁻)

Major body buffer systems:

Buffer	Location	pKa	How it works
Bicarbonate/Carbonic acid (HCO₃⁻/H₂CO₃)	Blood, ECF	6.1	Most important blood buffer; controlled by lungs (CO₂ expiration) and kidneys (HCO₃⁻ excretion/retention)
Phosphate (HPO₄²⁻/H₂PO₄⁻)	Cells, urine	6.8	Important inside cells and in urine
Hemoglobin (HbO₂/HbH⁺)	Red blood cells	~7.1	Absorbs H⁺ as blood passes through tissues; releases it in lungs
Plasma proteins	Blood	~6.7	Histidine residues on proteins act as buffers

Metabolic acids produced daily:

The body produces approximately 13,000-22,000 mmol of acid per day from normal metabolism:

CO₂ (from cellular respiration) → + H₂O → H₂CO₃ (carbonic acid) - the largest source
Lactic acid (from anaerobic metabolism in muscles)
Ketone bodies (acetoacetic acid, β-hydroxybutyric acid) - from fat metabolism
Sulfuric acid - from metabolism of sulfur-containing amino acids (methionine, cysteine)

How the body eliminates acid:

Lungs: Breathe out CO₂ (reduces carbonic acid)
Kidneys: Excrete H⁺ as ammonium (NH₄⁺) and in combination with phosphate

LECTURES 2 & 3 - Biomolecules

(Standard Med 1001 content based on the BAU International syllabus)

CARBOHYDRATES

Definition: Molecules of C, H, and O with the general formula (CH₂O)ₙ.

Classification by size:

Class	Units	Examples	Role
Monosaccharides	1	Glucose, fructose, galactose, ribose, deoxyribose	Direct fuel; building blocks
Disaccharides	2	Sucrose (glucose+fructose), Lactose (glucose+galactose), Maltose (glucose+glucose)	Dietary sugars
Polysaccharides	Many	Glycogen, Starch, Cellulose	Storage, structure

Glucose - The body's primary fuel:

Formula: C₆H₁₂O₆
In solution, glucose exists as a ring (pyranose form)
α-glucose and β-glucose differ only in whether the -OH group on carbon 1 points down (α) or up (β) - this tiny difference has massive consequences: starch (α-linkages) is digestible; cellulose (β-linkages) is not
Normal blood glucose: 3.9-6.1 mmol/L (70-110 mg/dL)

Glycogen:

The storage form of glucose in humans
Liver glycogen: maintains blood glucose between meals (up to ~100g)
Muscle glycogen: provides fuel for the muscle itself (up to ~400g)
Highly branched polymer of glucose via α-1,4 bonds (linear) and α-1,6 bonds (branch points)

Clinical relevance:

Diabetes mellitus - failure to regulate blood glucose
Lactose intolerance - deficiency of lactase enzyme (cannot break lactose into glucose + galactose)
Glycogen storage diseases - enzyme defects in glycogen synthesis/breakdown (e.g., Von Gierke disease)

PROTEINS AND AMINO ACIDS

Proteins are the workhorses of the cell. Functions include: enzymes (catalysts), structural support (collagen), transport (hemoglobin), hormones (insulin), antibodies, receptors, and more.

Amino Acid Structure:

Every amino acid has a central α-carbon bonded to:

An amino group (-NH₂)
A carboxyl group (-COOH)
A hydrogen atom (-H)
A variable side chain (-R) - this defines each amino acid's identity and properties

Amino acids are amphoteric - they can act as both acid and base:

At low pH (acidic): -NH₃⁺ and -COOH (both protonated)
At neutral/physiological pH: zwitterion - -NH₃⁺ and -COO⁻ (both charges present simultaneously)
At high pH (basic): -NH₂ and -COO⁻ (both deprotonated)

The 20 standard amino acids are classified by their R-group:

Non-polar/hydrophobic: Glycine, Alanine, Valine, Leucine, Isoleucine, Proline, Phenylalanine, Tryptophan, Methionine
Polar/uncharged: Serine, Threonine, Cysteine, Tyrosine, Asparagine, Glutamine
Positively charged (basic): Lysine, Arginine, Histidine
Negatively charged (acidic): Aspartate, Glutamate

Essential amino acids (cannot be made by the body, must come from diet):

Histidine, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Threonine, Tryptophan, Valine Mnemonic: "PVT TIM HaLL" (Private Tim Hall)

Peptide Bond: Amino acids are joined by peptide bonds - a covalent bond between the -COOH of one amino acid and the -NH₂ of the next, with loss of a water molecule (condensation reaction). The result is a polypeptide chain.

