The document discusses the structure and functions of proteins, including their primary, secondary, tertiary, and quaternary structure. It describes different protein domains like alpha helices and beta sheets, and how proteins fold into their lowest energy confirmation through interactions between polar and nonpolar amino acids. The summary also examines how molecular chaperones can help proteins fold and how disulfide bonds can stabilize proteins structures.
I shikha popali and my colleague harshpal singh wahi presents a presentation "RECENT DEVELOPMENT IN DRUG DESIGN AND DISCOVERY " A detail account on protein structure is given
I shikha popali and my colleague harshpal singh wahi presents a presentation "RECENT DEVELOPMENT IN DRUG DESIGN AND DISCOVERY " A detail account on protein structure is given
Protein structures, Detail about protein dystrophin DMD and BMD primary structures, secondary structures, tertiary structures, Quaternary structures, functions of proteins ,
different sub types of protein structures, dystropins proteins structures , locations of it in chromosomes, chromosomal abnormalities, facts of Duchenne Muscular Dystrophy
In this pdf amino acid and protein classification is given in excellent manner.
Amino acids are molecules that combine to form proteins. Amino acids and proteins are the building blocks of life.When proteins are digested or broken down, amino acids are left. The human body uses amino acids to make proteins to help the body:Break down food,Grow,Repair body tissue,Perform many other body functions.Amino acids can also be used as a source of energy by the body.
Amino acids are classified into three groups:
Essential amino acids
Nonessential amino acids....
Function and Classification of protein given in this pdf .
Structure of proteins given in this pdf with different types of interaction between amino acids like hydrogen bonding , intermolecular and intramolecular bondings. Also structure of protein given in primary, secondary, tertiary and quarternary forms.
Physicochemical properties of protein also given in this pdf.
Amino acisd structure
Peptide bond formation
Analysis of protein Structure- X-ray Crystallography
Different structural levels of proteins with examples.
Importance of protein structure
Creutzfeldt-Jacob-Disease due to changes in normal protein conformation.
Protein structures, Detail about protein dystrophin DMD and BMD primary structures, secondary structures, tertiary structures, Quaternary structures, functions of proteins ,
different sub types of protein structures, dystropins proteins structures , locations of it in chromosomes, chromosomal abnormalities, facts of Duchenne Muscular Dystrophy
In this pdf amino acid and protein classification is given in excellent manner.
Amino acids are molecules that combine to form proteins. Amino acids and proteins are the building blocks of life.When proteins are digested or broken down, amino acids are left. The human body uses amino acids to make proteins to help the body:Break down food,Grow,Repair body tissue,Perform many other body functions.Amino acids can also be used as a source of energy by the body.
Amino acids are classified into three groups:
Essential amino acids
Nonessential amino acids....
Function and Classification of protein given in this pdf .
Structure of proteins given in this pdf with different types of interaction between amino acids like hydrogen bonding , intermolecular and intramolecular bondings. Also structure of protein given in primary, secondary, tertiary and quarternary forms.
Physicochemical properties of protein also given in this pdf.
Amino acisd structure
Peptide bond formation
Analysis of protein Structure- X-ray Crystallography
Different structural levels of proteins with examples.
Importance of protein structure
Creutzfeldt-Jacob-Disease due to changes in normal protein conformation.
Multi-source connectivity as the driver of solar wind variability in the heli...Sérgio Sacani
The ambient solar wind that flls the heliosphere originates from multiple
sources in the solar corona and is highly structured. It is often described
as high-speed, relatively homogeneous, plasma streams from coronal
holes and slow-speed, highly variable, streams whose source regions are
under debate. A key goal of ESA/NASA’s Solar Orbiter mission is to identify
solar wind sources and understand what drives the complexity seen in the
heliosphere. By combining magnetic feld modelling and spectroscopic
techniques with high-resolution observations and measurements, we show
that the solar wind variability detected in situ by Solar Orbiter in March
2022 is driven by spatio-temporal changes in the magnetic connectivity to
multiple sources in the solar atmosphere. The magnetic feld footpoints
connected to the spacecraft moved from the boundaries of a coronal hole
to one active region (12961) and then across to another region (12957). This
is refected in the in situ measurements, which show the transition from fast
to highly Alfvénic then to slow solar wind that is disrupted by the arrival of
a coronal mass ejection. Our results describe solar wind variability at 0.5 au
but are applicable to near-Earth observatories.
