Questions tagged [protein-structure]
The 3-dimensional organisation of amino acids in a protein, specifically including the secondary, tertiary and quaternary structures.
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Using BLAST for molecular replacement in structural biology
This is my first time trying to do molecular replacement to solve a protein structure. I am using the NCBI blastp program to find suitable search models. When choosing a search model, I understand ...
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2answers
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How can predicting protein folding speed up drug discovery?
I'm asking this as a layperson without much knowledge in biology, so please correct me if my understanding is wrong.
Recently DeepMind's AlphaFold managed to predict protein structure from acid amino ...
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Why did the protein structure prediction accuracy in terms of GDT-TS decrease from 2008 (CASP 8) to 2014 (CASP 11)?
I read on https://doi.org/10.1038/d41586-020-03348-4:
Why did the protein structure prediction accuracy in terms of GDT-TS (Global Distance Test — Total Score) decrease from 2008 (CASP 8) to 2014 (...
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Why are Ramachandran angles of first and the last amino acid not necessary to define the full 3D structure of a protein chain?
I have come across an online ppt slide of the bioinformatic algorithm where it is said that first and the last amino acid Ramachandran angle is not necessary to tell all its internal coordinates. Is ...
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33 views
Generating Cartesian coordinates of each atom in protein chain from the internal coordinates using python or some software
I am trying to compute Cartesian coordinates of backbone atoms and side-chain atoms (C beta alone) for a given set of internal coordinates (bond lengths, bond angles and dihedral angles) I have ...
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49 views
Why does sequencing virus proteins take time?
According to the below paper, the coronavirus spike protein sequence was available to scientists by end of february 2020 - the begin of march 2020 timeline. I had this question that why does ...
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2answers
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Why do large, aromatic residues prefer beta-pleated sheets?
I read in many journals that amino acids with branched and large aromatic R-groups have higher beta pleated sheet propensities. However, none really go in depth into the significance or reasoning ...
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Which condition is most likely to cause a buildup of materials in the lysosome?
Stated below, I must answer a question related to lysosomes. I am unsure of the answer, and have explained my reasoning after the question.
Lysosomes contain hydrolytic enzymes that derive from the ...
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1answer
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Questions about Cohesin - what does the ATPase domain do, and any suggested PDBs to look at?
I've been reading about cohesin lately, and I'm confused about the head subunit interactions. I've read a few papers, and also found this nice figure from wiki that demonstrates the crux of my ...
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1answer
40 views
Determine similarity in percentages between species A and B, A and C, and B and C
The chart above is a graphic that shows the amino acid sequence differences between different organisms for a protein keratin.
The question I am required to answer begins as, "Keratin is made up ...
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Why is protein cyclisation desirable?
There are a number of methods to "cyclize" an existing peptide:
Disulphide bond as described in Disulfide Bond Mimetics: Strategies and Challenges by Gori et al.
"Linchpin" based (...
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What programs account for structural alignment of different parts of distant homologs which have significant structural differences?
If there is a need to align structurally different parts of distant homologs, which program one should use?
Since distant homologs often have significant structural changes, does that means the ...
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What's superposition and thread in RosettaCM?
I'm a beginner in structural biology.
I had a question while reading a paper on RosettaCM.
What does RosettaCM's superposition and thread mean?
I googled it.
As a result, the following results were ...
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2answers
99 views
Why are some protein sequences known but their 3D structure isn't?
Why are there some proteins that have a known amino acid sequence, but their 3D structure is not known? Wouldn't finding the former in a lab lead to the discovery of the latter? Please correct me if I ...
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What is a Protein contact map, and how do I read one?
Protein contact maps are symmetrical and look great, but how does one read one?
I tried to underside the following source: 'Understanding contact patterns of protein structures from protein contact ...
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Any kind of online “molecular modeling playground”?
I'm wondering if anyone has ever made a tool to try out new molecular modeling/simulation algorithms, where the tool itself handles the "boring" tasks of loading PDB files, building chains ...