Four Levels of Protein Structure:

Level	Description	Stabilising Forces
Primary (1°)	The linear sequence of amino acids in the chain	Peptide bonds (covalent)
Secondary (2°)	Local regular folding: α-helix (coiled spring) and β-pleated sheet (zigzag)	Hydrogen bonds between backbone atoms
Tertiary (3°)	Overall 3D shape of the entire polypeptide	H-bonds, disulfide bridges (-S-S-), ionic bonds, hydrophobic interactions
Quaternary (4°)	Association of 2+ polypeptide chains	Same non-covalent forces; sometimes disulfide bonds

Example of quaternary structure: Hemoglobin = 2 α-chains + 2 β-chains (tetramer).

Denaturation: Loss of secondary/tertiary/quaternary structure (but primary structure = peptide sequence is intact).

Causes: heat (boiling), strong acids/bases, organic solvents, heavy metals
Example: boiling an egg white (albumin protein denatures irreversibly - turns white and solid)
Clinical note: High fever can denature enzymes, disrupting metabolism. Sterilisation uses heat to denature bacterial proteins.
Sickle cell disease: A single amino acid change in hemoglobin (glutamate → valine at position 6 of the β-chain) causes the protein to polymerise in low-oxygen conditions, distorting red blood cells into a sickle shape.

LIPIDS

Lipids are not polymers - they are a diverse group of molecules defined by their hydrophobicity (insolubility in water). They are soluble in organic solvents (chloroform, ether).

1. Fatty Acids: Long hydrocarbon chains with a -COOH group at one end.

Type	Bond structure	Physical state	Example	Where found
Saturated	No C=C double bonds	Solid at room temp	Palmitic acid (C16:0), Stearic acid (C18:0)	Animal fats, butter, coconut oil
Monounsaturated	One C=C double bond	Liquid at room temp	Oleic acid (C18:1, omega-9)	Olive oil
Polyunsaturated	Multiple C=C double bonds	Liquid at room temp	Linoleic acid (C18:2, omega-6), α-Linolenic acid (C18:3, omega-3)	Fish oil, flaxseed oil

Essential fatty acids (cannot be synthesised by humans): linoleic acid (omega-6) and α-linolenic acid (omega-3) - must come from diet.

The cis vs. trans configuration of double bonds matters clinically: natural unsaturated fats have cis double bonds; industrial hydrogenation creates trans fats which increase LDL cholesterol and cardiovascular risk.

2. Triglycerides (Triacylglycerols):

Structure: one glycerol molecule + three fatty acids joined by ester bonds
Primary form of energy storage in adipose tissue
Yield 9 kcal/g (vs. 4 kcal/g for carbohydrates and proteins) - twice as energy-dense
Mobilised by hormone-sensitive lipase when energy is needed

3. Phospholipids:

Structure: glycerol + 2 fatty acids + phosphate group + polar "head" group
Amphipathic: one end is hydrophilic (polar head), the other is hydrophobic (fatty acid tails)
This dual nature drives the formation of the cell membrane lipid bilayer:
- In water, phospholipids spontaneously arrange so tails face inward (away from water) and heads face outward
Most important example: Phosphatidylcholine (lecithin)
Sphingomyelin (a sphingophospholipid) is a major component of the myelin sheath of neurons

4. Cholesterol:

A sterol - has a characteristic 4-ring (steroid) structure
An essential component of all animal cell membranes:
- At high temperatures: reduces membrane fluidity (keeps it from melting)
- At low temperatures: prevents packing (keeps it from solidifying)
- This is called membrane fluidity regulation
Precursor of:
- Steroid hormones: cortisol, aldosterone, testosterone, estrogen, progesterone
- Bile acids: needed for fat digestion in the small intestine
- Vitamin D: made in skin upon UV light exposure
Clinical note: Statins (e.g., atorvastatin, simvastatin) block HMG-CoA reductase (the rate-limiting enzyme of cholesterol synthesis in the liver), reducing LDL cholesterol and cardiovascular risk.

NUCLEIC ACIDS

Nucleic acids carry, store, and transmit the genetic information needed to build and maintain every cell.