This pdf is about the Schizophrenia.
For more details visit on YouTube; @SELF-EXPLANATORY;
https://www.youtube.com/channel/UCAiarMZDNhe1A3Rnpr_WkzA/videos
Thanks...!
Richard's aventures in two entangled wonderlandsRichard Gill
Since the loophole-free Bell experiments of 2020 and the Nobel prizes in physics of 2022, critics of Bell's work have retreated to the fortress of super-determinism. Now, super-determinism is a derogatory word - it just means "determinism". Palmer, Hance and Hossenfelder argue that quantum mechanics and determinism are not incompatible, using a sophisticated mathematical construction based on a subtle thinning of allowed states and measurements in quantum mechanics, such that what is left appears to make Bell's argument fail, without altering the empirical predictions of quantum mechanics. I think however that it is a smoke screen, and the slogan "lost in math" comes to my mind. I will discuss some other recent disproofs of Bell's theorem using the language of causality based on causal graphs. Causal thinking is also central to law and justice. I will mention surprising connections to my work on serial killer nurse cases, in particular the Dutch case of Lucia de Berk and the current UK case of Lucy Letby.
A brief information about the SCOP protein database used in bioinformatics.
The Structural Classification of Proteins (SCOP) database is a comprehensive and authoritative resource for the structural and evolutionary relationships of proteins. It provides a detailed and curated classification of protein structures, grouping them into families, superfamilies, and folds based on their structural and sequence similarities.
Richard's entangled aventures in wonderlandRichard Gill
Since the loophole-free Bell experiments of 2020 and the Nobel prizes in physics of 2022, critics of Bell's work have retreated to the fortress of super-determinism. Now, super-determinism is a derogatory word - it just means "determinism". Palmer, Hance and Hossenfelder argue that quantum mechanics and determinism are not incompatible, using a sophisticated mathematical construction based on a subtle thinning of allowed states and measurements in quantum mechanics, such that what is left appears to make Bell's argument fail, without altering the empirical predictions of quantum mechanics. I think however that it is a smoke screen, and the slogan "lost in math" comes to my mind. I will discuss some other recent disproofs of Bell's theorem using the language of causality based on causal graphs. Causal thinking is also central to law and justice. I will mention surprising connections to my work on serial killer nurse cases, in particular the Dutch case of Lucia de Berk and the current UK case of Lucy Letby.
2. SHAPE AND
STRUCTURE OF
PROTEINS
MODULE 1: LESSON 1 OF 3
BIOL6299 Fall 2022
Northeastern University
(Source: Bruce Alberts; Alexander Johnson; Julian Lewis; David Morgan; Martin Raff; Keith Roberts; Peter Walter: 6th Edition)
3. INTRODUCTION
• In this lesson we consider how the location of amino acids that form a specific
protein can determine its shape and structural characteristics in the cell.
• By the end of this lesson, you should be able to:
• Identify common protein structures and domains.
• Classify specific examples of important proteins and their cellular roles.
4. MODULE 1
– LESSON 1
OF 3
• Role of Proteins
• Major components of Proteins
• The Genetic Code
• Amino acid side chains
Protein Overview
• Primary, Secondary, Tertiary and Quaternary
Structure of Proteins
• Protein Domains
• Protein Folding
• Disulfide bonds in Protein folding
Common Protein Structure and Domains
6. THE ROLE
OF
PROTEINS
Proteins serve as the building blocks of
cells and execute virtually all the cells
functions, like import and export of
signals or small molecules.
Proteins that carry the functions by which
they conduct many of the necessary
chemical reactions to drive cellular
processes are referred to as enzymes.
7. THE MAJOR
COMPONENTS OF
PROTEINS
• A protein molecule is made from a long
chain of amino acids, that is joined to its
neighbor molecule via covalent bond.
• Each protein differs in its sequence and
number of amino acids; therefore, it is the
sequence of the chemically different side
chains that make each protein distinct.