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How to build SEG in your personal environment?
I'm trying to implement SEG (Wootton & Federhen,1993) in my MATLAB and Python environment. From this oriinal article I cannot figure out what I need to build my script. Are there any related ...
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Protein structure prediction from amino acids sequence
Information given at this resource https://predictioncenter.org/ is close to impossible to digest (as with everything in this field), so if anyone could tell me what is the accuracy we can predict ...
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2answers
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How do you biologists draw a protein when you write a paper?
The following is one example of protein structure diagram that I want to put in my research paper. I took this from
Koniev, O. & Wagner, A. “Developments and recent advancements in the field of ...
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39 views
Why does insertion of transmembrane domains occur in the rough ER?
To elaborate on that question, why in the secretory pathway does the insertion of transmembrane domains into the membrane occur in the rough ER as the protein is translated and threaded across the ER ...
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31 views
What are good techniques for determining direct maps of proteins?
I am looking for which techniques to explore to determine electron density maps (or Fourier maps) for a protein (possibly using an assumed model).
In particular, I want to avoid techniques that ...
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1answer
69 views
Can the knowledge about torsion angles alone be sufficient for specifying secondary structures of protein?
I have read that Ramachandran plots are used to identify secondary structures of proteins. Also, alpha helices and beta strands cluster around specific regions of the plot which gives us the ...
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Glucose 6-phosphate dehydrogenase: reaction mechanism
I have searched the internet for the reaction mechanism of G6PD but couldn't find it, so I am asking whether anyone here knows its mechanism and whether they could recommend some sources that give ...
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1answer
52 views
Why does the structure for cellular retinol binding protein show interactions with cadmium ions?
A structure of cellular retinol binding protein (1CRB) contains two cadmium ions as ligands. Is Cd2+ a ligand of CRBP and, if so, is that interaction necessary for protein function or is the protein a ...
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1answer
52 views
Formation of disulfide bonds in protein expressed after transduction
Say I transduce a nucleic acid sequence using a viral vector that encodes a protein having at least one disulfide linkage. For simplicity, let’s assume that there are only two cysteines in the protein ...
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Estimating diffusion constant of a protein based on number of amino acids
Is there a way to estimate the diffusion constant of a protein based on the number of amino acids it is comprised of. I know that the shape of the protein has an influence on the diffusion constant, ...
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2answers
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Can 1.5 gigabytes encoded in the human genome really account for the complexity of a human being?
I read the human genome is 1.5 gigabytes in size. Thats actually not a lot; Photoshop probably takes more space. Mac OS takes 10+ gigabytes of space. Also, the genome is 1.5 gigabytes when counting ...
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What is the native structure of amyloid-beta protein under physiological conditions?
The amyloid-beta protein forms cross-beta structured fibrils. But under normal physiological conditions what is their predominant secondary structure. Is it alpha-helix, random coil or beta-sheet?
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Software to model and analyse protein–ligand interactions
I am currently trying to model a certain protein (Golgi Mannosidase II) and compare the induced fit of the inhibitor swainsonine. I would like to be able to analyse the distances between bonding ...
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1answer
81 views
Is the chitin in an insect's exoskeleton cross-linked?
This answer to the question How to clean and preserve a cicada's molted exoskeleton (exuvia)? states:
The exuvia is made of cross-liked chitin, and will not decay. You don't need any special ...
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1answer
60 views
Can denatured GFP show fluorescence?
GFP ( green fluorescent protein) can show green fluorescence. And its fluorescence is due to the tri peptide chromophore which is given in below I was wondering, can we observe fluorescence, if we ...
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3answers
207 views
Why does it matter to predict protein structure?
And how do you predict it ? What is your input data (sequence of amino acids, temperature, pH, ...) ? Is there a "standardized" input that scientists agree on ?
Moreover, I've read that knowing the ...
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Protein structure prediction using PSSM? Or not?
I have been studying protein structure prediction algorithms. A lot of recent work uses something called the PSSM, the position-specific scoring matrix.