The building block: Nucleotide

Each nucleotide has three components:

A pentose sugar (5-carbon ring):
- DNA → 2'-deoxyribose (no -OH at carbon 2)
- RNA → ribose (has -OH at carbon 2)
A nitrogenous base:
- Purines (double-ring): Adenine (A), Guanine (G) - in both DNA and RNA
- Pyrimidines (single-ring): Cytosine (C) - in both; Thymine (T) - DNA only; Uracil (U) - RNA only
- Memory trick: PURe As Gold (Purines = Adenine + Guanine)
Phosphate group(s)

From nucleoside to nucleotide:

Nucleoside = sugar + base (no phosphate)
Nucleotide = sugar + base + 1-3 phosphate groups
ATP = adenosine triphosphate → the cell's energy currency

DNA Structure (Watson-Crick double helix):

Two anti-parallel polynucleotide strands wound around each other in a right-handed helix
The sugar-phosphate backbone is on the outside (hydrophilic, faces water)
The bases are on the inside, paired via hydrogen bonds:
- A pairs with T: 2 hydrogen bonds (A=T)
- G pairs with C: 3 hydrogen bonds (G≡C) - stronger
The two strands are antiparallel: one runs 5'→3', the other 3'→5'
Chargaff's Rule: In any DNA molecule, %A = %T and %G = %C

RNA - Types and Functions:

Type	Name	Function
mRNA	Messenger RNA	Carries the genetic code (codons) from the nucleus to ribosomes
rRNA	Ribosomal RNA	Structural and catalytic component of ribosomes (the translation machinery)
tRNA	Transfer RNA	Cloverleaf-shaped; carries specific amino acids to the ribosome; matches codon to anticodon

The Central Dogma of Molecular Biology:

DNA → (Transcription) → mRNA → (Translation) → Protein

Replication: DNA → DNA (before cell division; each strand serves as a template)
Transcription: DNA → mRNA (in the nucleus; only one strand is the template)
Translation: mRNA → Protein (at the ribosome; codons specify amino acids)

The Genetic Code:

Each codon = 3 consecutive nucleotide bases on mRNA = codes for one amino acid
There are 4³ = 64 possible codons for 20 amino acids - the code is redundant (multiple codons can code for the same amino acid)
Start codon: AUG (codes for methionine; signals start of translation)
Stop codons: UAA, UAG, UGA (signal end of translation - no amino acid added)

ATP as the energy molecule:

ATP has three phosphate groups in sequence. Breaking the bond between the 2nd and 3rd phosphate releases ~7.3 kcal/mol:

ATP + H₂O → ADP + Pᵢ + energy
This energy drives virtually all cellular processes: muscle contraction, ion pumping, protein synthesis, etc.

KEY CLINICAL CONNECTIONS

Lecture Topic	Clinical Application
pH and buffers	Arterial blood gas (ABG) interpretation; managing metabolic acidosis in DKA
Body water compartments	IV fluid selection (normal saline vs. Ringer's vs. 5% dextrose)
Protein denaturation	Fever causing enzyme dysfunction; sterilisation; burn injuries
Amino acids	Sickle cell disease (valine for glutamate in HbS); phenylketonuria (deficient phenylalanine metabolism)
Cholesterol metabolism	Statins for hypercholesterolaemia; bile acid for fat-soluble vitamin absorption
Phospholipids	Respiratory distress syndrome in premature infants (deficient surfactant = phospholipid)
DNA replication	Cancer (uncontrolled replication); chemotherapy drugs target DNA synthesis
Nucleotide metabolism	Gout (uric acid = purine breakdown product); Allopurinol blocks xanthine oxidase
Glycogen	Hypoglycaemia in fasting; glycogen storage diseases (Von Gierke, Pompe, McArdle)

QUICK-REFERENCE FORMULAS

Formula	Meaning
pH = -log[H⁺]	Definition of pH
pH = pKa + log([A⁻]/[HA])	Henderson-Hasselbalch equation
Ka = [H⁺][A⁻]/[HA]	Acid dissociation constant
pKa = -log(Ka)	Negative log of Ka
Normal blood pH: 7.35-7.45	Acidosis <7.35; Alkalosis >7.45
ATP hydrolysis: ~7.3 kcal/mol	Energy released per mole of ATP

Sources: Basic Medical Biochemistry: A Clinical Approach, 6th edition (Marks et al.), p. 81-93; BAU International University Med 1001 Course Syllabus; Lecture 1 slide content (MS Elene Bezhanidze).

Since Lectures 2 and 3 could not be read from your files (image-only slides), if you share what topics they specifically cover, I can provide targeted deep explanations. Reply with "continue" if you'd like me to expand any section further or go into more detail on a specific topic.

This is a shared conversation. Sign in to Orris to start your own chat.