• The function of a protein is dependent upon
its structure, which is determined by the
sequence of amino acids that make the
protein.
8. THE MAJOR
COMPONENTS OF
PROTEINS
• The two ends of a polypeptide chain
are chemically different: one end
carries the amino group (NH3+) known
as the amino terminus, or N-terminus,
and the other end carries the carboxyl
group (COO-/COOH) known as the
carboxyl terminus or C-terminus.
• The amino acids sequence of a protein
is always presented in the N-to-C
terminus direction and is read from left
to right.
9. THE GENETIC
CODE
• There are 20 amino acids found in
proteins.
• Each amino acid has a 3 letter code
that corresponds to the nucleic acid
sequence in mRNA, summarized in the
figure.
• The genetic code can be read by
navigating from the left to right.
• For e.g., First letter, Second letter, and
the Third letter.
• E.g.; let’s decode the codon CAU.
v Genetic code is redundant.
10. POLARITY OF AMINO
ACID SIDE CHAINS
• There are equal number of polar
and nonpolar side chains of amino
acids; however, some side chains
listed in this table as polar are large
enough to have some nonpolar
properties (for e.g., Try, Thr, Arg,
Lys).
• The polarity of the amino acid side
chains that make up the polypeptide
is an essential determinant of the
final structure of protein.
11. POLARITY OF
AMINO ACID SIDE
CHAINS
BASIC AMINO ACIDS
CONTAIN SIDE
CHAINS THAT CAN
GAIN A PROTON.
12. POLARITY OF
AMINO ACID SIDE
CHAINS
ACIDIC AMINO ACIDS
CONTAIN SIDE
CHAINS THAT CAN
LOSE A PROTON.
13. UNCHARGED AMINO ACIDS CONTAIN SIDE
CHAINS THAT HAVE NO CHARGE BUT HAVE
POLAR CHARACTERISTICS AT NEUTRAL PH
(FORM HYDROGEN BONDS WITH WATER).
POLARITY OF AMINO
ACID SIDE CHAINS
14. POLARITY OF AMINO ACID
SIDE CHAINS
NON-POLAR AMINO
ACIDS CONTAIN SIDE
CHAINS THAT ARE
HYDROPHOBIC AND
CAN CONTAIN RING-
LIKE STRUCTURES.
17. ALPHA
HELICES
Formed by backbone interactions parallel to
the primary axis of helix.
It is stabilized by hydrogen bonds between
amide hydrogen of one amino acid and
carbonyl oxygen four aminos acids away.
18. COILING FEATURES OF ALPHA
HELICES – COILED-COIL
E.g.: Alpha- Keratin
Collagen
Elastin
19. BETA SHEETS
e.g: Fibronin
Anti-parallel:
folds back and forth on itself
Parallel:
neighboring polypeptide
chains, run in same orientation
Formed by hydrogen binding between adjacent parallel or anti-parallel peptide strands.
In β-sheets, the backbone N–H and C=O of one strand hydrogen bond with
the C=O and N–H of an adjacent strand, respectively.
20. ROLE OF PROTEIN DOMAINS
*** A domain typically consists of between
40 and 350 amino acids, each with
different functions.
22. IMPORTANCE OF PROTEIN FOLDING
• An important feature governing the folding of any protein is the distribution of its
polar and nonpolar amino acids.
• The nonpolar amino acid side chains
are hidden inside of the protein to form
a tightly packed hydrophobic core of
atoms that are protected from water
that surrounds the cell.
• The polar amino acid side chains tend
to gather on the outside of the protein,
where they can interact with water and
other polar molecules in the cell’s
environment.
23. PROTEINS FOLD INTO THE LOWEST ENERGY
CONFIRMATION
***MOLECULAR CHAPERONS: Conversely, many proteins use special helper proteins to aid in protein folding.
These molecular chaperons are often necessary to prevent aggregation of proteins that
have temporarily exposed hydrophobic regions, especially in newly synthesized proteins.
26. IN THIS LESSON
• Identified the common protein structures and domains
• Classified specific examples of important proteins and their cellular roles.