Exchange behavior of the H-bonded amide protons in the 3 to 13 helix of ribonuclease S (Q70165186)

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9 October 2019

title

Exchange behavior of the H-bonded amide protons in the 3 to 13 helix of ribonuclease S (English)

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9 October 2019

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24 September 2023

amides

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24 September 2023

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24 September 2023

author name string

K. Kuwajima

series ordinal

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A6312052

24 September 2023

R. L. Baldwin

series ordinal

2

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24 September 2023

language of work or name

English

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National Center for Biotechnology Information

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24 September 2023

publication date

1 September 1983

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9 October 2019

5 September 1983

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National Center for Biotechnology Information

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full work available at URL

24 September 2023

https://api.elsevier.com/content/article/PII:S0022283683801855?httpAccept=text/xml

1 reference

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https://api.elsevier.com/content/article/PII:S0022283683801855?httpAccept=text/plain

24 September 2023

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Journal of Molecular Biology

24 September 2023

published in

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9 October 2019

volume

169

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9 October 2019

issue

1

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9 October 2019

page(s)

299-323

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Nuclear magnetic resonance studies of the unfolding of pancreatic ribonuclease. II. Unfolding by urea and guanidine hydrochloride

9 October 2019

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Nuclear magnetic resonance evidence for a structural intermediate at an early stage in the refolding of ribonuclease A

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Individual assignments of amide proton resonances in the proton NMR spectrum of the basic pancreatic trypsin inhibitor

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Structural intermediates trapped during the folding of ribonuclease A by amide proton exchange

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A competing salt-bridge suppresses helix formation by the isolated C-peptide carboxylate of ribonuclease A

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Protein dynamics investigated by the neutron diffraction-hydrogen exchange technique.

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Nature and locations of the most slowly exchanging peptide NH protons in residues 1 to 19 of ribonuclease S

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Strategy for trapping intermediates in the folding of ribonuclease and for using 1H-nmr to determine their structures

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The Aromatic Residues of Bovine Pancreatic Ribonuclease Studied by 1H Nuclear Magnetic Resonance

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A new approach to the determination of pKa's of histidine residues in proteins

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A Fourier transform NMR study of the thermal denaturation of ribonuclease A at low pH

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Nmr analysis of structure and function of snake neurotoxins

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Primary structure effects on peptide group hydrogen exchange.

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Reassignment of the active site histidines in ribonuclease A by selective deuteration studies

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Detection of an early intermediate in the folding of ribonuclease A by protection of amide protons against exchange

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Concentration-dependent hydrogen exchange kinetics of 3H-labeled S-peptide in ribonuclease S

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Mechanism of dissociation of S-peptide from ribonuclease S

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Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance

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Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance

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Identifiers

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9 October 2019

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