Question from NMRWiki Q&A forum !3C NMR of Peptide

		BioNMR > NMR community > News from other NMR forums
[Question from NMRWiki Q&A forum] !3C NMR of Peptide

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

Thread Tools

Search this Thread

Rate Thread

Display Modes

06-11-2013, 09:33 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,732

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

!3C NMR of Peptide

!3C NMR of Peptide

Hi, thank you for reading my question. I am a novice at NMR, I apologize in advance if my question appears naive. I am synthesizing peptides composed solely of Lys and Leu residues in either a block or random orientation. To demonstrate the orientation, I am proposing to use 13C NMR. My expectation is the block orientation will demonstrate higher intensity carbonyl peaks for Lys-Lys and Leu-Leu than Lys-Leu whereas the random peptide will show a higher intensity peak for the Lys-Leu. Does this sound reasonable or does anyone have any other suggestions?

Check if somebody has answered this question on NMRWiki QA forum

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
NMR for a 30-residue peptide Dear all, Is that possible to do structure determination of a 30-residue peptide using 500 MHz NMR? I have a 30-residue linear peptide with three Gly and two AHx (aminohexanoic acid) groups at the center of the peptide. I read some papers from people who use 500 MHz NMR to determine the structure of up to 20-residue peptides, but not a 30-residue peptide.	bimo	NMR Questions and Answers	5	03-06-2013 12:35 AM
[CNS Yahoo group] Re: peptide bond cut during annealing Re: peptide bond cut during annealing Hi Nic, thanks a lot! This was the solution as you suggested: I forgot to add the new residue into the link file to be patched with PEPT. SInce the involved More...	nmrlearner	News from other NMR forums	0	03-05-2012 04:29 PM
[CNS Yahoo group] Re: peptide bond cut during annealing Re: peptide bond cut during annealing Yes. I have had this happen when I had to create a novel amino acid (oxidized cysteine) and didn't set it up to 'link' with the normal amino acids. More...	nmrlearner	News from other NMR forums	0	03-05-2012 04:29 PM
[CNS Yahoo group] peptide bond cut during annealing peptide bond cut during annealing Dear All, I was generated topologies/parameters for a new residue in a peptide. The generate.inp created a correct peptide bond from the new residue to the More...	nmrlearner	News from other NMR forums	0	03-05-2012 04:04 AM
[CNS Yahoo group] Re: peptide bond cut during annealing Re: peptide bond cut during annealing Most likely, there is some error in topology. Please post your topology/parameter/link files for the unconventional residue. More...	nmrlearner	News from other NMR forums	0	03-05-2012 04:04 AM
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions. Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions. Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions. Chem Biol Drug Des. 2011 Feb 5; Authors: Gizachew D, Dratz E Protein-protein interactions control signaling, specific adhesion and many other biological functions. The three dimensional structures of the interfaces and bound ligand can be...	nmrlearner	Journal club	0	02-08-2011 06:28 PM
[Question from NMRWiki Q&A forum] peptide protein interaction peptide protein interaction I have determined the structure of a 110 residues protein(11kDa) which is known to interact with a 15mer peptide. Now I am interested to know which residues of the 15mer peptide interacts with this 11kDa protein. Can anyone suggest a simple nmr experiment which can tell the residues from the 15mer peptide which interact with the protein. Check if somebody has answered this question on NMRWiki QA forum	nmrlearner	News from other NMR forums	0	02-01-2011 06:40 PM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off