I think that what a PSSM does is to build a 2-...
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conversion of distance matrices to pdb/coordinates
I am currently facing two transformational issues. Suppose I am given a protein's residue sequence and calpha distance matrix; is there a way to generate the 3d coordinates of the protein's residues ...
3
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1answer
73 views
Emergence of novel protein interactions by mutation of amino acids
Are there any examples of proteins that, without coming from a recent duplication event, underwent a mutation(s) that caused it to have a novel interaction with a new ligand, substrate, other protein ...
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Where can I find and download HMMTOP training set?
I would like to perform redundancy reduction for my test set for membrane topology prediction. I checked the 1998 paper and website of the HMMTOP server but haven't found any download links for the ...
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1answer
114 views
Backbone hydrogen bonds between adjacent amino acids in a protein?
Is it possible for two adjacent amino acids in a peptide to form hydrogen bonds between the backbone NH and CO?
Are there any examples of such situations in proteins and how common are they?
If ...
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TBX3 Protein structure and function
Is it possible for an anti-cancer monoclonal antibody to target the two repressor domains in the N and C terminal of the TBX3 protein ?
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1answer
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Difference between prions and amyloid proteins?
Amyloid and prions are misfolded proteins, but what, if any, is the difference between them?
Is amyloid a type of prion with a fibrillar structure?
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1answer
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Obtaining protein atomic co-ordinates from dihedral angles
https://en.wikipedia.org/wiki/Dihedral_angle#/media/File:Protein_backbone_PhiPsiOmega_drawing.svg
I've been reading on Protein Amino Acid Sequences and their 3D structure. It seems that the 3D ...
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1answer
597 views
What are the different types of helices in protein secondary structures and how do they differ?
What are the different types of helices in protein secondary structures and how are they differentiated?
In the DSSP docs, types of helices mentioned are: Alpha-Helix, Helix-3, and Helix-5.
In the ...
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Quantify Protein Denaturation with Change in Solubility
I plan to run a lab which compares the impacts of ethanol and methanol, in varying concentrations, on the denaturation of whey protein.
Change in water solubility is a good indicator of the degree ...
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Are there any enzymes without aromatic amino acids?
I'd like to try a new spectroscopic technique to study enzymatic reactions (which reaction doesn't especially matter, something simple and with fast kinetics like catalase would do fine - I'm just ...
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2answers
122 views
When does protein folding begin?
I had always assumed that protein folding is an independent activity that occurs after translation is complete. However, recently, I learned that intermolecular forces begin shaping the peptide bonds ...
3
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1answer
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Is there a reason for the lack of full RTK structures?
Bocharov et al. (2013) write that
As there are no structures of full-length RTKs [receptor tyrosine kinases], we do not fully understand how different domains function together to mediate signal ...
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1answer
67 views
What is the length and number of the parts of a conformational epitope?
I am interested in the question whether exposure to protein A might create antibodies that also bind to protein B.
I am wondering whether, if the antigen of protein A is a conformational epitope, it ...
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1answer
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How similar do proteins have to be to trigger the same immune response?
The title really says it all. How precise or vague is the immunity we get from vaccination or from having encountered a germ before?
Is it about protein parts that are recognised if they are ...
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1answer
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Homology modelling of protein with two identical subunits in its quaternary structure
I am using homology modelling to assign the 3D structure of Torpedo acetylcholine receptor (Unwin 2004, 2bg9 in RCSB) to human muscle nAChR. The problem is, both Torpedo receptor, and human receptor ...
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1answer
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Is α-keratin a fully functional protein?
Is α-keratin before it coils with another polypeptide, makes chains, and build intermediate filaments a fully functional protein?
I mean, is the single monomer of α-keratin a protein or does it have ...
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Why are the first and last amino acids of an alpha helix not hydrogen bonded?
I am studying protein structures and in alpha helix I found out that one amino acid residue's carbonyl oxygen is linked to the nitrogen of amino group of 4 residues ahead.. However the first and last ...